RU2772730C2 - Bioactive polypeptides for improving protection, growth and productivity of plant - Google Patents

Abstract

FIELD: biochemistry.

SUBSTANCE: invention relates to the field of biochemistry, in particular to polypeptide for bioactive plant priming. A recombinant microorganism expressing the specified polypeptide; a composition containing the specified polypeptide are also disclosed. Use of the specified polypeptide, composition and recombinant microorganism; a method for bioactive plant priming using the specified polypeptide, and a method for producing fused protein in a bacterial culture are disclosed.

EFFECT: invention allows for the effective increase in bioactive plant priming.

31 cl, 16 dwg, 100 tbl, 57 ex

Description

CROSS-REFERENCE TO RELATED APPLICATIONS

[0001] This application claims priority over U.S. Provisional Application No. 62/534,710, filed July 20, 2017, the contents of which are hereby incorporated by reference in their entirety.

FIELD OF TECHNOLOGY

[0002] Bioactive primer polypeptides are provided that can be delivered in agricultural formulations. These polypeptides can be used to achieve agronomically desirable plant crop outcomes, such as improved plant phenotypes (eg showing protection against pests, pathogens and abiotic stress), improved plant growth, productivity and yield.

BACKGROUND OF THE INVENTION

[0003] Conventional methods for achieving desired agronomic phenotypes, such as increased yield, disease prevention, disease resistance, and improved abiotic stress tolerance, have previously relied primarily on selective breeding, grafting, transgenic approaches, and agrochemical approaches.

Bioactive priming polypeptides involved in defense responses in plants

[0004] Plants have an immune system that detects microbes capable of causing disease and protects against them. Antimicrobial peptides (AMPs) in plants typically represent the first line of defense against pathogen invasion and are involved in the initiation of defense responses that may confer plant innate immunity. Many PMPs are characterized by general activity against various types of infectious agents. They are usually classified as antibacterial, fungicidal, antiviral and/or antiparasitic.

[0005] The resistance of certain plant species to certain pathogenic organisms that can contact the surface of the plant and colonize it is based on highly specialized systems for recognizing molecules produced only by certain microbes (for example, specific strains of bacteria or fungi). Plants sense the presence of potential invasive microbes by using pattern recognition receptors (RRPs) to recognize their associated pathogen-associated molecular patterns (PAMPs).

Flagellin/Flagellin-Associated Polypeptides

[0006] Flagellins and flagellin-associated polypeptides derived from these flagellins have been reported to primarily play functional roles in innate immune responses in plants. These polypeptides are derived from highly conserved domains of eubacterian flagellin. Flagellin is the main building block of the bacterial flagellum. The flagellin protein subunit, which forms the filament of the bacterial flagellum, can act as a potent elicitor in cells, inducing defense responses in various plant species.

[0007] "Flagellin" is a globular protein that self-assembles into a hollow cylinder to form a filament in the bacterial flagellum. Flagellin is the main component of the bacterial flagellum present in flagellar bacteria. Plants can sense presence, fight infection, and provide protection against bacterial microbes by recognizing conserved epitopes such as the 22 amino acid long stretch (Flg22) located at the N-terminus of the full-length flagellin coding sequence. The elicitor activity of the Flg22 polypeptide is attributed to the specified conserved domain in the N-terminus of the flagellin protein (Felix et al., 1999). Plants can perceive bacterial flagellin through a pattern recognition receptor (RRP) on the plant cell surface, known as the flagellin-responsive receptor, which is a leucine-rich repeat receptor kinase localized in the plasma membrane and accessible on the surface of plant cells. In plants, the most studied RRP is represented by the FLAGELLIN SENSING 2 (FLS2) receptor, which is highly conserved in both monocots and dicots.

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000). У Arabidopsis thaliana FLS2 представляет собой РРП, определяющий восприятие флагеллина, и является специфическим для связывания флагеллин-ассоциированного полипептида или полипептидов. Например, связывание Flg22 с внешним мембраносвязанным рецептором FLS2 растения запускает сигнальный каскад, вовлеченный во врожденный иммунный ответ, который индуцирует развитие у растения высокоспецифического ассоциированного с сигнализацией каскада, вовлеченного в активацию запускаемого паттернами иммунитета (Chinchilla et al., “The Arabidopsis receptor kinase FLS2 binds Flg22 and determines the specificity of flagellin perception,” Plant Cell 18: 465-476, 2006). Соответственно, связывание Flg22 с мембраносвязанным рецептором FLS2 Arabidopsis способствует первому этапу активации, на котором связывание вызывает каскад активации защитных ответов у растения. Взаимодействие Flg22-FLS2 может также приводить к продуцированию активных форм кислорода (АФК), которые вносят вклад в индукцию окислительного взрыва, ощелачиванию клеточной среды, последующей индукции патоген-реактивных генов и связанных с защитой ответов, которые в дальнейшем могут обеспечивать устойчивость к заболеванию у растения (Felix G. et al., “Plants have a sensitive perception system for the most conserved domain of bacterial flagellin,” The Plant Journal 18: 265-276, 1999,

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000, Meindi et al., “The bacterial elicitor flagellin activates its receptor in tomato cells according to the address-message concept,” The Plant Cell 12: 1783-1794, 2000). У томата высокоаффинное связывание Flg22 с FLS-рецептором наблюдали при использовании как интактных клеток, так и препаратов микросомальных мембран. В указанном исследовании связывание Flg22 с рецептором (рецепторами) FLS2 на поверхности плазматической мембраны было необратимым в физиологических условиях, что отражает процесс поглощения элиситора Flg22 с импортом в клетки томата (Meindi et al., “The bacterial elicitor flagellin activates its receptor in tomato cells according to the address-message concept,” The Plant Cell 12: 1783-1794, 2000). Распознавание Flg22 рецептором FLS2 запускает как местный, так и системный иммунные ответы у растений. Flg22-связанный, активированный комплекс рецептора FLS2 интернализуется в растительные клетки путем эндоцитоза и системно перемещается по растению (Jelenska et al., “Flagellin peptide flg22 gains access to long-distance trafficking in Arabidopsis via its receptor, FLS2,” Journal of Experimental Botany 68: 1769-1783, 2017), что может вносить вклад в системные иммунные ответы на Flg22.[0008] In Arabidopsis, the innate immune response to Flg22 involves a host recognition protein complex that contains the leucine-rich repeat (LRR) receptor kinase FLS2 (

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000). In Arabidopsis thaliana, FLS2 is the flagellin sensing RRP and is specific for the binding of a flagellin-associated polypeptide or polypeptides. For example, binding of Flg22 to the plant's external membrane-bound FLS2 receptor triggers a signaling cascade involved in the innate immune response, which induces the development in the plant of a highly specific signaling-associated cascade involved in the activation of pattern-driven immunity (Chinchilla et al., “The Arabidopsis receptor kinase FLS2 binds Flg22 and determines the specificity of flagellin perception,” Plant Cell 18: 465-476, 2006). Accordingly, binding of Flg22 to the membrane-bound Arabidopsis FLS2 receptor promotes the first step of activation, in which binding induces a cascade of activation of defense responses in the plant. The Flg22-FLS2 interaction may also lead to the production of reactive oxygen species (ROS), which contribute to the induction of an oxidative burst, alkalization of the cellular environment, subsequent induction of pathogen-reactive genes, and defense-related responses that may further confer disease resistance in the plant. (Felix G. et al., “Plants have a sensitive perception system for the most conserved domain of bacterial flagellin,” The Plant Journal 18: 265-276, 1999,

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000, Meindi et al., “The bacterial elicitor flagellin activates its receptor in tomato cells according to the address-message concept,” The Plant Cell 12: 1783-1794, 2000). In tomato, high affinity binding of Flg22 to the FLS receptor was observed using both intact cells and microsomal membrane preparations. In this study, Flg22 binding to the FLS2 receptor(s) on the plasma membrane surface was irreversible under physiological conditions, reflecting the process of Flg22 elicitor uptake with import into tomato cells (Meindi et al., “The bacterial elicitor flagellin activates its receptor in tomato cells according to the address-message concept,” The Plant Cell 12: 1783-1794, 2000). Flg22 recognition by the FLS2 receptor triggers both local and systemic immune responses in plants. The Flg22-bound, activated FLS2 receptor complex is internalized into plant cells by endocytosis and translocated systemically throughout the plant (Jelenska et al., “Flagellin peptide flg22 gains access to long-distance trafficking in Arabidopsis via its receptor, FLS2,” Journal of Experimental Botany 68 : 1769-1783, 2017), which may contribute to systemic immune responses to Flg22.

[0009] Mechanisms mediating perception via flagellin receptors involving Flg22 are highly conserved across diverse plant taxa (Taki et al., “Analysis of flagellin perception mediated by flg22 receptor OsFLS2 in rice,” Molecular Plant Microbe Interactions 21: 1635-1642, 2008 ). Synthetic polypeptides containing 15-22 or 28 amino acids from the conserved domains of the flagellin protein act as elicitors in submicromolar concentrations, initiating defense responses in plants of various species.

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000). Трансгенные растения, экспрессирующие флагеллин-связывающий рецептор, продемонстрировали эффективный ответ против определенных патогенов. Связывание флагеллина с FLS2 было вовлечено в инициацию экспрессии специфических MAP-киназных транскрипционных факторов, функционирующих на следующих после рецептора флагеллина FLS2 этапах. Мутантные растения (fls2), в которых отсутствует рецептор FLS2, нечувствительны к Flg22 (

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000) и характеризуются нарушенным связыванием Flg22 с рецептором FLS2. Мутантные растения (fls2) также демонстрировали повышенную восприимчивость к инфекции и заболеванию при обработке патогенными бактериями (Zipfel et al., “Bacterial disease resistance in Arabidopsis through flagellin perception,” Nature 428: 764-767, 2004).[0010] The production of transgenic plants was used to confirm flagellin-specific PAMPs that bind to flagellin-specific RRP. Ectopic expression of FLS2 in Arabidopsis plants has demonstrated a direct correlation between responses to flagellin and FLS2 expression levels, indicating that FLS2 is involved in the recognition of flagellin (a signal for the presence of bacteria) and mediates the activation of defense responses in plants (

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000). Transgenic plants expressing the flagellin-binding receptor have demonstrated an effective response against certain pathogens. Binding of flagellin to FLS2 has been implicated in initiating the expression of specific MAP kinase transcription factors that function downstream of the FLS2 flagellin receptor. Mutant plants (fls2) lacking the FLS2 receptor are insensitive to Flg22 (

. and Boller T., "FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis," Molecular Cell 5: 1003-1011, 2000) and are characterized by impaired binding of Flg22 to the FLS2 receptor. Mutant plants (fls2) also showed increased susceptibility to infection and disease when treated with pathogenic bacteria (Zipfel et al., “Bacterial disease resistance in Arabidopsis through flagellin perception,” Nature 428: 764-767, 2004).

[0011] Traditionally, methods for increasing disease resistance have been based on these and other similar discoveries and have involved a transgenic approach. Transgenic plants and seeds transformed with flagellin-sensing (FLS) receptor protein (source: WO2016007606A2, incorporated herein by reference in its entirety) or transcription factors involved in post-FLS signaling steps (source: WO2002072782A2, incorporated herein in its entirety by reference) ), ensured the production of plants that acquired resistance to the disease caused by certain pathogenic microorganisms. In another example, transgenic plants expressing the flagellin-responsive (FLS3) receptor also showed increased disease resistance compared to non-transgenic plants not expressing the FLS3 receptor (source: WO2016007606A2, herein incorporated by reference in its entirety).

Plant defensins/thionins

[0012] Plant defensins have also been characterized as antimicrobial peptides (AMPs). Plant defensins contain several conserved cysteinyl residues that form disulfide bridges and contribute to their structural stability. Defensins are among the most fully characterized cysteine-rich PMPs in plants. Members of the defensin family contain four disulfide bridges that fit into a globular structure. This highly conserved structure plays highly specialized roles in protecting plants from microbial pathogens. (Nawrot et al., “Plant antimicrobial peptides,” Folia Microbiology 59: 181-196, 2014).

[0013] Thionins are cysteine-rich plant PMPs classified as belonging to the defensin family and typically contain 45-48 amino acid residues, of which 6-8 are cysteine forming 3-4 disulfide bonds in higher plants. Thionins have been found to be present in both monocots and dicots, and their expression can be induced by infection with various microbes (Tam et. al., “Antimicrobial peptides from plants,” Pharmaceuticals 8: 711-757, 2015). Certain thionin amino acids, such as Lys1 and Tyr13, which are highly conserved, have been found to be critical to the functional toxicity of these PMPs.

Harpin and harpin-like (HpaG-like) polypeptides

[0014] Similar to flagellins or flagellin-associated polypeptides, harpins include a group of bacterially derived elicitors that are derived from larger precursor proteins. Harpins are critical for stimulating a hypersensitive response (HR) upon infiltration into the intercellular space or apoplast in plant cells (Kim et al., “Mutational analysis of Xanthomonas harpin HpaG identifies a key functional region that elicits the hypersensitive response in nonhost plants,” Journal of Bacteriology 186: 6239-6247, 2004). The use of a distant harpin-like (HpaG-like) bioactive primer polypeptide or polypeptides in a plant provides an alternative way to protect the plant from disease and insect attack. Harpins use a type III secretion system that allows proteins to be transported across the lipid bilayers that make up the plant cell plasma membrane. Binding of harpins to the plasma membrane surface of a cell can trigger an innate immune response resembling that triggered by pathogen-associated molecular patterns (PAMP) and are known to activate PAMP-triggered immunity (Engelhardt et al., “Separable roles of the Pseudomonas syringae pv. phaseolicola accessory protein HrpZ1 in ion-conducting pore formation and activation of plant immunity,” The Plant Journal 57: 706-717, 2009). Mutational analysis of a harpin-like HpaG-derived polypeptide showed that the 12 amino acid residues between Leu-39 and Leu50 of the original 133 amino acid harpin elicitor precursor protein are critical for stimulating the hypersensitivity (HR) response and subsequent innate immune responses in tobacco (Kim et al., “Mutational analysis of Xanthomonas harpin HpaG identifies a key functional region that elicits the hypersensitive response in nonhost plants,” Journal of Bacteriology 186: 6239-6247, 2004). This indicates that a specific region of the harpin amino acid sequence (similar to other PMPs) is responsible for elicitor responses. Harpins, such as HpaG-like polypeptides, can be used to increase resistance not only to plant pathogens but also to insects (Choi et al., “Harpins, multifunctional proteins secreted by gram-negative plant pathogenic bacteria,” Molecular Plant Microbe Interactions 26 : 1115-1122, 2013). Harpin has been used to induce plant resistance to diseases and protect against colonization and eating by phloem feeding insects such as aphids (Zhang et al., “Harpin-induced expression and transgenic overexpression of phloem protein gene At.PP2A1 in Arabidopsis repress phloem feeding of the green peach aphid Myzus persicae,” BMC Plant Biology 11: 1-11, 2011).

Elongation factor Tu (EF-Tu)

[0015] The elongation factor Tu is a protein commonly found in bacteria that acts as a pathogen-associated molecular pattern (PAMP) and initiates signaling cascades involved in plant disease resistance and innate immunity to microbial pathogens. Interestingly, some EF-Tu polypeptides are also found in plants. The first 18 amino acid residues of the N-terminus of EF-Tu from Escherichia coli, called elf18, are known to be a potent inducer of PAMP-triggered immune responses in plants (Zipfel et al., “Perception of the bacterial PAMP EF-Tu by the Receptor EFR restricts Agrobacterium -mediated transformation,” Cell 125: 749-760, 2006). Polypeptides derived from E. coli EF-Tu recognize the EF-Tu receptor (EFR) localized on the surface of plant cells (Zipfel et al., 2006). The mechanism of EF-Tu binding and EFR activation is similar to that of the complex of the Flg peptide with the FLS2 receptor (Mbengue et al., “Clathrin-dependent endocytosis is required for immunity mediated by pattern recognition receptor kinases,” Proc Natl Acad Sci U.S.A. 113: 11034 -9, 2016).

Growth-modifying bioactive priming polypeptides

Phytosulfokines (PSKα)

[0016] Phytosulfokines (PSKs) belong to a group of sulfated plant polypeptides encoded by ancestral genes that are common and highly conserved in higher plants (Sauter M., “Phytosulfokine peptide signaling,” Journal of Experimental Biology 66: 1-9, 2015). CSF genes encode small families of genes present in both monocots and dicots that encode a CSF polypeptide or polypeptides that can be active either as a pentapeptide or as a C-terminally truncated tetrapeptide (Lorbiecke R, Sauter M, “Comparative analysis of PSK peptide growth factor precursor homologs,” Plant Science 163: 348-357, 2002).

[0017] The phytosulfokine protein targets the plant secretory pathway through a conserved signal polypeptide (Lorbiecke R, Sauter M, “Comparative analysis of PSK peptide growth factor precursor homologs,” Plant Science 163: 348-357, 2002). Processing of the phytosulfokine precursor protein involves sulfonylation by tyrosylprotein sulfotransferase in the plant secretory pathway, particularly in the trans-Golgi, followed by secretion and proteolytic cleavage in the apoplast to produce CSF (Sauter M., “Phytosulfokine peptide signaling,” Journal of Experimental Biology 66: 1 -9, 2015). After the larger precursor polypeptide is processed to form CSF, the polypeptide undergoes tyrosine sulfation (Ryan et al., “Polypeptide hormones,” The Plant Cell Supplement, S251-S264, 2002). A membrane-bound receptor kinase from the leucine-rich repeat kinase family then recognizes the secreted polypeptide on the cell surface (Sauter M., “Phytosulfokine peptide signaling,” Journal of Experimental Biology 66: 1-9, 2015, where CSF can bind to a specialized CSF receptor (e.g. , PSK1 from Arabidopsis), which contains a leucine-rich repeat region located on the surface of the plant plasma membrane. Specific binding of CSF has been detected in plasma membrane fractions from suspension cell cultures derived from rice and maize, and binding to this receptor has been shown to initiate and stimulates cell proliferation (Matsubayashi et al., “Phytosulfokine-α, a sulfated pentapeptide, stimulates the proliferation of rice cells by means of specific high- and low-affinity binding sites,” Proceedings National Academy of Science USA 94:13357-13362 , 1997).

[0018] Phytosulfokines (PSKs) act as sulfated growth factors with biostimulatory activity, and they are involved in the control of root and shoot apical meristem development, growth regulation, and reproductive processes. CSFs have also been reported to initiate cell proliferation, differentiation of resting tissues, and are involved in the formation, stimulation, and differentiation of tracheal elements (Matsubayashi et al., “The endogenous sulfated pentapeptide phytosulfokine-α stimulates tracheary element differentiation of isolated mesophyll cells of zinnia, Plant Physiology 120:1043-1048, 1999). It has also been reported that PSK signaling is involved in the regulation of root and hypocotyl elongation in Arabidopsis seedlings (Kutschmar et al., “PSK-α promotes root growth in Arabidopsis,” New Phytologist 181: 820-831, 2009).

Root Spike Stimulator Polypeptide (RHPP)

[0019] Root spikelet stimulator polypeptide (RHPP) is a 12 amino acid fragment derived from soybean Kunitz trypsin inhibitor (KTI) protein that was found in soybean meal digested with Bacillus circulans HA ₁₂ alkaline protease (Matsumiya Y and Kubo M. “Soybean and Nutrition, Chapter 11: Soybean Peptide: Novel plant growth promoting peptide from soybean,” Agricultural and Biological Sciences, Sheny HE (editor), pgs. 215-230, 2011). RHPP, when applied to soybean roots, has been shown to accumulate in the roots and promote root growth by stimulating cell division and root hair differentiation in Brassica.

BRIEF DESCRIPTION OF THE INVENTION

[0020] A polypeptide is provided for bioactively priming a plant or plant part to improve growth, yield, health, increase longevity, productivity, and/or vitality of a plant or plant part, and/or reduce abiotic stress in a plant or plant part, and/ or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering plant architecture. Said polypeptide contains any of the following:

(a) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 1-225, 227-375, 526, 528, 530, 532, 534, 536, 538, 540, 541, 751 and 752; or

(b) a mutant flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 571-579 and 753; or

(c) a mutant flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 580-586; or

(d) a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450, 527, 531, 533, 535, 537 and 539; or

(e) a retro inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525; or

(f) a retro inverse Flg15 polypeptide, wherein the amino acid sequence of said retro inverse Flg15 polypeptide comprises SEQ ID NO: 529; or

(g) a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises any of SEQ ID NOs: 587, 589, 591, 593, 594, and 595; or

(h) a retro-inverse harpin or harpin-like polypeptide, wherein the amino acid sequence of said retro-inverse harpin or harpin-like polypeptide comprises any of SEQ ID NOs: 588, 590, 592, 596, and 597; or

(i) a root hair stimulator polypeptide (RHPP), wherein the amino acid sequence of said RHPP comprises any of SEQ ID NOs: 600, 603, and 604; or

(j) a Kunitz trypsin inhibitor (KTI) polypeptide, wherein the amino acid sequence of said KTI polypeptide comprises SEQ ID No: 602; or

(k) a retro inverse root hair stimulator polypeptide (RI RHPP), wherein the amino acid sequence of said RI RHPP comprises any of SEQ ID NOs: 601, 605 and 606; or

(l) a Tu elongation factor (EF-Tu) polypeptide, wherein the amino acid sequence of said EF-Tu polypeptide comprises any of SEQ ID NOs: 607-623; or

(m) a retro inverse Tu elongation factor (RI EF-Tu) polypeptide, wherein the amino acid sequence of said EF-Tu RI polypeptide comprises any of SEQ ID NOs: 624-640; or

(n) a fusion polypeptide containing SEQ ID NO: 750; or

(o) a phytosulfokine (FSK) polypeptide, wherein the amino acid sequence of said FSK polypeptide comprises SEQ ID NO: 598; or

(p) a retro-inverse phytosulfokine (RI CSF) polypeptide, wherein the amino acid sequence of said CSF RI polypeptide comprises SEQ ID NO: 599; or

(q) a thionine or thionine-like polypeptide, wherein the amino acid sequence of said thionine or thionine-like polypeptide comprises any of SEQ ID NOs: 650-749, and

wherein, optionally, said flagellin or flagellin-associated polypeptide according to (a), mutant flagellin or flagellin-associated polypeptide according to (c), harpin or harpin-like polypeptide according to (g), CSF polypeptide according to (o) and thionin or thionin-like polypeptide according to (q) either contains a chemical modification; or is a variant characterized by an insertion, deletion, inversion, repetition, duplication, addition or substitution of an amino acid in an amino acid sequence; either is part of a fusion protein; or contains a protease recognition sequence.

[0021] A composition is provided for bioactively priming a plant or plant part to improve growth, yield, health, increase longevity, productivity, and/or vitality of a plant or plant part, and/or reduce abiotic stress in a plant or plant part, and/ or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering plant architecture. Said composition contains either a polypeptide as described above, or any combination of said polypeptides, and an agrochemical or carrier; or any combination of these polypeptides.

[0022] Also provided is a seed coated with a polypeptide or composition as described herein.

[0023] Also provided is a recombinant microorganism that expresses or overexpresses a polypeptide. The specified polypeptide contains polypeptides as described above for the composition.

[0024] Methods are provided for increasing growth, yield, improving health, increasing longevity, productivity, and/or vitality of a plant or plant part, and/or reducing abiotic stress in a plant or plant part, and/or protecting a plant or plant part from diseases, insects and/or nematodes, and/or enhancement of the innate immune response of the plant or plant part, and/or changes in plant architecture. Said method may include the use of said polypeptide or said composition as described herein on a plant, on a plant part or plant growth medium, or in the rhizosphere in an area surrounding the plant or plant part, to improve growth, yield, health, increase longevity, productivity and/or vitality of the plant or plant part, and/or reduction of abiotic stress in the plant or plant part; and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering the architecture of the plant.

[0025] Alternatively, said method may include using said polypeptide or said composition as described herein in a plant growth medium to improve growth, yield, health, lifespan, productivity, and/or vitality of a plant or plant part. , which is intended to grow in said plant growth medium, and/or reduce abiotic stress in a plant or plant part, which is intended to be grown in said plant growth medium, and/or protect a plant or plant part, which is intended to be grown in said growth medium for plants, disease, insects and/or nematodes, and/or enhancement of the innate immune response, and/or alteration of the architecture of the plant or plant part to be grown in said plant growth medium.

[0026] Another method includes the use of a recombinant microorganism as described herein on a plant, on a plant part or plant growth medium, or in the rhizosphere in the area surrounding the plant or plant part, to improve growth, yield, health, increase the duration life, productivity and/or vitality of the plant or plant part, and/or reduction of abiotic stress in the plant or plant part; and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering the architecture of the plant. Said recombinant microorganism expresses said polypeptide, and the expression of said polypeptide is increased compared to the level of expression of said polypeptide in a wild-type microorganism of the same species under the same conditions.

[0027] A method for producing a polypeptide, comprising obtaining a fusion protein containing any polypeptide as described herein and an enterokinase (EK) cleavage site by fermentation, said enterokinase cleavage site enhancing the activity and stability of said polypeptide.

[0028] The features of the present invention are further defined in the appended claims and the list of embodiments provided below in the section entitled "Embodiments". Other objects and features will be partly understood and partly shown hereinafter in this document.

BRIEF DESCRIPTION OF THE DRAWINGS

[0029] FIG. 1 shows the bioactive Bt.4Q7Flg22 priming polypeptide in the natural L configuration (SEQ ID NO: 226) and the corresponding retro inverse or D configuration (SEQ ID NO: 375).

[0030] FIG. 2 illustrates the total available yield of corn treated with foliar applications of bioactive Bt.4Q7Flg22 priming polypeptides (SEQ ID NO:226) at 12 locations (panel A) and retro-inverse (RI) Bt.4Q7Flg22 variant (SEQ ID NO:375) at 10 locations (panel B) reported in bushels per acre compared to yields in the untreated control.

[0031] FIG. 3 illustrates the total available yield of corn treated by foliar application of the bioactive Bt.4Q7Flg22 priming polypeptide (SEQ ID NO: 226) at 6 locations, reported in bushels per acre, compared to that of the untreated control.

[0032] FIG. 4 illustrates the total available yield of soybean treated by foliar application of bioactive priming polypeptides Bt.4Q7Flg22 (SEQ ID NO: 226) (panel A) and retro-inverse (RI) Bt.4Q7Flg22 (SEQ ID NO: 375) (panel B) in 11 locations, reported in bushels per acre, compared to yields in the untreated control.

[0033] FIG. 5 illustrates the total available yield of corn treated with foliar application of bioactive priming polypeptides Ec.Flg22 (SEQ ID NO: 526) (panel A) and retro-inverse Ec.Flg22 (SEQ ID NO: 527) (panel B) at 12 locations, reported in bushels per acre compared to the yield in the untreated control.

[0034] FIG. 6 refers to the analysis of reactive oxygen species (ROS) activity when Bt.4Q7Flg22 is used in corn in combination with cellobiose at different concentrations as an additive (panel A) or in soybeans (panel B).

[0035] FIG. 7 relates to the assay of reactive oxygen species (ROS) activity using Bt.4Q7Flg22 at various concentrations to identify peak activity and timing of the assay.

[0036] FIG. 8 relates to the delivery of an agent using thionins to affect the growth (growth inhibition) of the Agrobacterium GV3101 strain in a flow dependent manner.

[0037] FIG. 9 relates to the delivery of an agent with Bt4Q7 Flg22 polypeptides, labeled or not labeled with thionins, to reduce the growth of Candidatus Liberibacter spp in HLB-infected citrus trees. Data are quantitative PCR results (cycle threshold values) for C. Liberibacter in leaf samples taken from treated infected trees.

[0038] FIG. 10 relates to the delivery of the agent to citrus trees that have been treated by injection with 1X or 10X Bt.4Q7Flg22 (SEQ ID NO: 226) to reduce the growth of Candidatus Liberibacter spp in HLB-infected citrus trees. Data are quantitative PCR results (cycle threshold values) for C. Liberibacter in leaf samples taken from treated infected trees.

[0039] FIG. 11 relates to 'Valencia' orange trees treated with 1X or 10X Bt.4Q7Flg22 (SEQ ID NO: 226) injection to increase fruit cluster per branch.

[0040] FIG. 12 relates to Valencia orange trees treated with 1X or 10X Bt.4Q7Flg22 injection (SEQ ID NO: 226) to improve fruit growth, measured in centimeters.

[0041] FIG. 13 refers to 'Valencia' orange trees treated with 1X or 10X Bt.4Q7Flg22 (SEQ ID NO: 226) injection to increase fruit population based on calculated fruit volume per branch.

[0042] FIG. 14 relates to 'Ruby Red' grapefruit trees sprayed with 1X or 10X Bt.4Q7Flg22 (SEQ ID NO: 226) to increase fruit cluster per branch.

[0043] FIG. 15 refers to 'Ruby Red' grapefruit trees sprayed with 1X or 10X Bt.4Q7Flg22 (SEQ ID NO: 226) to improve fruit growth, measured in centimeters.

[0044] FIG. 16 relates to 'Ruby Red' grapefruit trees sprayed with 1X or 10X Bt.4Q7Flg22 (SEQ ID NO: 226) to increase fruit population based on calculated fruit volume per branch.

DEFINITIONS

[0045] When used herein, terms in the singular, including those preceded by the definition "specified", they mean "at least one" or "one or more", unless otherwise indicated.

[0046] The terms "comprising", "including" and "having" are inclusive and imply the possibility of the presence of additional elements in addition to those listed.

[0047] "Abiotic stress" is defined herein as environmental conditions that can have a negative effect on a plant. Abiotic stress may include: temperature stress (caused by high or low temperatures), radiation-induced (visible or UV) stress, drought-induced stress, cold stress, salinity-induced stress, osmotic stress caused by nutrient deficiencies or high metal content stress, or water stress that leads to water scarcity, flooding or anoxia. Other abiotic stress factors include dehydration, injury, ozone, and high or low humidity.

[0048] "Bioactive priming" refers to the effect of the polypeptides as described herein to improve a plant or plant part. Bioactive priming can improve growth, yield, health, increase longevity, productivity and/or vitality of a plant or plant part, and/or reduce abiotic stress in a plant or plant part; and/or protect the plant or plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or plant part, and/or alter the architecture of the plant.

[0049] The term "bioactive priming polypeptide" herein may be used interchangeably with the term "priming agent(s)" and as described for the polypeptide classes of: flagellins and flagellin-associated polypeptides, harpins and harpin-like polypeptides (HpaG-like), thionins, Tu elongation factor (EF-Tu) and its polypeptides, phytosulfokine α (FSK-α), Kunitz trypsin inhibitor (KTI) and root hair stimulator polypeptide (RHPP), as well as any corresponding retro-inverse polypeptides listed.

[0050] "Coloring agent" in this document acts as a visual identifier of the product to identify and use the product. Coloring agents may include, but are not limited to, dyes and pigments, inorganic pigments, organic pigments, polymeric colorants, and pigment coating dispersions available in a variety of highly concentrated shades.

[0051] "Endogenous" as used herein refers to application from the inside of the plant surface. Bioactive priming polypeptides of small size are suitable, in particular, for signaling and communication within the plant. "Under the surface of a plant" refers to the surface on the inside of any plant membrane or plant cell. "Internal" may mean extracellular or intracellular in relation to a plant cell, and includes xylem, phloem, tracheids, and the like. "Endogenous" may refer to systemic movement or movement through a plant, for example, refer to movement from cell to cell in a plant. Endogenous application may include the delivery of bioactive primer polypeptides using recombinant endophytic bacteria or fungi, wherein the endophytic microorganism is brought to the plant from outside, and through natural mechanisms it moves into the plant.

[0052] "Exogenously" as used herein refers to application to the outside surface of a plant. The plant surface can be any external surface of the plant, such as the plasma membrane, cuticle, trichome, leaf, root hair, seed coat, and the like.

[0053] "Associated" or "like" polypeptides, as used herein, refers to polypeptides derived from or structurally similar to said polypeptide, but differing from said polypeptide in a different amino acid sequence and/or different source. For example, the thionin-like protein from Brassica rapa (SEQ ID NO: 694) has a different sequence from the Brassica napus thionin (SEQ ID NO: 693), but is structurally and functionally similar to it.

[0054] "Foliar treatment" as used herein refers to a composition that is applied to the aerial parts or foliage of a plant or plant part, which may include leaves, stems, flowers, branches, or any exposed part of a plant, such as a scion.

[0055] "Injection" as used herein can be used interchangeably with vaccination or immunization and provides a process in which bioactive primer polypeptides are delivered endogenously to a plant or plant part.

[0056] "Inoculation" means the delivery of bacteria or live microorganisms that produce a priming polypeptide to a plant or plant part. Inoculation may also refer to the delivery of a priming polypeptide for passive entry through a stomata or any opening or on a plant or plant part. "Plant" refers to, but is not limited to, a monocot plant, a dicot plant, or a gymnosperm plant. The term "plant" as used herein includes whole plants, plant organs, progeny of whole plants or plant organs, embryos, somatic embryos, germ structures, proto-feeds, proto-feed-like bodies, and plant cell suspensions. Plant organs include vegetative shoot organs/structures (e.g., leaves, stems, and tubers), roots, flowers, and flowering organs/structures (e.g., bracts, sepals, petals, stamens, carpels, anthers, and ovules), seeds, including the embryo , endosperm and seed coat, and fruit (mature ovary), plant tissue (eg, phloem tissue, vascular tissue, integumentary tissue, etc.), and cells (eg, sentinel cells, ova, trichomes, etc.). The class of plants that can be used in the methods described herein generally includes the entire class of higher plants, in particular angiosperms, monocotyledonous (monocotyledonous) and dicotyledonous (dicotyledonous) plants and gymnosperms. It includes plants of various levels of ploidy, including aneuploid, polyploid, diploid, haploid, homozygous and hemizygous. The plants described herein are agricultural monocots such as sorghum, corn, wheat, rice, barley, oats, rye, millet and triticale. The plants described herein may also be agricultural dicots such as apple, pear, peach, plum, orange, lemon, lime, grapefruit, kiwi, pomegranate, olive, peanut, tobacco, tomato, and the like. Also, these plants can be represented by horticultural and fruit plants, such as rose, calendula, primrose, dogwood, violet, geranium, and the like.

[0057] A plant "biostimulant" is any substance or microorganism applied to a plant or plant part that is used to improve nutritional efficiency, abiotic stress tolerance, and/or any other trait or traits of plant quality.

[0058] "Plant cell" as used herein refers to any plant cell and may include a cell on the surface of a plant or on the inside of a plant's plasma membrane, such as an epidermal cell, a trichome cell, a xylem cell, a phloem cell, a sieve tube element, or a cell- companion.

[0059] "Part of a plant" as used herein refers to a plant cell, leaf, stem, flower, flowering organ, fruit, pollen, vegetable, tuber, corm, bulb, pseudobulb, pod, root, rhizome, root ball, rootstock , graft or seed.

[0060] "Polypeptide" as used herein refers to any protein, peptide or polypeptide.

[0061] "Priming" or "peptide priming" as used herein refers to a technique used to improve plant performance. In particular, priming is a process in which bioactive priming polypeptides are applied exogenously or endogenously to a plant, plant part, plant cell, or plant cell space, resulting in outcomes that provide benefits to the plant, such as improved growth, productivity, tolerability. abiotic stress, tolerance or prevention of pests and diseases.

[0062] "Retro-inverse" ("retro-inverted") polypeptide as used herein refers to the polypeptide chain of a naturally occurring polypeptide from a normal all-L chain, reconfigured and constructed using non-naturally occurring D-amino acids in reverse order relative to naturally occurring L-amino acids. The fully dextrorotatory D-amino acid form and the parent chain containing the fully levorotatory L-form are topologically mirror-symmetric protein structures.

[0063] "Seed treatment" as used herein refers to a substance or composition that is used to treat or coat a seed. Examples of seed treatments include the use of biological organisms, chemical ingredients, inoculants, herbicide safeners, micronutrients, plant growth regulators, seed coatings, and the like applied to seeds to inhibit, control, or repel plant, insect, or other pathogens. pests that attack seeds, seedlings or plants, or any suitable agent that promotes plant growth and health.

[0064] A "synergistic" effect refers to an effect resulting from the interaction or cooperation of two or more bioactive priming polypeptides, substances, compounds, or other agents to produce a combined effect that is greater than the sum of their individual effects.

[0065] "Synergistic effective concentration" refers to the concentration or concentrations of two or more bioactive primer polypeptides, substances, compounds or other agents, which gives an effect greater than the sum of the individual effects.

DESCRIPTION OF THE PREFERRED IMPLEMENTATION OPTIONS

[0066] There is a growing need for bioactive polypeptides that act as "priming agents" to provide benefits in agricultural use. The use of bioactive "priming" polypeptides in agricultural practices represents a paradigm shift in integrated crop management practices, such as disease management, abiotic stress, and harvesting programs. Bioactive (naturally occurring, recombinant or synthetic) priming polypeptides are supplied in agricultural formulations. Described are compositions with bioactive priming polypeptides and methods for their use for a multi-stage crop treatment regimen to achieve agronomically desirable outcomes. Such desirable outcomes include improved plant phenotypes, for example showing protection from pests, pathogens and abiotic stress, as well as improved growth, increased plant productivity and yield. More specifically, bioactive primer polypeptides or formulations with bioactive primer polypeptides can be applied in various treatment regimens, exogenously and/or endogenously, to a plant or plant part and have been found to improve growth, yield, health, lifespan, productivity. and/or the vitality of a plant or plant part, and/or reduce abiotic stress in a plant or plant part, and/or protect the plant or plant part from disease, insects and/or nematodes, and/or increase the innate immune response in the plant or plant part plants, and/or change the architecture of plants.

[0067] Specific classes of synthetically or naturally occurring bioactive priming polypeptides, including flagellins and flagellin-associated polypeptides (including those conserved in Bacillus genera), thionins, harpin-like (HpaG-like) polypeptide, elongation factor Tu (EF -Tu), phytosulfokine (FSK-α) and root hair stimulator polypeptide (RHPP) were chosen due to their differing mechanisms of action, and they can be used alone or in combination with other polypeptides to meet the specific needs of agriculture described above. They can be used as a substitute for or in conjunction with commercially available agrochemicals, biostimulants, bioactive additives and/or pesticide compounds.

[0068] Also provided are combinations of bioactive primer polypeptides used in synergistically effective amounts to provide control of pests, pathogens; and, in addition, to obtain benefits in the form of improved growth and health of plants.

I. Polypeptides

[0069] Proposed bioactive primer polypeptides in naturally occurring, recombinant or chemically synthesized forms derived from bacteria or plants. Bioactive priming polypeptides are provided in both conventional L-amino acid and non-naturally occurring retro-inverse D-amino acid forms. In addition, bioactive priming polypeptides are provided that include non-naturally occurring modifications, including N-terminal and C-terminal modifications, cyclization, β-containing α-amino acids and D-amino acids, and other chemical modifications that increase the stability or efficacy of said polypeptides. . For example, flagellins and 22 amino acid long Flg-associated polypeptides derived from the entire flagellin coding region were initially isolated and identified from the assembled self-genome of the bacterial strain Bacillus thuringiensis 4Q7. These Flg22-derived polypeptides have been proposed in standard (L) and retro-inverse (D) forms. They are described as Bt.4Q7Flg22 and retro inverse (RI) Bt.4Q7Flg22. Other bacterial-derived bioactive priming polypeptides are Ec.Flg22 (Escherichia coli), HpaG-like polypeptide (Xanthomonas spp.) and plant-derived polypeptides include thionins (Citrus spp. and other plant species), CSF-α (Arabidopsis thaliana and other plants), EF-Tu (derived from both bacteria and plants) and RHPP (Glycine max).

[0070] Bioactive primer polypeptides may include full-length proteins, represented by naturally occurring, synthetic or recombinant forms derived from bacteria or plants. For example, both flagellin and EF-Tu, and KTI, and HpaG can be delivered to plants.

[0071] These bioactive priming polypeptides can also be delivered as fusion partners fused to other protein sequences, including protease cleavage sites, binding proteins, and targeting proteins for specific delivery to plants or plant parts.

[0072] Also provided are signature sequences, signal anchor sorting sequences, and secretion sequences, which may be naturally occurring or chemically synthesized, and targeting sequences, such as phloem targeting sequences, that are produced together with a bioactive primer polypeptide or polypeptides using recombinant microorganisms, and used either as fusion polypeptides or as accessory polypeptides with bioactive priming polypeptides as described herein.

[0073] Non-naturally occurring polypeptides are also described herein. More specifically, a polypeptide is provided for bioactively priming a plant or plant part to improve growth, yield, health, increase longevity, productivity and/or vitality of the plant or plant part, and/or reduce abiotic stress on the plant or plant part, and/ or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering plant architecture. Said polypeptide contains any of the following:

(a) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 1-225, 227-375, 526, 528, 530, 532, 534, 536, 538, 540 and 541; or

(b) a mutant flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 571-579; or

(c) a mutant flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 580-586; or

(d) a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450, 527, 531, 533, 535, 537 and 539; or

(e) a retro inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525; or

(f) a retro inverse Flg15 polypeptide, wherein the amino acid sequence of said retro inverse Flg15 polypeptide comprises SEQ ID NO: 529; or

(g) a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises any of SEQ ID NOs: 587, 589, 591, 593, 594, and 595; or

(h) a retro-inverse harpin or harpin-like polypeptide, wherein the amino acid sequence of said retro-inverse harpin or harpin-like polypeptide comprises any of SEQ ID NOs: 588, 590, 592, 596, and 597; or

(i) a root hair stimulator polypeptide (RHPP), wherein the amino acid sequence of said RHPP comprises any of SEQ ID NOs: 600, 603, and 604; or

(j) a Kunitz trypsin inhibitor (KTI) polypeptide, wherein the amino acid sequence of said KTI polypeptide comprises SEQ ID No: 602; or

(k) a retro inverse root hair stimulator polypeptide (RI RHPP), wherein the amino acid sequence of said RI RHPP comprises any of SEQ ID NOs: 601, 605 and 606; or

(l) a Tu elongation factor (EF-Tu) polypeptide, wherein the amino acid sequence of said EF-Tu polypeptide comprises any of SEQ ID NOs: 607-623; or

(m) a retro inverse Tu elongation factor (RI EF-Tu) polypeptide, wherein the amino acid sequence of said EF-Tu RI polypeptide comprises any of SEQ ID NOs: 624-640; or

(n) a fusion polypeptide containing SEQ ID NO: 750; or

(o) a phytosulfokine (FSK) polypeptide, wherein the amino acid sequence of said FSK polypeptide comprises SEQ ID NO: 598; or

(p) a retro-inverse phytosulfokine (RI CSF) polypeptide, wherein the amino acid sequence of said CSF RI polypeptide comprises SEQ ID NO: 599; or

(q) a thionine or thionine-like polypeptide, wherein the amino acid sequence of said thionine or thionine-like polypeptide comprises any of SEQ ID NOs: 650-749, and

wherein optionally said flagellin or flagellin-associated polypeptide according to (a), mutant flagellin or flagellin-associated polypeptide according to (c), harpin or harpin-like polypeptide according to (g), CSF polypeptide according to (o) and thionin or thionin-like polypeptide according to (q ) or contains a chemical modification; or is a variant characterized by an insertion, deletion, inversion, repetition, duplication, addition or substitution of an amino acid in an amino acid sequence; either is part of a fusion protein; or contains a protease recognition sequence.

Flagellins and flagellin-associated polypeptides

[0074] The specified polypeptide may include flagellin or flagellin-associated polypeptide.

[0075] Said flagellin or flagellin-associated polypeptide may be derived from a bacterium of the genus Bacillus, Lysinibacillus, Paenibacillus, Aneurinibacillus, or any combination thereof.

[0076] One of the major classes of bioactive priming polypeptides as described herein are flagellin(s) and flagellin-associated priming polypeptide or polypeptides. Conservative full and partial sequences encoding the amino acids of flagellin from various bacterial species, whether or not related to Bacillus, were identified using methods as described herein.

[0077] Flagellin is a structural protein that forms the bulk of the flagellar filaments of flagellated bacterial species, which can be conserved in the N-terminal and C-terminal regions of the protein, but can be variable in the central or middle part (Felix G. et al ., “Plants have a sensitive perception system for the most conserved domain of bacterial flagellin,” The Plant Journal 18: 265-276, 1999). The N- and C-terminal conserved regions of flagellins, which form the inner core of the flagellin protein, may play roles in the polymerization of the protein into a filament, in the mobility and transport of said protein, and in the surface attachment of the peptide fragment to the plant cell membrane/plant cell surface receptors.

[0078] Complete or partial flagellins (Tables 1-2) and flagellin-associated polypeptides derived from Bacillus flagellins and non-Bacillus flagellins (Tables 3 and 5) are provided.

[0079] The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 1-768, or any combination thereof.

[0080] Flagellin-associated bioactive priming polypeptides are derived from the coding sequences for flagellin polypeptides (such as Flg22 precursor proteins). More specifically, a polypeptide or cleavage fragment derived from said polypeptide is provided for the production of a bioactive Flg priming polypeptide that can be used to prime or treat a plant. Cleavage of the Flg22 fragment from larger precursors can be accomplished by introducing proteolytic cleavage sites near Flg22 to facilitate processing to produce an active biopeptide from the larger polypeptide.

[0081] Flagellin-associated bioactive primer polypeptides can be derived from full-length flagellin proteins (or precursor proteins from Flg-associated polypeptides of Bacillus, Lysinibacillus, Paenibacillus or Aneurinibacillus, or other unrelated genera of bacteria). For example, PCR-purified DNA from flagellin-associated polypeptides such as Flg22 and FlgII-28 (genus Bacillus) and Flg15 and Flg22 (E. coli) are cloned into a recombinant vector, amplified to obtain adequate amounts of purified DNA, which is then sequenced. using standard methods known to a person skilled in the art and used by him. The same methods can be applied to flagellin encoding sequences or partial flagellin sequences (Table 1), N- or C-terminal flagellin polypeptides (Table 2) and any Flg-associated polypeptides (Tables 3-5).

[0082] Said flagellin or flagellin-associated polypeptide can be derived from any member of eubacteria that contains a conserved 22 amino acid region recognized by plants. Preferred flagellin or flagellin-associated polypeptides may be from bacteria of the genus Bacillus, Lysinibacillus, Paenibacillus, Aneurinibacillus, or any combination thereof. Additional preferred flagellin and Flg22 sequences can be derived from gamma proteobacteria, which contain conserved 22 amino acid sequences with >68% identity.

Conserved flagellin sequences from Bacillus

[0083] Flagellin-associated bioactive priming polypeptides correspond to the N-terminal conserved domains of Bacillus spp. and other eubacterial flagellins, and are provided in synthetic, recombinant, or naturally occurring forms. Flagellin bioactive priming polypeptides Flg22, Flg15 and FlgII-28 (Table 3) have been identified and act as potent elicitors on a wide range of plant and vegetable crops to prevent and treat the spread of certain disease(s) while synergistically stimulating and promoting growth responses. in plants.

[0084] Flagellin and flagellin-associated bioactive priming polypeptides as described herein are provided for use alone or in combination with other bioactive priming polypeptides as described herein, and include conserved total and partial flagellins from Bacillus (Table 1), conserved N - and C-terminal regions from flagellin polypeptides (Table 2), Bacillus Flg22-derived and FlgII-28-derived bioactive priming polypeptides (Table 3) and retro-inverse mirror image sequences derived from Bacillus Flg22 and FlgII-28 (table 4). The underlined portion of the sequences in Tables 1 and 3 correspond to the identified sorting or secretion signal anchor sequences and signal anchor sequences, respectively. Other non-Bacillus-derived polypeptides and proteins are also described as functional equivalents and can be used in a similar manner (Table 5).

Table 1. Conserved sequences of flagellin from Bacillus

SEQID NO: Whole or partial coding sequence of flagellin - amino acids Flagellin
SEQID NO:1
Bacillus thuringiensis strain 4Q7 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTLDTGSTNPAQIEITLNSVKSADLGLDVQIGDEGDAESTAAADPTSAKQAIDAIDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO:2
Bacillus thuringiensis strain
HD1002 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTLDTGSTNPAQIEITLNSVKSADLGLDVQIGDEGDAESTAAADPTSAKQAIDAIDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO:3
Bacillus thuringiensis strain HD-789 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTLDTGSTNPAQIEITLNSVKSADLGLDVQIGDEGDAESTAAADPTSAKQAIDAIDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO:4
Bacillus cereus strain G9842 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTLDTGSTNPAQIEITLNSVKSADLGLDVQIGDEGDAESTAAADPTSAKQAIDAIDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO:5
Bacillus thuringiensis, indiana serovar, strain HD521 MRIGTNVLSMNARQSLYENEKHMNVAMEHLATGKKLNNASDNPANIAIVTRMHARASGMRVAIRNNEDAISMLRTAEAALQTVTNILQRMRDLAVQSANGTNSNKNRHSLNKEFQSLTEKIGYIGETTEFNDLSVFEGQNRPITLDDIGHTINMMKHIPPSPTQHDIKISTEQEARAAILKIEDALQSVSLHRADLGAMINRLQFNIENLNSQSMALTDAASLIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 6
Bacillus thuringiensis strain CTC mrintninsmrtqeymrqnqakmsnsmdrlssgkrinnasddaaglaiatrmraresglgvaadntqngmslirtadsamnsvsnillrmrdianqsangtntnenksalqkefaqlqkqityiaentqfndknllnedsevkiqtldsskgeqqitidlkavtleklnikdiaigkadaadkpvtpgatvdqkdldsvtdkiaaltetsskadidaiqssldnfkasmtpedvktledalkgfktgqanpadagvdaiqdalskvklptataaapaadadksdalaaiaaidaaltkvadnratlgatlnrldfnvnnlksqsssmasaasqiedadmakemsemtkfkilneagismlsqanqtpqmvskllq Flagellin
SEQ ID NO: 7
bacillus
thuringiensis,
yunnanensis serovar, strain IEBC-T20001 MTGITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGENKTIAIQTLDNADTTKQININLADSSTSALQIDKLTISGKTTDTTKTETITVTDDEIKAAKTDIDEFNDAKKALADLKAETSAGKADGSTDDEIKTAVSNFTKSFEKIQKFMNDSDIKTVQTEIEKFDAAAPALDKAKGMGIAFTSAMDPKAGTITKAATRQNASDAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANV Flagellin
SEQ ID NO: 8
Bacillus thuringiensis, serovar tolworthi MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALQSVSNILLRMRDLANQSANGTNTDENKAAMEKEFGQLKDQIKYITDNTQFNDKNLLDAASGTTKSIAIQTLDSDQASTQIEIKIAGSSLAALGLDKVQIGQETVAQKDLDVLTKAMGRLAAPDADATTRDLDVQVAKDAFDKVKGFIADPAQAKAVERAFEDYTAAEAGKEEDAAKAIDAAYKKVTGLTAGTTGTVDAHNAVNKIDAALKTVADNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 9
Bacillus cereus strain FM1 MRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQVALQKEFGELQKQIDYIAKNTQFNDKNLLSGKAGAPDQALEINIQTLDSSDPNQQIKISLDSVSTAQLGVKDLQIGSSSITQQQLDTLDNAMKRLETASTTAAVRDQDVADAKAAFENVKGFFSEGNVDSINRAFTDFANETTNKDDKAEAIYALYNNATLITKPTPDASNPASVDPANAIKKIDQAIEKIASSRATLGATLNRLDFNVNNLKSQQSSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 10
Bacillus cereus strain FM1 MRIGTNVLSMNARQSFYENEKRMNVAIEHLATGKKLNHASDNPANVAIVTRMHARTSGIHVAIRNNEDAISMLRTAEAALQTVTNILQRMRDVAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIDETTEFNDLSVFDRQNCPVTLDDIGHTVNVTKHIPPSPTQHDINISTEQEARAAIRKIEETLQNVSLHRADLGAMINQLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVYKLLQS Flagellin
SEQ ID NO: 11
Bacillus thuringiensis strain MC28 MDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTADNQQALQKEFGQLKEQISYIADNTEFNDKTLLKADNSVKIQTLDSADTNKQISIDLKGVTLNQLGLDTVNIGSEKLSAESLNVAKATMARLVKADQNADPSTFALDVNTAKESFDKIKGFIANKTNVQNVENAFNDYAVADPADKADKADAIQAAFNTAITGLTAGTPNTSNPSSAVDSIDAALKTVASNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 12
Bacillus bombysepticus strain Wang MRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASGTNTDKNQAAMQKEFDQLKEQIQYIADNTEFNDKKLLDGSNSTINIQTLDSHDKNKQITISLDSASLKNLDIKDLAIGSATINQTDLDTATNSMKRLATPATDGKVLAQDIADAKAAFNKVQSAYTPAEVDKIQDAFKAYDKLAADPASKATDIADAAKNVNTVFGTLATPTATKFDPSSAVEKIDKAIETIASSRATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 13
Bacillus thuringiensis, serovar kenyae MTGITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASGTNTDKNQAAMQKEFDQLKEQIQYIADNTEFNDKKLLDGSNSTINIQTLDSHDKNKQITISLDSASLKNLDIKDLAIGSATINQTDLDTATNSMKRLATPATDGKVLAQDIADAKAAFNKVQSAYTPAEVDKIQDAFKAYDKLAADPASKDTDIADAAKNVNTVFGTLATPTATKFDPSSAVEKIDKAIETIASSRATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 14
Bacillus thuringiensis, serovar kenyae MRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASGTNTDKNQAAMQKEFDQLKEQIQYIADNTEFNDKKLLDGSNSTINIQALDSHDKNKQITISLDSASLKNLDIKDLAIGSATINQTDLDTATNSMKRLATPATDGKVLAQDIADAKAAFNKVQSAYTPAEVDKIQDAFKAYDKLAADPASKDTDIADAAKNVNTVFGTLATPTATKFDPSSAVEKIDKAIETIASSRATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin (A-type)
SEQ ID NO: 15
Bacillus cereus MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKTIAIQTLDNADTSKQININLADSSTSALKIEKLTISGSTAIAGKTEKVTITAEDIKAAEEDIKAFTQAQEGLANLVKEVKDTDGSVKTPGSTPDDIKKAVTAFTESFEKMKKFMNDEDITKVEEKIKAFDAASPDLDAAKEMGTAFTAAMKPAAGEITKAAMKPNASDAIKSIDEALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin (A-type)
SEQ ID NO: 16
Bacillus cereus MRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNNASDNPANIAIVTRMHARASGMRLAIRNNEDTISMLRTAEAALQTLTNILQRMRDLAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIGETTEFNDLSVFDGQNRPVTLDDIDHTINMTKHIPPSPTQHDIKISTEQEARAAILKIEEALQSVSIHRADLGSMINRLQFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 17
Bacillus thuringiensis, serovar finitimus, strain YBT-020 MRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANVAIVTRMHARASGMRVAIRNNEDAISMLRTAEAALQTVTNVLQRMRDVAVQSANGTNLNKNRDSLNNEFQSLTEQIGYIDETTAFNDLSVFDGQNRPVTLDDIGHTVNVTKHISPSPTQHDINISTEQEARAAIRKIEEALQNVSLYRADLGAMINRLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVYKLLQS Flagellin
SEQ ID NO: 18
Bacillus thuringiensis, serovar finitimus, strain YBT-020 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLNVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDSNKSALQKEFAELQKQITYIADNTQFNDKNLLKEDSEVKIQTLDSSKGEQQIGIDLKAVTLEKLGINNISIGKADGTTEGTKADLTALQAAAKKLEKPDTGTMEKDVKDAKEEFDKVKASLSDEDVKKIEAAFGEFDKDKTNTTKASDIFNAIKDVKLADKAAAAPAPADLTKFKAALDKLQTPNAGTMVDDVKDAKDEFEKIKGSLSDADAQKIQAAFEEFEKANTDDSKASAIYNLAKDVKVNATDTTTGTDKDTTTSTDKDAALAAIAAIDAALTKVADNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 19
bacillus cereus,
strain B4264 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTAENKAAMQKEFGELKDQIKYISENTQFNDQHLLNAAKGSTNEIAIQTLDSDSSSKQIKITLQGASLDSLDIKDLQIGSGSTVSQTDLDVLDATMTRVKTATGATRDVDVQAAKSAFDKVKGLMTKPAEVKAIERAFEDYNAGKTDALATAIEAAYTANKTGLPAPAAAAGTVDALGAITKIDAALKTVADNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 20
Bacillus thuringiensis, serovar nigeriensis MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTSDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTTKQININLADSSTTALNIDKLSIEGTGNKTITLTAADIAKDKANIDAVGTAKTALAGLTGTPAAAAINSAVADFKTAFAKADKNLMSDAQIKAVTDAITAFEADATPDLTKAKAIGTAYTAPAAGDITKASPNASEAIKSIDAALDTIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 21
Bacillus thuringiensis MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTADNQQALQKEFGQLKEQISYIADNTEFNDKTLLKADNSVKIQTLDSADTNKQISIDLKGVTLNQLGLDTVNIGSETLSAESLNVAKATMARLVKADQNADPSTFALDVNTAKESFDKIKGFITNKTNVQNVENAFNDYTVADPADKADKADAIQAAFNTAITGLTAGTPNTSNPSSAVDAIDAALKTVASNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 22
Bacillus thuringiensis, serovar konkukian, strain 97-27 MRIGTNVLSMNARQSLYENEKRMNVAMEHFATGKKLNHASDNPANVAIVTRMHARASGMRVAIRNNEDAISMLRTAEAALQTVMNILQRMRDLAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIGETTEFNDLSVFDGQNRPVTLDDIGHTVNVTKHTSPSPTKHDIKISTEQEARAAIRKIEEALQNVSLHRADFGAMINRLQFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 23
Bacillus thuringiensis, serovar konkukian, strain 97-27 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTADNQQALQKEFGQLKEQISYIADNTEFNDKTLLKADNSVKIQTLDSADTNKQISIDLKGVTLNQLGLDTVNIGSETLSAESLNVAKATMARLVKADQNADPSTFALDVNTAKESFDKIKGFITNKTNVQNVENAFNDYTVADPADKADKADAIQAAFNTAITGLTAGTPNTSNPSSAVDAIDAALKTVASNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin protein FlaA
SEQ ID NO: 24
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 MRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANIVIVTRMYARASGMRVAIRNNEDAISMLRTAEAALQTVTNILQHMRDFAIQSANGTNSNTNRDSLNKEFQSLTEPIGYIGETTEFNDLSVFDGQNRPITLDDIGHTINMTKHIPPSPTQHDIKISTEQEARAAIRKIEEALQNVSLHRADLGSMINRLQFNIENLNSQSMALIDTASQVEDADMAQEISDFLKFKLLTAVALSVVSQANQIPQIVSKLLQS Flagellin protein FlaA
SEQ ID NO: 25
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLLDGSKKSIAIQTLDNADTNKQIDIQLSNVSTKELKLDTLSIEGSSSKTFTITADDMLAVGTANATAKAKAGTLKGLNVTTGDLTAAKTDVQDFRAAFDKVKGFMGSTEVTNIEKALTKFDGDQSLANAKAIGDALTSDLATTIAKDQTYSKNVSNASSAIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin B
SEQ ID NO: 26
Bacillus thuringiensis strain Bt407 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLLDGSKKSIAIQTLDNADTNKQIDIQLSNVSTKELKLDTLSIEGSSSKTFTITADDMLAVGTANATAKAKAGTLKGLNVTTGDLTAAKTDVQDFRAAFDKVKGFMGSTEVTNIEKALTKFDGDQSLANAKAIGDALTSDLATTIAKDQTYSKNVSNASSAIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 27
Bacillus thuringiensis, serovar chinensis CT-43 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLLDGSKKSIAIQTLDNADTNKQIDIQLSNVSTKELKLDTLSIEGSSSKTFTITADDMLAVGTANATAKAKAGTLKGLNVTTGDLTAAKTDVQDFRAAFDKVKGFMGSTEVTNIEKALTKFDGDQSLANAKAIGDALTSDLATTIAKDQTYSKNVSNASSAIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 28
Bacillus thuringiensis, serovar canadensis MTGITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTNENQAALNKEFDALKEQIDYISTNTEFNDKKLLDGSNKTIAVQTLDNADTSKQININLSNVSTKELGLDTLSIGTDKVEKTVYDATTKAFADLGAKTGADKAAFDADVTAAMKEFDKVKPFMSADDVKKIETKLEDYNKANDAGAQTAAQALGKEFATLTKLETTDLKANASGAIASIDTALKNIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 29
Bacillus thuringiensis, serovar galleriae MTGITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTNENQAALNKEFDALKEQIDYISTNTEFNDKKLLDGSNKTIAVQTLDNADTSKQININLSNVSTKELGLSTLSIGTDKVEKTVYDATTKAFADLGAKTGTDKAAFAADVTAAMKEFDKVKPFMSADDVKKIETKLEDYNKANDAGAEAAAQALGKEFATLTKLETTDLKANASGAIASIDTALKNIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ N-terminal helical region of flagellin
SEQ ID NO: 30
Bacillus weihenstephanensis MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLSVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLSNQSANGTNTDENQQALNKEFAALKDQIDYISKNTEFNDKKLLDGSNKSIAIQTLDNADTTKQINIDLSNVSTDTLNISGLTINGKKDITVTISDKDIANAATDIGKATSAQQGLADLTDTTPAVPDTPAVIGTGTAGNPQFPAVKGTPEIPGSSPAEIAKAVDDFKQAFNKVKGLMSDSAVSAMEQKFATFEKDKSLANAKDIGTAFSAPIAGNITKGEQNASGAIKSIDAALEKIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 31
Bacillus thuringiensis, serovar ostriniae MTGITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTAKQININLADSSTKALNIDTLSIAGTTDKTITITAKDLTDNKTTLDALKTAKDDLAKLDDKSDQATIDKAVDAFKTAFNNVDKNLLSDKAIEGITEKMTAFDGTHTAAAAIGAAYTEPTAADIKKSAPNASGAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 32
Bacillus thuringiensis MRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANVAIVTRMHARASGMRVAIRNNEDALSMLRTAEATLQTVANILQRMRDLAVQSSNDTNSNKNRDSLNKEFQSLTEQISYIGETTEFNDLSVFDGQNRPVTLDDIGHTVNVTKHISPSPTQHDIKISTEQEARAAIRKIEEALQNVLLHRADLGAMINRLQFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLSEVALSMVSQANQIPQMVSELLQS Flagellin
SEQ ID NO: 33
Bacillus thuringiensis MRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGENKTIAIQTLDNADTTKQININLADSSTSALQIDKLTISGKTTDTTKTQTITVTDDEIKAAKTDIDEFNDAKKALADLKAESAPSKGDGSSDDEIKEAVSNFKKSFEKIQKFMNDSDIKTVQTEIEKFDAAAPALDKAKGMGIAFTSAMDPKAGTITKAATRQNASDAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 34
Bacillus thuringiensis, serovar pondicheriensis MTGITINLEIDFFAYYRFSICRKVNIKKWGFLIMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGENKTIAIQTLDNADTTKQININLADSSTSALQIDKLTISGKTTDTTKTQTITVTDDEIKAAKTDIDEFNDAKKALADLKAESAPSKGDGSSDDEIKEAVSNFKKSFEKIQKFMNDSDIKTVQTEIEKFDAAAPALDKAKGMGIAFTSAMDPKAGTITKAATRQNASDAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin B
SEQ ID NO: 35
Bacillus thuringiensis, Berliner serovar MSIMRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANIVIVTRMYARASGMRVAIRNNEDAISMLRTAEAALQTVTNILQHMRDFAIQSANGTNSNTNRDSLNKEFQSLTEPIGYIGETTEFNDLSVFDGQNRPITLDDIGHTINMTKHIPPSPTQHDIKISTEQEARAAIRKIEEALQNVSLHRADLGSMINRLQFNIENLNSQSMALIDTASQVEDADMAQEISDFLKFKLLTAVALSVVSQANQIPQIVSKLLQS Flagellin A
SEQ ID NO: 36
Bacillus thuringiensis, Berliner serovar MARITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQDYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLLDGSKKSIAIQTLDNADTNKQIDIQLSNVSTKELKLDTLSIEGSSSKTFTITADDMLAVGTANATAKAKAGTLKGLNVTTGDLTAAKTDVQDFRAAFDKVKGFMGSTEVTNIEKALTKFDGDQSLANAKAIGDALTSDLATTIAKDQTYSKNVSNASSAIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 37
Bacillus cereus strain Q1 MRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNHASNNPANVAIVTRMHARASGMRVAIRNNEDAISMLRTAEAALQTVTNVLQRMRDVAVQSANGTNSSKNRDSLNKEFQSLTEQIGYIDETTEFNDLSVFDGQNRTVTLDDIGHTVNVTKHIPPSPTQHDINISTEQEARAAIRKIEEALQNVSLHRADLGAMINRLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 38
Bacillus cereus strain Q1 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLSVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQVALQKEFAALKEQITYIADNTQFNDKNLLNGNQTINIQTLDSHDSTKQIGIDLKSATLEALGIKDLTVGAVGSTEAKNYVDAKEALAKNVAANEFIDAKKALDGNAIAKGYVEAKTAFDDAKPEVKALVSNYTDALAALAKDDTNDDLKKDVADTKALMDANTVAKTYFEAKTAHDGADQAIKDIVTTYDSKLGALDDAANKAISDFDKAKAAFDESPAAKELVKTMDDAKQAATQNNTANAYLVAKAAAELAPNDADKKAELENATKALEKDDTAKGLVKTYENAKEALNPANAMPLDAVKQIDAALKTVADNRATLGATLNRLDFNVNNLKSQSSAMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 39
Bacillus thuringiensis, serovar morrisoni MRIGTNFLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANIAIVTRMHARANGMRVAIRNNEDAISMLRTAEAALQTVMNILQRMRDLAIQSANSTNSNKNRDSLNKEFQSLTEQISYIGETTEFNDLSVFDGQNRPVTLDDIGHTVHISKSIPPPSPTQHDIKISTEQEARAAILKIEEALQSVSLHRADLGAMINRLHFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 40
Bacillus thuringiensis, serovar neoleonensis MRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTSDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTTKQININLADSSTSALNIDKLSIEGTGNKTITLTAADIAKDKTNIDAVGTAKTALAGLTGTPAAAAINSAVADFKTAFAKADKNLMSDAQIKSVTDAITAFEADATPDLTKAKAIGTAYTAPAAGDITKASPNASEAIKSIDAALDTIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 41
Bacillus thuringiensis, serovar morrisoni MTGITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTAKQININLADSSTKALNIDTLSIAGTTDKTITITAKDLTDNKATLDALKTAKADLAKLDDKSDQATIDKAVDAFKTAFNNVDKNLLSDKAIEGITDKMTAFDGTHTAAAAIGTAYTEPTAGDITKSAPNASGAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 42
Bacillus thuringiensis, serovar morrisoni MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTAKQININLADSSTKALNIDTLSIAGTTDKTITITAKDLTDNKATLDALKTAKADLAKLDDKSDQATIDKAVDAFKTAFNNVDKNLLSDKAIEGITDKMTAFDGTHTAAAAIGTAYTEPTAGDITKSAPNASGAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 43
Bacillus thuringiensis, jegathesan serovar MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTNGNQAALNKEFDALKQQINYISTNTEFNDKKLLDGSNKTIAIQTLDNADTSKKIDIQLADVSTKSLNIDKLKIGGVSKETTDAVGDTFTKLSTTATTDMGALKIEVEAAMKEFDKVKGAMSAEDAKAVTDKLDAFNTAAAATNDAATIAAAKALGAAFDKTKVEMADPNASVAAIDSALENIASNRATLGATLNRLDFNVNNLKSQQSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 44
Bacillus cereus strain ATCC 10987 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMALIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQAALQKEFGELQKQIDYIAGNTQFNDKNLLDGSNPSISIQTLDSADQSKQISIDLKSATLEALGIKDLTVGATENTLAKATITAKDAFDAAKDASDAAKKEIDAAAKDTPSKNDAQLAKEYIEAKATLATLKPTDATYAAKAAELDAATTALNDNAKVLVDGYEKKLTTTKTKEAEYTAAKEQSTKSTAAADLVTKYETAKSNALGNDIAKEYLEAKTAYEANKNDISSKSRFEAAETELNKDITANKAAKVLVETYEKAKTAGTTEKSLVAVDKIDEALKTIADNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 45
Bacillus thuringiensis, serovar monterrey MTGITINLEIDFFAYYRFSICRKVNIKKWGFLIMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTNENQAALNKEFDALKEQINYISTNTEFNDKKLLDGSNKTIAIQTLDNADTSKKIDIKLADVSTESLKIDKLKIGGVSKETTDAVSETFTKLSTTKTTDKDALKAEVEAAMKEFDKVKGAMSTEDAKAVTDKLGLFNTAAAGTDDTAIATAAKNLGAAFDKTKVNMADPNASVAAIDSALENIASNRATLGATLNRLDFNVNNLKSQQSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 46
Bacillus cereus strain NC7401 MRIGTNVLSLNARQSLYENEKRMNVAMEHLATGKKLNNASDNPANIAIVTRMHARASSMRVAIRNNEDAISMLRTAEAALQTVTNVLQRMRDLAVQSANDTNSNKNRDSLNKEFQSLTEQIGYIDETTDFNDLSVFDGQNRTVTLDDIGHTVNVTKHIPPSPTQHDINISTEQEARAAIRKIEEALQNVSLHRADLGAMINRLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 47
Bacillus cereus strain NC7401 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLLNADKGITKEIAIQTLDSDSDSKQIKIKLQGSSLEALDIKDLQIGNTELAQKDLDLLNATMDRLDATVPGTRDVDVQAAKDAFDKVKGFYTNSDSVKAIERAFEDYATASTAGTAKADAATAIKAAFDLAANKVGKPATGGAQGSANSLGAITKIDAALKTVADNRATLGATLNRLDFNVNNLKSQASSMAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin (A-type)
SEQ ID NO: 48
Bacillus cereus strain AH820 MRINTNINSLRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRARESGLNVAANNTQDGMSLIRTADSALGSVSNILLRMRDLANQSANGTNTSDNQAAMQKEFAELQKQITYIADNTQFNDKNLLQSNSSINIQTLDSSDGNQQIGIELKSASLKSLGIEDLAIGASVNPLAKATVEASEAYDKAKADTAAFAKSIADTAATGTGAAKADAAAVDAYIKEADPTAKGNLYTGLTADQKKLADEHNTLKAAEDGKKAELTMATTKSTADGTAKGLVDAYDNAKSDAMNDPKAKAYLEAKMAYEKDTSNVANKQKLDSTKEAMEKDPASKDLVVKLDAAKAAATNGTPLDAVSKIDAALKTVADNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 49
Bacillus cereus AH187 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLLNADKGITKEIAIQTLDSDSDSKQIKIKLQGSSLEALDIKDLQIGNTELAQKDLDLLNATMDRLDATVPGTRDVDVQAAKDAFDKVKGFYTNSDSVKAIERAFEDYATASTAGTAKADAATAIKAAFDLAANKVGKPATGGAQGSANSLGAITKIDAALKTVADNRATLGATLNRLDFNVNNLKSQASSMAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 50
Bacillus cereus MDFFAYYRFSICRKVNIKKWGFFYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLLNADKGITKEIAIQTLDSDSDSKQIKIKLQGSSLEALDIKDLQIGNTELAQKDLDLLNATMDRLDATVPGTRDVDVQAAKDAFDKVKGFYTNSDSVKAIERAFEDYATASTAGTAKADAATAIKAAFDLAANKVGKPATGGAQGSANSLGAITKIDAALKTVADNRATLGATLNRLDFNVNNLKSQASSMAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin protein Fla
SEQ ID NO: 51
Bacillus cereus MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGENTSIAIQTLDSADTAKQININLADSSTSALLIDKLSISGAGAGTALAGVATADINAAGTKQAALSGLTGSKTTDELDDAVKEFKTEFDKVKSGLSAENADKITAAMDKYTNNKTLDNAKAIGDLYKTMAPADSTVVGTAGTKGQALIDLNATATGDTAQKRQVAVDAFKDDFDKIKGGLNAQDAAKVTAALDKFNKADGSGNTLENAQEIGKVFAEVAAGSTKSNASDAIKSIDKALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 52
Bacillus thuringiensis strain HD-771
[51] MRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASETNTSKNQAAMQKEFDQLKEQIQYIADNTEFNDKKLLDGSNSTINIQTLDSHDKNKQITISLDSASLKNLDITDLAIGSNTVNKNDLDTLNNSMKRLETAAADAAVQAQDVTDAKNAFNKVKSGYTPAEVEKMEDAFKAYDKVVADPAKTDALLKAAAEKINTEFKTLTAPTATAFDPSSSVEKIDKAIETIASSRATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 53
Bacillus thuringiensis, serovar sotto
[52] MRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASETNTSKNQAAMQKEFDQLKEQIQYIADNTEFNDKKLLDGSNSTINIQTLDSHDKNKQITISLDSASLKNLDITDLAIGSNTVNKNDLDTLNNSMKRLETAAADAAVQAQDVTDAKNAFNKVKSGYTPAEVEKMEDAFKAYDKVVADPAKTDALLKAAAEKINTEFKTLTAPTATAFDPSSSVEKIDKAIETIASSRATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 54
Bacillus thuringiensis, serovar Novosibirsk MGVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTSKQINIDLANTSTSSLKIDKLSIEGKGNQTIAITAADIAKDTNIAALTSAQGKLAALTGTPAPAALTTAVDEFKAAFEKVDKNLMSDTQITGIENAIKAYDGATTKTLALAQAVGTAYTAPTPGDITKELPNASSSIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQASSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 55
Bacillus thuringiensis, serovar londrina MGVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTSENQAALDKEFGALKEQINYISTNTEFNDKKLLDGSNETIAIQTLDNADEGKKIDIKLANVSTDSLKIDKLTIGGAAQKTVDAVADKFNALKTTTTTDKAAIQTEVDAVMKEFDKVKGSMSAEDAKVITDKLKDYNDAADTDTAKATAAKDLGAAFDKTKVNIANPNAAVAAIDSALENIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 56
Bacillus cereus strain E33L MRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNHASNNPANIAIVTRMHARASGMRVAIRNNEDALSMLRTAEAALQTVTNILQRMRDLAVQSANVTNSNKNRNSLNKEFQSLTEQISYIGETTEFNDLSVFDGQNRPVTLDDIGYTVNVTKHTPPSPTQHDIKISTEQEARAAIRKIEEALQNVSLHRADLGSMMNRLQFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 57
Bacillus cereus strain E33L MRINTNINSMRTQEYMRQNQAKMSTAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTDKNQGALDKEFAALKEQIDYISKNTEFNDKKLLDGSNKAIAIQTLDSDDKGKQIDISLSDTSTTALKINNLSIAANGLGIGSGKELVGVADNTIANASAEALKKLDGTTGDTDVKRSNAVKAFTDQYKDLKVAMNAKDVETIDAAIKKFEGANTLENAQAIGAAFEGAAKATLTTDINNATLTSKALSDLDTDSTTETRKAAMKDFVAAFDKVKGSMNSSDVTKISDAIDRFSKTDDSGNTLEAARAIGDAFKAATTNGKTSTATDANSAIKAIDEALETIASNRATLGATLNRLDFNVNNLKNQASSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 58
Bacillus cereus strain FRI-35 MRINTNINSMRTQEYMRQNQAKMSTAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTDKNQAALDKEFNALKEQIDYISKNTEFNDKKLLDGSNKSIAVQTLDNADTSKQININLSNTSTKALEINSLTISGTTPIAGKNETSKITAEQMTAASDALEKFKTAQEGLANLTEPTKGSDGKPEAGTGSSNEDIVKAVKAFKEAFKNIQPLMSDTDITTVQNKIDLFDEDAPDLSAAKLIGTTFEESMKPVADKEITKAAVKPNASDAIAAIDAALTKVADNRATLGATLNRLDFNVNNLKSQASSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 59
Bacillus cereus strain FRI-35 MRIGTNVLSLNARQSLYENEKRMNVAMEHLATGKKLNNASDNPANIAIVTRMHARASGMRVAIRNNEDAISMLRTAEAALQTVTNVLQRMRDLAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIDETTEFNNLSVFDGQNRPVTLDDIGHTVNVTKHIPPFPTQHDINISTEQEARAAIRKIEEALQNVSLHRADLGAMINRLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQVPQMVSKLLQS Flagellin
SEQ ID NO: 60
Bacillus thuringiensis MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRAHESGLSVAARNTSDGISLIRTADSALQSVSNILLRMRDIANQTANGTNKDTDIEALGKEFAALKEQITYVSDNTKFNGRELLKGGDDINIQTYDGSDESQQIKIKISELDLSSLDTGEVTDSDTARGTVSTLDDAITNIASKRAELGATLNRLDYNTQNVNSEAASMAASASQIEDADMAKEMSEMTKFKILSEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 61
Bacillus cereus strain ATCC 4342 MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRAHESGLSVAARNTSDGISLIRTADSALQSVSNILLRMRDIANQTANGTNKDTDIEALGKEFAALKEQITYVSDNTKFNGRELLKGGDDINIQTYDGSDESQQIKIKISELDLSSLDTGEVTDSDTARGTVSTLDDAITNIASKRAELGATLNRLDYNTQNVNSEAASMAASASQIEDADMAKEMSEMTKFKILSEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 62
Bacillus thuringiensis MRIGTNFLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANIAIVTRMHARANGMRVAIRNNEDAISMLRTAEAALQTVMNILQRMRDLAIQSANSTNSNKNRDSLNKEFQSLTEQISYIGETTEFNDLSVFDGQNRPVTLDDIGHTVHISKSIPPPSPTQHDIKISTEQEARAAILKIEEALQSVSLHRADLGAMINRLHFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQS Flagellin
SEQ ID NO: 63
Bacillus thuringiensis MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTAKQININLADSSTKALNIDTLSIAGTTDKTITITAKDLTDNKATLDALKTAKADLAKLDDKSDQATIDKAVDAFKTAFNNVDKNLLSDKAIEGITDKMTAFDGTHTAAAAIGTAYTEPTAGDITKSAPNASGAIKSIDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 64
Bacillus aryabhattai MRINHNITALNTYRQFNNANNAQAKSMEKLSSGQRINSASDDAAGLAISEKMRGQIRGLDQASRNAQDGVSLIQTAEGALNETHDILQRMRELVVQAGNGTNKTEDLDAIQDEIGSLIEEIGGETDSKGISDRAQFNGRNLLDGSLDITLQVGANAGQQVNLKIGDMSAGALGADTDSDGAADAFVNSINVKDFATTSFDDQLAIIDGAINQVSEQRSGLGATQNRLDHTINNLSTSSENLTASESRIRDVDYALAA Flagellin
SEQ ID NO: 65
Bacillus manliponensis MRINTNINSMRTQEYMRQNQDKMNTSMNRLSSGKQINSASDDAAGLAIATRMRAKEGGLNVGAKNTQDGMSALRTMDSALNSVSNILLRMRDLATQSATGTNQGNDRESLDLEFQQLTEEITHIAEKTNFNGNALLSGSGSAINVQLSDAAEDKLTIAAIDATASTLLKGAVDVKTEDKADAAITKIDQAIQDIADNRATYGSQLNRLDHNLNNVNSQATNMAAAASQIEDADMAKEMSEMTKFKILSEAGVSMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 66
Lysinibacillus sp. strain BF-4 MRIGSWTATGMSIVNHMNRNWNAASKSMLRLSSGYRINSAADDAAGLAISEKMRGQIRGLTMASKNIMDGVSLIQTAEGALNETHAIVQRMRELAVQAATDTNTDDDRAKLDLEFQELKKEIDRISTDTEFNTRTLLNGDYKDNGLKIQVGANSGQAIEVKIGDAGLAGIGLSTESIATREGANAALGKLDEATKNVSMERSRLGAYQNRLEHAYNVAENTAINLQDAESRIRDVDIAKEMMNMVKSQILAQVGQQVLAMHMQQAQGILRLLG Flagellin
SEQ ID NO: 67
Lysinibacillus sp. strain 13S34_air MKIGSWTATGMSIVNHMNRNWNAASKSMLRLSSGYRINSAADDAAGLAISEKMRGQIRGLTMASKNIMDGVSLIQTAEGALNETHAIVQRMRELAVQAATDTNTDDDRAKLDLEFQELKKEIDRISTDTAFNTRTLLNGDYKDNGLKIQVGANSGQAIEVKIGDAGLAGIGLSTESIATREGANAALGKLDEATKNVSMERSRLGAYQNRLEHAYNVAENTAINLQDAESRIRDVDIAKEMMHMVKSQILAQVGQQVLAMHIQQAQGILRLLG Flagellin
SEQ ID NO: 68
Paenibacillus sp. strain HW567 MIISHNLTALNTMNKLKQKDLAVSKSLGKLSSGLRINGASDDAAGLAISEKMRGQIRGLNQASRNIQDGISLIQVADGAMQEIHSMLQRMNELAVQASNGTYSGSDRLNIQSEVEQLIEEIDEIAGNTGFNGIKLLNGNNEKTEKTEKTGSVVSVNNPPNNKLITISSPVGTSVSEILNNLLTVFNEAKNGQVGDSDSKRVSSKFTLSINNDELSIVCDTGDGFLLSGGSPNLFYQGYIGGSYKYKFTEFINENDFINIMDIGGANGGDTLKFNFSSISKEPEEQKEQKGLTLQIGANSGETLNIKLPNVTTSAIGISSIDVSTIPNAESSLSSISAAIDKVSAERARMGAYQNRLEHSRNNVVTYAENLTAAESRIRDVDMAKEMMELMKNQIFTQAGQAMLLQTNTQPQAILQLLK Flagellin
SEQ ID NO: 69
Bacillus anthracis MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTKENQDALDKEFGALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTLDNADTAKQININLADSSTKALNIDSLTISGSKDATITITAEDITAASAEITAAKGARTALANLKDTPADPTKDPAASTPAEIKAAVDDFKGKFEKIKGLMNDTDVKAVEEKIKEFETTSTLAKAQAIGTAFTTGMEPKAGNITKNVPAASSSIKAIDSALETIASNRATLGATLNRLDFNVNNLKSQSSAMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 70
Bacillus anthracis MQKSQYKKMGVLKMRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETLDSSATNQQITIKLANTTAEKLGIDATTSNISISGAASALAAISALNTALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 71
Bacillus anthracis MRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETLDSSATNQQITIKLANTTAEKLGIDATTSNISISGAASALAAISALNTALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIKDADKAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 72
Bacillus anthracis MRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETLDSSATNQQITIKLANTTAEKLGIDATTSNISISGAASALAAISALNTALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMV Flagellin
SEQ ID NO: 73
Bacillus anthracis strain H9401 MNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETLDSSATNQQITIKLANTTAEKLGIDATTSNISISGAASALAAISALNTALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
SEQ ID NO: 74
Bacillus megaterium strain WSH-002 MRINHNITALNTYRQFNNANNAQAKSMEKLSSGQRINSASDDAAGLAISEKMRGQIRGLDQASRNAQDGVSLIQTAEGALNETHDILQRMRELVVQAGNGTNKTEDLDAIQDEIGSLIEEIGGEADSKGISDRAQFNGRNLLDGSLDITLQVGANAGQQVNLKIGDMSAGALGADTNSDGAADAFVNSINVKDFTATSFDDQLAIIDGAINQVSEQRSGLGATQNRLDHTINNLSTSSENLTASESRIRDVDYALAA Flagellin
SEQ ID NO: 75
Aneurinibacillus sp.XH2 MRINHNLPALNAYRNLAQNQIGTSKILERLSSGYRINRASDDAAGLAISEKMRGQIRGLEQGQRNTMDGVSLIQTAEGALQEIHEMLQRMRELAVQAANGTYSDKDKKAIEDEINQLTAQIDQIAKTTEFNGIQLIGDSDSTSLQDVKIQYGPKKEDSLTLELTTQPEADPPFAAGCKADKASLKIDNVDVISDPEGAIETFKAAIDQVSRIRSYFGAIQNRLEHVVNNLSNYTENLTGAESRIRDADMAKEMTEFTRFNIINQSATAMLAQANQLPQGVLQLLKG

N- and C-terminal conserved regions of flagellin

[0085] The flagellin or flagellin-associated polypeptide may comprise a truncated N-terminal polypeptide, wherein the amino acid sequence of said truncated N-terminal polypeptide may comprise SEQ ID NOs: 76, 78, 80, 82, 84, 86, 88, 90, 92 , 94, 96, 98, 100, 102, 104, 106.108, 109, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128, 130, 132, 134, 136, 138, 140, 142 , 144, 146, 148, 150, 152, 154.156, 158, 160, 162, 164, 166, 168, 170, 172, 174, 176, 178, 180, 182.184, 186, 188, 190, 194.19 , 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 752, or any combination thereof.

[0086] Flagellin or flagellin-associated polypeptide may contain a truncated C-terminal polypeptide, wherein the amino acid sequence of said truncated C-terminal polypeptide may comprise SEQ ID NOs: 77, 79, 81, 83, 85, 87, 89, 91, 93 , 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117, 119, 121, 123, 125, 127, 129, 131, 133, 135, 137, 141, 143, 145 , 147, 149, 151, 153, 155, 157, 159, 161, 163, 165, 167, 169, 171, 173, 175, 177, 179, 181, 183, 185, 187, 189, 191, 201, 203 , 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225 or any combination thereof.

[0087] N-terminal and C-terminal conserved regions were identified from full-length flagellin sequences from various strains of Bacillus spp. and other eubacteria (Table 2). Conservative N- and C-terminal domains were identified using BLAST multiple alignment software and functional annotations were assigned based on individual matches in Bacillus and other eubacteria database searches. The start site of the N-terminal region of the coding sequences is represented by methionine in bold (M). Conserved domains are shown as amino acid sequences N-terminus (left column) and C-terminus (right column).

Table 2. N- and C-terminal conserved regions of flagellins

SEQID NO: Conservative N-terminus Conservative C-terminus Flagellin
N-SEQ ID NO: 76
C-SEQ ID NO: 77
Bacillus thuringensis strain 4Q7
[CDS of SEQ ID NO:1] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTL IDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 78
C-SEQ ID NO: 79
Bacillus thuringiensis strain
HD1002
[CDS of SEQ ID NO:2] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTL IDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 80
C-SEQ ID NO: 81
bacillus thuringiensis,
strain HD-789
[CDS of SEQ ID NO:3] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTL IDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 82
C-SEQ ID NO: 83
bacillus cereus,
strain G9842
[CDS of SEQ ID NO:4] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINSASDDAAGLAIATRMKAREGGLNVAGRNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTKGNQASLQKEFAQLTEQIDYIAKNTQFNDQQLLGTADKKIKIQTL IDAAITTVAGQRATLGATLNRFEFNANNLKSQETSMADAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 84
C-SEQ ID NO: 85
Bacillus thuringiensis, indiana serovar, strain HD521
[CDS of SEQ ID NO:5] GFLNMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINSAADDAAGLAIATRMKAREGGLNVAARNTQDGMSLIRTADSALNSVSNILLRMRDLANQSATGTNTTKNQVALNKEFAALKEQITYIADNTQFNDKNLLKSTQEIKIQTL QLDAALTKVADNRATLGATLNRLDFNVNNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 86
C-SEQ ID NO: 87
Bacillus thuringiensis strain CTC
[CDS of SEQ ID NO:6] WGFLIMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTNENKSALQKEFAQLQKQITYIAENTQFNDKNLLNEDSEVKIQTLDS AIAAIDAALTKVADNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 88
C-SEQ ID NO: 89
bacillus
thuringiensis,
yunnanensis serovar, strain IEBC-T20001
[CDS of SEQ ID NO:7] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQAN Flagellin
N-SEQ ID NO: 90
C-SEQ ID NO: 91
Bacillus thuringiensis, serovar tolworthi
[CDS of SEQ ID NO:8] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALQSVSNILLRMRDLANQSANGTNTDENKAAMEKEFGQLKDQIKYITDNTQFNDKNLLDA IDAALKTVADNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 92
C-SEQ ID NO: 93
Bacillus cereus strain FM1
[CDS of SEQ ID NO: 9] MGVLNMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQVALQKEFGELQKQIDYIAKNTQFND RATLGATLNRLDFNVNNLKSQQSSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 94
C-SEQ ID NO: 95
Bacillus cereus strain FM1
[CDS of SEQ ID NO: 10] MGVLNMRIGTNVLSMNARQSFYENEKRMNVAIEHLATGKKLNHASDNPANVAIVTRMHARTSGIHVAIRNNEDAISMLRTAEAALQTVTNILQRMRDVAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIDETTEFND RADLGAMINQLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVYKLLQ Flagellin
N-SEQ ID NO: 96
C-SEQ ID NO: 97
Bacillus thuringiensis strain MC28
[CDS of SEQ ID NO: 11] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTADNQQALQKEFGQLKEQISYIADNTEFNDKTLL AVDSIDAALKTVASNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 98
C-SEQ ID NO: 99
bacillus bombysepticus,
Wang strain
[CDS of SEQ ID NO: 12] GFLNMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASGTNTDKNQAAMQKEFDQLKEQIQYI LGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 100
C-SEQ ID NO: 101
Bacillus thuringiensis, serovar kenyae
[CDS of SEQ ID NO: 13] GFLNMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASGTNTDKNQAAMQKEFDQLKEQIQYI RATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 102
C-SEQ ID NO: 103
Bacillus thuringiensis, serovar kenyae
[CDS of SEQ ID NO: 14] GFLNMRINTNINSMRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASGTNTDKNQAAMQKEFDQLKEQIQYI RATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin (A-type)
N-SEQ ID NO: 104
C-SEQ ID NO: 105
Bacillus cereus
[CDS of SEQ ID NO: 15] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin (A-type)
N-SEQ ID NO: 106
C-SEQ ID NO: 107
Bacillus cereus
[CDS of SEQ ID NO: 16] GFLNMRIGTNVLSMNARQSLYENEKRMNVAMEHLATGKKLNNASDNPANIAIVTRMHARASGMRLAIRNNEDTISMLRTAEAALQTLTNILQRMRDLAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIGETTEFND RADLGSMINRLQFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQ Flagellin
N-SEQ ID NO: 108
C-SEQ ID NO: 109
Bacillus thuringiensis, serovar finitimus,
strain YBT-020
[CDS of SEQ ID NO: 17] GVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLNVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDSNKSALQKEFAELQKQITYIADNTQFNDKNLLKEDSEVKIQTLDS AIDAALTKVADNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 110
C-SEQ ID NO: 111
Bacillus thuringiensis, serovar finitimus,
strain YBT-020
[CDS of SEQ ID NO: 18] GVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLNVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDSNKSALQKEFAELQKQITYIADNTQFNDKNLLKEDSEVKIQTLDS AAIDAALTKVADNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 112
C-SEQ ID NO: 113
bacillus cereus,
strain B4264
[CDS of SEQ ID NO: 19] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTAENKAAMQKEFGELKDQIKYISENTQFNDQHLL TVADNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 114
C-SEQ ID NO: 115
Bacillus thuringiensis, serovar nigeriensis
[CDS of SEQ ID NO: 20] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTSDNQKALDKEFSALKEQIDYISKNTEFNDKKLL AIKSIDAALDTIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 116
C-SEQ ID NO: 117
Bacillus thuringiensis
[CDS of SEQ ID NO: 21] WGFLIMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTADNQQALQKEFGQLKEQISYIADNTEFND AVDAIDAALKTVASNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 118
C-SEQ ID NO: 119
Bacillus thuringiensis, serovar konkukian,
strain 97-27
[CDS of SEQ ID NO: 22] WGFLIMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMetRDIANQSANGTNTADNQQALQKEFGQLKEQISYIADNTEFNDKTLL AVDAIDAALKTVASNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 120
C-SEQ ID NO: 121
Bacillus thuringiensis, serovar konkukian,
strain 97-27
[CDS of SEQ ID NO: 23] WGFLIMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin protein FlaA
N-SEQ ID NO: 122
C-SEQ ID NO: 123
Bacillus thuringiensis, serovar thuringiensis, strain IS5056
[CDS of SEQ ID NO: 24] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin protein FlaA
N-SEQ ID NO: 124
C-SEQ ID NO: 125
Bacillus thuringiensis, serovar thuringiensis, strain IS5056
[CDS of SEQ ID NO: 25] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin B
N-SEQ ID NO: 126
C-SEQ ID NO: 127
bacillus thuringiensis,
strain Bt407
[CDS of SEQ ID NO: 26] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 128
C-SEQ ID NO: 129
Bacillus thuringiensis, serovar chinensis CT-43
[CDS of SEQ ID NO: 27] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 130
C-SEQ ID NO: 131
Bacillus thuringiensis, serovar Canadensis
[CDS of SEQ ID NO: 28] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTNENQAALNKEFDALKEQIDYISTNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 132
C-SEQ ID NO: 133
Bacillus thuringiensis, serovar galleriae
[CDS of SEQ ID NO: 29] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTNENQAALNKEFDALKEQIDYISTNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ N-terminal helical region of flagellin
N-SEQ ID NO: 134
C-SEQ ID NO: 135
Bacillus weihenstephanensis
[CDS of SEQ ID NO: 30] GVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLSVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLSNQSANGTNTDENQQALNKEFAALKDQIDYISKNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 136
C-SEQ ID NO: 137
Bacillus thuringiensis, serovar ostriniae
[CDS of SEQ ID NO: 31] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLL IDAALETIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQS Flagellin
N-SEQ ID NO: 138
C-SEQ ID NO: 139
Bacillus thuringiensis
[CDS of SEQ ID NO: 32] WGFLIMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLL LGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 140
C-SEQ ID NO: 141
Bacillus thuringiensis
[CDS of SEQ ID NO: 33] WGFLIMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLL LGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 142
C-SEQ ID NO: 143
Bacillus thuringiensis, serovar pondicheriensis
[CDS of SEQ ID NO: 34] WGFLIMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTDDNQKALDKEFSALKEQIDYISKNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMAAAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin B
N-SEQ ID NO: 144
C-SEQ ID NO: 145
Bacillus thuringiensis, Berliner serovar
[CDS of SEQ ID NO: 35] GFLNMRINTNINSMRTQDYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin A
N-SEQ ID NO: 146
C-SEQ ID NO: 147
Bacillus thuringiensis, Berliner serovar
[CDS of SEQ ID NO: 36] GFLNMARITINLEIDFFAYYRFSICRKVNIKKWGFLNMRINTNINSMRTQDYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDISNQSANGTNTDKNQSALDKEFAALKDQIDYISKNTEFNDQKLL AIASIDAALESIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 148
C-SEQ ID NO: 149
Bacillus cereus strain Q1
[CDS of SEQ ID NO: 37] GVLYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLSVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQVALQKEFAALKEQITYIADNTQFNDKNLLNGNQTINIQTLDSHDST TVADNRATLGATLNRLDFNVNNLKSQSSAMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 150
C-SEQ ID NO: 151
Bacillus cereus strain Q1
[CDS of SEQ ID NO: 38] GVLYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLSVAADNTQNGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTDKNQVALQKEFAALKEQITYIADNTQFNDKNLLNGNQTINIQTLDSHDST TVADNRATLGATLNRLDFNVNNLKSQSSAMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 152
C-SEQ ID NO: 153
Bacillus thuringiensis, serovar morrisoni
[CDS of SEQ ID NO: 39] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLL LGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 154
C-SEQ ID NO: 155
Bacillus thuringiensis, serovar neoleonensis
[CDS of SEQ ID NO: 40] GFLNMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARENGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTSDNQKALDKEFSALKEQIDYISKNTEFNDKKLL AIKSIDAALDTIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 156
C-SEQ ID NO: 157
Bacillus thuringiensis, serovar morrisoni
[CDS of SEQ ID NO: 41] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 158
C-SEQ ID NO: 159
Bacillus thuringiensis, serovar morrisoni
[CDS of SEQ ID NO: 42] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLL RATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 160
C-SEQ ID NO: 161
Bacillus thuringiensis, jegathesan serovar
[CDS of SEQ ID NO: 43] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDIANQSANGTNTNGNQAALNKEFDALKQQINYISTNTEFNDKKLLDGSNKTIAIQTLD LGATLNRLDFNVNNLKSQQSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 162
C-SEQ ID NO: 163
Bacillus cereus strain ATCC 10987
[CDS of SEQ ID NO: 44] GVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMALIRTADSAMNSVSNILLRRDIANQSANGTNTDKNQAALQKEFGELQKQIDYIAGNTQFNDK DKIDEALKTIADNRATLGATLNRLDFNVNNLKSQSASMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 164
C-SEQ ID NO: 165
Bacillus thuringiensis, serovar monterrey
[CDS of SEQ ID NO: 45] WGFLIMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTNENQAALNKEFDALKEQINYISTNTEFNDKKLL RATLGATLNRLDFNVNNLKSQQSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 166
C-SEQ ID NO: 167
Bacillus cereus strain NC7401
[CDS of SEQ ID NO: 46] WGFFYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLL TVADNRATLGATLNRLDFNVNNLKSQASSMAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 168
C-SEQ ID NO: 169
Bacillus cereus strain NC7401
[CDS of SEQ ID NO: 47] WGFFYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLL TVADNRATLGATLNRLDFNVNNLKSQASSMAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin (A-type)
N-SEQ ID NO: 170
C-SEQ ID NO: 171
Bacillus cereus strain AH820
[CDS of SEQ ID NO: 48] GVLNMRINTNINSLRTQEYMRQNQAKMSNSMDRLSSGKRINNASDDAAGLAIATRMRARESGLNVAANNTQDGMSLIRTADSALGSVSNILLRMRDLANQSANGTNTSDNQAAMQKEFAELQKQITYIADNTQFNDKNLL IDAALKTVADNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 172
C-SEQ ID NO: 173
Bacillus cereus AH187
[CDS of SEQ ID NO: 49] WGFFYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLL TVADNRATLGATLNRLDFNVNNLKSQASSMAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 174
C-SEQ ID NO: 175
Bacillus cereus
[CDS of SEQ ID NO: 50] WGFFYMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVASNNTQDGMSLIRTADSALNSVSNILLRMRDLANQSANGTNTNENKAAMQKEFGELKEQIKYIAENTQFNDQHLL TVADNRATLGATLNRLDFNVNNLKSQASSAAAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin protein Fla
N-SEQ ID NO: 176
C-SEQ ID NO: 177
Bacillus cereus
[CDS of SEQ ID NO: 51] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYISKNTEFNDKKLL LGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 178
C-SEQ ID NO: 179
bacillus thuringiensis,
strain HD-771
[CDS of SEQ ID NO: 52] GFLNMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASETNTSKNQAAMQKEFDQLKEQIQYI RATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 180
C-SEQ ID NO: 181
Bacillus thuringiensis, serovar sotto
[CDS of SEQ ID NO: 53] GFLNMRINTNINSMRTQEYMRQNQTKMSNAMDRLSSGKRINNASDDAAGLAIATRMRSREGGLNVAARNTEDGMSLIRTADSALNSVSNILLRMRDLANQSASETNTSKNQAAMQKEFDQLKEQIQYI RATLGATLNRLDFNVTNLKSQENSMAASASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 182
C-SEQ ID NO: 183
Bacillus thuringiensis, serovar Novosibirsk
[CSD of SEQ ID NO: 54] MGVLNMRINTNINSMRTQEYMRQNQAKMSTAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTDKNQGALDKEFAALKEQIDYISKNTEFNDKKLL AIKAIDEALETIASNRATLGATLNRLDFNVNNLKNQASSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 184
C-SEQ ID NO: 185
Bacillus thuringiensis, serovar Londrina
[CDS of SEQ ID NO: 55] MGVLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTSENQAALDKEFGALKEQINYISTNTEFNDKKLL AIDSALENIASNRATLGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 186
C-SEQ ID NO: 187
Bacillus cereus strain E33L
[CDS of SEQ ID NO: 56] MGVLNMRINTNINSMRTQEYMRQNQAKMSTAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTDKNQGALDKEFAALKEQIDYISKNTEFNDKKLL LGATLNRLDFNVNNLKNQASSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 188
C-SEQ ID NO: 189
Bacillus cereus strain E33L
[CDS of SEQ ID NO: 57] MGVLNMRINTNINSMRTQEYMRQNQAKMSTAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTDKNQGALDKEFAALKEQIDYISKNTEFNDKKLL ATLNRLDFNVNNLKNQASSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 190
C-SEQ ID NO: 191
bacillus cereus,
strain FRI-35
[CDS of SEQ ID NO: 58] WGFFYMRINTNINSMRTQEYMRQNQAKMSTAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGISLIRTADSAMNSVSNILLRMRDLANQSANGTNTDKNQAALDKEFNALKEQIDYISKNTEFNDKKL AIAAIDAALTKVADNRATLGATLNRLDFNVNNLKSQASSMASAASQVEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 192
C-SEQ ID NO: 193
bacillus cereus,
strain FRI-35
[CDS of SEQ ID NO: 59] WGFFYMRIGTNVLSLNARQSLYENEKRMNVAMEHLATGKKLNNASDNPANIAIVTRMHARASGMRVAIRNNEDAISMLRTAEAALQTVTNVLQRMRDLAVQSANGTNSNKNRDSLNKEFQSLTEQIGYIDETTEFNN AIRKIEEALQNVSLHRADLGAMINRLQFNIENLNSQSTALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQVPQMVSKLLQ Flagellin
N-SEQ ID NO: 194
C-SEQ ID NO: 195
Bacillus thuringiensis
[CDS of SEQ ID NO: 60] LVPFAVWLAMSRIRRRILDTDCKAESAVRIKEIPSDVLRAATERPLSCARIRVAIARPAASSEALLIRLPLDKRSIALLILAWFWRMYSCVRMLLMFVLILMLRTP MAASASQIEDADMAKEMSEMTKFKILSEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 196
C-SEQ ID NO: 197
Bacillus cereus strain ATCC 4342
[CDS of SEQ ID NO: 61] AVWLAMSRIRRRILDTDCKAESAVRIKEIPSDVLRAATERPLSCARIRVAIARPAASSEALLIRLPLDKRSIALLILAWFWRMYSCVRMLLMFVLILMLRTP SMAASASQIEDADMAKEMSEMTKFKILSEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 198
C-SEQ ID NO: 199
Bacillus thuringiensis
[CDS of SEQ ID NO: 62] GFLNMRIGTNFLSMNARQSLYENEKRMNVAMEHLATGKKLNHASDNPANIAIVTRMHARANGMRVAIRNNEDAISMLRTAEAALQTVMNILQRMRDLAIQSANSTNSNKNRDSLNKEFQSLTEQISYI LGAMINRLHFNIENLNSQSMALTDAASRIEDADMAQEMSDFLKFKLLTEVALSMVSQANQIPQMVSKLLQ Flagellin
N-SEQ ID NO: 200
C-SEQ ID NO: 201
Bacillus thuringiensis
[CDS of SEQ ID NO: 63] GFLNMRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSALNSVSNILLRMRDIANQSANGTNTGDNQKALDKEFSALKEQIDYI LGATLNRLDFNVNNLKSQSSSMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 202
C-SEQ ID NO: 203
Bacillus aryabhattai
[CDS of SEQ ID NO: 64] MRINHNITALNTYRQFNNANNAQAKSMEKLSSGQRINSASDDAAGLAISEKMRGQIRGLDQASRNAQDGVSLIQTAEGALNETHDILQRMRELVVQAGNGTNKTEDLDAIQDEIGSLIEEIGGETDSKGISDRAQFNGRNLLDGSLDITLQVGA IDGAINQVSEQRSGLGATQNRLDHTINNLSTSSENLTASESRIRDVDYALAA Flagellin
N-SEQ ID NO: 204
C-SEQ ID NO: 205
Bacillus manliponensis
[CDS of SEQ ID NO: 65] MRINTNINSMRTQEYMRQNQDKMNTSMNRLSSGKQINSASDDAAGLAIATRMRAKEGGLNVGAKNTQDGMSALRTMDSALNSVSNILLRMRDLATQSATGTNQGNDRESLDLEFQQLTEEITHIAEKTNFNGNALLSGSGSGSAINVQLS IDQAIQDIADNRATYGSQLNRLDHNLNNVNSQATNMAAAASQIEDADMAKEMSEMTKFKILSEAGVSMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 206
C-SEQ ID NO: 207
Lysinibacillus sp., strain BF-4
[CDS of SEQ ID NO: 66] MRIGSWTATGMSIVNHMNRNWNAASKSMLRLSSGYRINSAADDAAGLAISEKMRGQIRGLTMASKNIMDGVSLIQTAEGALNETHAIVQRMRELAVQAATDTNTDDDRAKLDLEFQELKKEIDRISTDTEFNTRTLLNGDYKDNGLKIQVG LDEATKNVSMERSRLGAYQNRLEHAYNVAENTAINLQDAESRIRDVDIAKEMMNMVKSQILAQVGQQVLAMHMQQAQGILRLLG Flagellin
N-SEQ ID NO: 208
C-SEQ ID NO: 209
Lysinibacillus sp., strain 13S34_air
[CDS of SEQ ID NO: 67] MKIGSWTATGMSIVNHMNRNWNAASKSMLRLSSGYRINSAADDAAGLAISEKMRGQIRGLTMASKNIMDGVSLIQTAEGALNETHAIVQRMRELAVQAATDTNTDDDRAKLDLEFQELKKEIDRISTDTAFNTRTLLNGDYKDNGLKIQVG LDEATKNVSMERSRLGAYQNRLEHAYNVAENTAINLQDAESRIRDVDIAKEMMHMVKSQILAQVGQQVLAMHIQQAQGILRLLG Flagellin
N-SEQ ID NO: 210
C-SEQ ID NO: 211
Paenibacillus sp., strain HW567
[CDS of SEQ ID NO: 68] MIISHNLTALNTMNKLKQKDLAVSKSLGKLSSGLRINGASDDAAGLAISEKMRGQIRGLNQASRNIQDGISLIQVADGAMQEIHSMLQRMNELAVQASNGTYSGSDRLNIQSEVEQLIEEIDEIAGNTGFNGIKLLNGNNEKTEKTEK ISAAIDKVSAERARMGAYQNRLEHSRNNVVTYAENLTAAESRIRDVDMAKEMMELMKNQIFTQAGQAMLLQTNTQPQAILQLLK Flagellin
N-SEQ ID NO: 212
C-SEQ ID NO: 213
Bacillus anthracis
[CDS of SEQ ID NO: 69] MRINTNINSMRTQEYMRQNQAKMSNAMDRLSSGKRINNASDDAAGLAIATRMRARESGLGVAANNTQDGMSLIRTADSAMNSVSNILLRMRDLANQSANGTNTKENQDALDKEFGALKEQIDYISKNTEFNDKKLLNGDNKSIAIQTL IDSALETIASNRATLGATLNRLDFNVNNLKSQSSAMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 214
C-SEQ ID NO: 215
Bacillus anthracis
[CDS of SEQ ID NO: 70] MQKSQYKKMGVLKMRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETL ALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 216
C-SEQ ID NO: 217
Bacillus anthracis
[CDS of SEQ ID NO: 71] MRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETL ALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIKDADKAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 218
C-SEQ ID NO: 219
Bacillus anthracis
[CDS of SEQ ID NO: 72] MRINTNINSMRTQEYMRQNQDKMNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETL ALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMV Flagellin
N-SEQ ID NO: 220
C-SEQ ID NO: 221
Bacillus anthracis strain H9401
[CDS of SEQ ID NO: 73] MNVSMNRLSSGKRINSAADDAAGLAIATRMRARQSGLEKASQNTQDGMSLIRTAESAMNSVSNILTRMRDIAVQSSNGTNTAENQSALQKEFAELQEQIDYIAKNTEFNDKNLLAGTGAVTIGSTSISGAEISIETL LNTALNTVAGNRATLGATLNRLDRNVENLNNQATNMASAASQIEDADMAKEMSEMTKFKILNEAGISMLSQANQTPQMVSKLLQ Flagellin
N-SEQ ID NO: 222
C-SEQ ID NO: 223
Bacillus megaterium strain WSH-002
[CDS of SEQ ID NO: 74] MRINHNITALNTYRQFNNANNAQAKSMEKLSSGQRINSASDDAAGLAISEKMRGQIRGLDQASRNAQDGVSLIQTAEGALNETHDILQRMRELVVQAGNGTNKTEDLDAIQDEIGSLIEEIGGEADSKGISDRAQFNGRNLLDGSLDITLQVGA IIDGAINQVSEQRSGLGATQNRLDHTINNLSTSSENLTASESRIRDVDYALAA Flagellin
N-SEQ ID NO: 224
C-SEQ ID NO: 225
Aneurinibacillus sp.XH2
[CDS of SEQ ID NO: 75] MRINHNLPALNAYRNLAQNQIGTSKILERLSSGYRINRASDDAAGLAISEKMRGQIRGLEQGQRNTMDGVSLIQTAEGALQEIHEMLQRMRELAVQAANGTYSDKDKKAIEDEINQLTAQIDQIAKTTEFNGIQLIGDSDSTSLQDVK FKAAIDQVSRIRSYFGAIQNRLEHVVNNLSNYTENLTGAESRIRDADMAKEMTEFTRFNIINQSATAMLAQANQLPQGVLQLLKG

[0088] The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226-300 or any combination thereof.

[0089] The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise SEQ ID NO: 226.

[0090] The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 301-375 or any combination thereof.

[0091] The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise SEQ ID NO: 301.

[0092] A flagellin-derived Bt4Q7Flg22 polypeptide sequence (SEQ ID NO: 226) was identified in a proprietary internal library for Bacillus thuringiensis (Bt.), strain 4Q7. Conservative primers to full-length flagellin from E. coli were used to screen the library for strain Bt.4Q7 and identified a functional flagellin-associated bioactive Flg22 priming polypeptide.

Table 3 Identified Flg22 and FlgII-28 flagellin polypeptides from Bacillus spp.

SEQID NO: Peptide Flg22 Flg22-Bt.4Q7
SEQ ID NO: 226
bacillus thuringiensis,
strain 4Q7 DRLSSGKRINSASDDAAGLAIA Flg22
SEQ ID NO: 227
Bacillus thuringiensis strain
HD1002 DRLSSGKRINSASDDAAGLAIA Flg22
SEQ ID NO: 228
Bacillus thuringiensis strain
HD-789 DRLSSGKRINSASDDAAGLAIA Flg22
SEQ ID NO: 229
bacillus cereus,
strain G9842 DRLSSGKRINSASDDAAGLAIA Flg22
SEQ ID NO: 230
Bacillus thuringiensis, serovar indiana,
strain HD521 EHLATGKKLNNASDNPANIAIV Flg22
SEQ ID NO: 231
Bacillus thuringiensis strain CTC drlssgkrinnasddaaglaiat Flg22
SEQ ID NO: 232
bacillus
thuringiensis
yunnanensis serovar, strain IEBC-T20001 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 233
Bacillus thuringiensis, serovar tolworthi DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 234
Bacillus cereus strain FM1 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 235
Bacillus cereus strain FM1 EHLATGKKLNHASDNPANVAIV Flg22
SEQ ID NO: 236
Bacillus thuringiensis strain MC28 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 237
Bacillus bombysepticus
Wang strain DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 238
Bacillus thuringiensis, serovar kenyae DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 239
Bacillus thuringiensis, serovar kenyae DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 240
Bacillus cereus DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 241
Bacillus cereus EHLATGKKLNNASDNPANIAIV Flg22
SEQ ID NO: 242
Bacillus thuringiensis, serovar finitimus
strain YBT-020 EHLATGKKLNHASDNPANVAIV Flg22
SEQ ID NO: 243
Bacillus thuringiensis, serovar finitimus
strain YBT-020 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 244
Bacillus cereus strain B4264 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 245
Bacillus thuringiensis, serovar nigeriensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 246
Bacillus thuringiensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 247
Bacillus thuringiensis, serovar konkukian
strain 97-27 EHFATGKKLNHASDNPANVAIV Flg22
SEQ ID NO: 248
Bacillus thuringiensis, serovar konkukian
strain 97-27 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 249
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 EHLATGKKLNHASDNPANIIVIV Flg22
SEQ ID NO: 250
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 251
bacillus thuringiensis,
strain Bt407 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 252
Bacillus thuringiensis, serovar chinensis CT-43 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 253
Bacillus thuringiensis, serovar canadensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 254
Bacillus thuringiensis, serovar galleriae DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 255
Bacillus weihenstephanensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 256
Bacillus thuringiensis, serovar ostriniae DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 257
Bacillus thuringiensis EHLATGKKLNHASDNPANVAIV Flg22
SEQ ID NO: 258
Bacillus thuringiensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 259
Bacillus thuringiensis, serovar pondicheriensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 260
Bacillus thuringiensis, Berliner serovar EHLATGKKLNHASDNPANIIVIV Flg22
SEQ ID NO: 261
Bacillus thuringiensis, Berliner serovar DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 262
Bacillus cereus strain Q1 EHLATGKKLNHASNNPANVAIV Flg22
SEQ ID NO: 263
Bacillus cereus strain Q1 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 264
Bacillus thuringiensis, serovar morrisoni EHLATGKKLNHASDNPANIAIV Flg22
SEQ ID NO: 265
Bacillus thuringiensis, serovar neoleonensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 266
Bacillus thuringiensis, serovar morrisoni DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 267
Bacillus thuringiensis, serovar morrisoni DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 268
Bacillus thuringiensis, jegathesan serovar DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 269
Bacillus cereus strain ATCC 10987 DRLSSGKRINNASDDAAGLAIA Flg22 from flagellin A
SEQ ID NO: 270
Bacillus thuringiensis, serovar monterrey DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 271
Bacillus cereus strain NC7401 EHLATGKKLNNASDNPANIAIV Flg22
SEQ ID NO: 272
Bacillus cereus strain NC7401 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 273
Bacillus cereus strain AH820 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 274
Bacillus cereus AH187 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 275
Bacillus cereus DRLSSGKRINNASDDAAGLAIA
Flg22
SEQ ID NO: 276
Bacillus cereus DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 277
Bacillus thuringiensis
Strain HD-771 [51] DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 278
Bacillus thuringiensis, serovar sotto [52] DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 279
Bacillus thuringiensis, serovar Novosibirsk DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 280
Bacillus thuringiensis, serovar londrina DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 281
Bacillus cereus strain E33L EHLATGKKLNHASNNPANIAIV Flg22
SEQ ID NO: 282
Bacillus cereus strain E33L DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 283
bacillus cereus,
strain FRI-35 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 284
Bacillus cereus strain FRI-35 EHLATGKKLNNASDNPANIAIV Flg22
SEQ ID NO: 285
Bacillus thuringiensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 286
Bacillus cereus strain ATCC 4342 DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 287
Bacillus thuringiensis EHLATGKKLNHASDNPANIAIV Flg22
SEQ ID NO: 288
Bacillus thuringiensis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 289
Bacillus aryabhattai EKLSSGQRINSASDDAAGLAIS Flg22
SEQ ID NO: 290
Bacillus manliponensis NRLSSGKQINSASDDAAGLAIA Flg22
SEQ ID NO: 291
Lysinibacillus sp. strain BF-4 LRLSSGYRINSAADDAAGLAIS Flg22
SEQ ID NO: 292
Lysinibacillus sp. strain 13S34_air LRLSSGYRINSAADDAAGLAIS Flg22
SEQ ID NO: 293
Paenibacillus sp., strain HW567 GKLSSGLRINGASDDAAGLAIS Flg22
SEQ ID NO: 294
Bacillus anthracis DRLSSGKRINNASDDAAGLAIA Flg22
SEQ ID NO: 295
Bacillus anthracis NRLSSGKRINSAADDAAGLAIA Flg22
SEQ ID NO: 296
Bacillus anthracis NRLSSGKRINSAADDAAGLAIA Flg22
SEQ ID NO: 297
Bacillus anthracis NRLSSGKRINSAADDAAGLAIA Flg22
SEQ ID NO: 298
Bacillus anthracis strain H9401 NRLSSGKRINSAADDAAGLAIA Flg22
SEQ ID NO: 299
Bacillus megaterium strain WSH-002 EKLSSGQRINSASDDAAGLAIS Flg22
SEQ ID NO: 300
Aneurinibacillus sp.XH2 ERLSSGYRINRASDDAAGLAIS SEQID NO: Peptide Flg15 Flg15-Bt4Q7
SEQ ID NO: 752
Modified FLG15-Bt4Q7; Syn01
Bacillus thuringiensis strain 4Q7 RINSAKDDAAGLAIA

SEQID NO: Peptide FglI-28 FlgII-28-Bt.4Q7
SEQ ID NO: 301
bacillus thuringiensis,
strain 4Q7 SVSNILLRMRDLANQSANGTNTKGNQAS FlgII-28
SEQ ID NO: 302
Bacillus thuringiensis strain
HD1002 SVSNILLRMRDLANQSANGTNTKGNQAS FlgII-28
SEQ ID NO: 303
Bacillus thuringiensis strain
HD-789 SVSNILLRMRDLANQSANGTNTKGNQAS FlgII-28
SEQ ID NO: 304
bacillus cereus,
strain G9842 SVSNILLRMRDLANQSANGTNTKGNQAS FlgII-28
SEQ ID NO: 305
Bacillus thuringiensis, serovar indiana,
strain HD521 TVTNILQRMRDLAVQSANGTNSNKNRHS FlgII-28
SEQ ID NO: 306
Bacillus thuringiensis strain CTC svsnillrmrdianqsanItntnenksa FlgII-28
SEQ ID NO: 307
bacillus
thuringiensis,
yunnanensis serovar, strain IEBC-T20001 SVSNILLRMRDLANQSANGTNTDDNQKA FlgII-28
SEQ ID NO: 308
Bacillus thuringiensis, serovar tolworthi SVSNILLRMRDLANQSANGTNTDENKAA FlgII-28
SEQ ID NO: 309
Bacillus cereus strain FM1 SVSNILLRMRDIANQSANGTNTDKNQVA FlgII-28
SEQ ID NO: 310
Bacillus cereus strain FM1 TVTNILQRMRDVAVQSANGTNSNKNRDS FlgII-28
SEQ ID NO: 311
Bacillus thuringiensis strain MC28 SVSNILLRMRDIANQSANGTNTADNQQA FlgII-28
SEQ ID NO: 312
Bacillus bombysepticus strain Wang SVSNILLRMRDLANQSASGTNTDKNQAA FlgII-28
SEQ ID NO: 313
Bacillus thuringiensis, serovar kenyae SVSNILLRMRDLANQSASGTNTDKNQAA FlgII-28
SEQ ID NO: 314
Bacillus thuringiensis, serovar kenyae SVSNILLRMRDLANQSASGTNTDKNQAA FlgII-28
SEQ ID NO: 315
Bacillus cereus SVSNILLRMRDLANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 316
Bacillus cereus TNILQRMRDLAVQSANGTNSNKNRDSLN FlgII-28
SEQ ID NO: 317
Bacillus thuringiensis, serovar finitimus,
strain YBT-020 TNVLQRMRDVAVQSANGTNLNKNRDSLN FlgII-28
SEQ ID NO: 318
Bacillus thuringiensis, serovar finitimus,
strain YBT-020 SVSNILLRMRDIANQSANGTNTDSNKSA FlgII-28
SEQ ID NO: 319
Bacillus cereus strain B4264 SVSNILLRMRDLANQSANGTNTAENKAAA FlgII-28
SEQ ID NO: 320
Bacillus thuringiensis, serovar nigeriensis SVSNILLRMRDIANQSANGTNTSDNQKA FlgII-28
SEQ ID NO: 321
Bacillus thuringiensis SVSNILLRMRDIANQSANGTNTADNQQA FlgII-28
SEQ ID NO: 322
Bacillus thuringiensis, serovar konkukian,
strain 97-27 TVMNILQRMRDLAVQSANGTNSNKNRDS FlgII-28
SEQ ID NO: 323
Bacillus thuringiensis, serovar konkukian,
strain 97-27 SVSNILLRMRDIANQSANGTNTADNQQA FlgII-28
SEQ ID NO: 324
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 TVTNILQHMRDFAIQSANGTNSNTNRDS FlgII-28
SEQ ID NO: 325
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 SVSNILLRMRDISNQSANGTNTDKNQSA FlgII-28
SEQ ID NO: 326
bacillus thuringiensis,
strain Bt407 SVSNILLRMRDISNQSANGTNTDKNQSA FlgII-28
SEQ ID NO: 327
Bacillus thuringiensis, serovar chinensis CT-43 SVSNILLRMRDISNQSANGTNTDKNQSA FlgII-28
SEQ ID NO: 328
Bacillus thuringiensis, serovar canadensis SVSNILLRMRDLANQSANGTNTNENQAA FlgII-28
SEQ ID NO: 329
Bacillus thuringiensis, serovar galleriae SVSNILLRMRDLANQSANGTNTNENQAA FlgII-28
SEQ ID NO: 330
Bacillus weihenstephanensis SVSNILLRMRDLSNQSANGTNTDENQQA FlgII-28
SEQ ID NO: 331
Bacillus thuringiensis, serovar ostriniae SVSNILLRMRDIANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 332
Bacillus thuringiensis TVANILQRMRDLAVQSSNDTNSNKNRDS FlgII-28
SEQ ID NO: 333
Bacillus thuringiensis SVSNILLRMRDLANQSANGTNTDDNQKA FlgII-28
SEQ ID NO: 334
Bacillus thuringiensis, serovar pondicheriensis SVSNILLRMRDLANQSANGTNTDDNQKA FlgII-28
SEQ ID NO: 335
Bacillus thuringiensis, Berliner serovar TVTNILQHMRDFAIQSANGTNSNTNRDS FlgII-28
SEQ ID NO: 336
Bacillus thuringiensis, Berliner serovar SVSNILLRMRDISNQSANGTNTDKNQSA FlgII-28
SEQ ID NO: 337
Bacillus cereus strain Q1 TVTNVLQRMRDVAVQSANGTNSSKNRDS FlgII-28
SEQ ID NO: 338
Bacillus cereus strain Q1 SVSNILLRMRDIANQSANGTNTDKNQVA FlgII-28
SEQ ID NO: 339
Bacillus thuringiensis, serovar morrisoni TVMNILQRMRDLAIQSANSTNSNKNRDS FlgII-28
SEQ ID NO: 340
Bacillus thuringiensis, serovar neoleonensis SVSNILLRMRDIANQSANGTNTSDNQKA FlgII-28
SEQ ID NO:341
Bacillus thuringiensis, serovar morrisoni SVSNILLRMRDIANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 342
Bacillus thuringiensis, serovar morrisoni SVSNILLRMRDIANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 343
Bacillus thuringiensis, jegathesan serovar SVSNILLRMRDIANQSANGTNTNGNQAA FlgII-28
SEQ ID NO: 344
Bacillus cereus strain ATCC 10987 SVSNILLRMRDIANQSANGTNTDKNQAA FlgII-28 from flagellin A
SEQ ID NO: 345
Bacillus thuringiensis, serovar monterrey SVSNILLRMRDLANQSANGTNTNENQAA FlgII-28
SEQ ID NO: 346
Bacillus cereus strain NC7401 TVTNVLQRMRDLAVQSANDTNSNKNRDS FlgII-28
SEQ ID NO: 347
Bacillus cereus strain NC7401 SVSNILLRMRDLANQSANGTNTNENKAA FlgII-28
SEQ ID NO: 348
Bacillus cereus strain AH820 SVSNILLRMRDLANQSANGTNTSDNQAA FlgII-28
SEQ ID NO: 349
Bacillus cereus AH187 SVSNILLRMRDLANQSANGTNTNENKAA FlgII-28
SEQ ID NO: 350
Bacillus cereus SVSNILLRMRDLANQSANGTNTNENKAA FlgII-28
SEQ ID NO: 351
Bacillus cereus SVSNILLRMRDIANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 352
bacillus thuringiensis,
strain HD-771 [51] SVSNILLRMRDLANQSASETNTSKNQAA FlgII-28
SEQ ID NO: 353
Bacillus thuringiensis, serovar sotto [52] SVSNILLRMRDLANQSASETNTSKNQAA FlgII-28
SEQ ID NO: 354
Bacillus thuringiensis, serovar Novosibirsk SVSNILLRMRDIANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 355
Bacillus thuringiensis, serovar londrina SVSNILLRMRDLANQSANGTNTSENQAA FlgII-28
SEQ ID NO: 356
Bacillus cereus strain E33L TVTNILQRMRDLAVQSANVTNSNKNRNS FlgII-28
SEQ ID NO: 357
Bacillus cereus strain E33L SVSNILLRMRDLANQSANGTNTDKNQGA FlgII-28
SEQ ID NO: 358
bacillus cereus,
strain FRI-35 SVSNILLRMRDLANQSANGTNTDKNQAA FlgII-28
SEQ ID NO: 359
Bacillus cereus strain FRI-35 TVTNVLQRMRDLAVQSANGTNSNKNRDS FlgII-28
SEQ ID NO: 360
Bacillus thuringiensis SVSNILLRMRDIANQTANGTNKDTDIEA FlgII-28
SEQ ID NO: 361
Bacillus cereus strain ATCC 4342 SVSNILLRMRDIANQTANGTNKDTDIEA FlgII-28
SEQ ID NO: 362
Bacillus thuringiensis TVMNILQRMRDLAIQSANSTNSNKNRDS FlgII-28
SEQ ID NO: 363
Bacillus thuringiensis SVSNILLRMRDIANQSANGTNTGDNQKA FlgII-28
SEQ ID NO: 364
Bacillus aryabhattai ETHDILQRMRELVVQAGNGTNKTEDLDA FlgII-28
SEQ ID NO: 365
Bacillus manliponensis SVSNILLRMRDLATQSATGTNQGNDRES FlgII-28
SEQ ID NO: 366
Lysinibacillus sp., strain BF-4 ETHAIVQRMRELAVQAATDTNTDDDRAK FlgII-28
SEQ ID NO: 367
Lysinibacillus sp., strain 13S34_air ETHAIVQRMRELAVQAATDTNTDDDRAK FlgII-28
SEQ ID NO: 368
Paenibacillus sp., strain HW567 EIHSMLQRMNELAVQASNGTYSGSDRLN FlgII-28
SEQ ID NO: 369
Bacillus anthracis SVSNILLRMRDLANQSANGTNTKENQDA FlgII-28
SEQ ID NO: 370
Bacillus anthracis SVSNILTRMRDIAVQSSNGTNTAENQSA FlgII-28
SEQ ID NO: 371
Bacillus anthracis SVSNILTRMRDIAVQSSNGTNTAENQSA FlgII-28
SEQ ID NO: 372
Bacillus anthracis SVSNILTRMRDIAVQSSNGTNTAENQSA FlgII-28
SEQ ID NO: 373
Bacillus anthracis strain H9401 SVSNILTRMRDIAVQSSNGTNTAENQSA FlgII-28
SEQ ID NO: 374
Bacillus megaterium strain WSH-002 ETHDILQRMRELVVQAGNGTNKTEDLDA FlgII-28
SEQ ID NO: 375
Aneurinibacillus sp.XH2 EIHEMLQRMRELAVQAANGTYSDKDKKA

Retro-inverse flagellin-associated polypeptides

[0093] The bioactive Flg polypeptide or polypeptides suitable for priming can be obtained in a non-naturally occurring isomeric or retro-inverse (RI) form.

[0094] Retro-inverse Flg polypeptides may exhibit improved binding affinity for the FLS receptor protein or proteins. Plant flagellin receptors, such as FLS2, are able to recognize a fragment of a retro-inverse Flg polypeptide, such as Flg22 or FlgII-28, located in the N-terminal conserved domain of flagellin. Retro-inverse forms of these Flg polypeptides have been proposed as biologically active forms capable of recognizing and interacting with the Flg-associated or FLS-receptor protein on the membrane surface of plant cells.

[0095] Retro-inverse Flg polypeptides may have increased activity and stability against proteolytic degradation at the plant membrane surface. For example, retro-inverse forms of Bacillus Flg22 or FlgII-28 polypeptides can increase the activity and stability of the Flg polypeptide or polypeptides and increase protection against proteolytic degradation on the plant surface or root surface. These retro-inverse forms also show improved stability when applied in the field, or in soil or soil.

[0096] Retro-inverse polypeptides are topological mirror-symmetrical forms of the natural structure of the original polypeptide. Retro-inverse synthetic forms of polypeptide sequences are formed by reversing the direction of rotation of the polypeptide sequences and using fully D-retropeptides or retro-enantio-peptides. The Flg polypeptide or polypeptides containing an entire D-amino acid chain take a form that is a "mirror image" of the three-dimensional structure of the corresponding L-peptide or L-amino acid chain.

[0097] This is further accomplished by retro-inverting any of the original Flg polypeptides derived from Bacillus or other eubacteria in Table 3. Designed retro-inverse polypeptides for Flg22 (RI Flg22: SEQ ID NO: 376-450) and FlgII-28 (RI-FlgII-28: SEQ ID NO: 451-525) are shown in Table 4. The retro inverse forms of Ec.Flg22 (SEQ ID NO: 526) and EcFlg15 (SEQ ID NO: 529) shown in Table 5 were also created from E. coli-derived sequences.

[0098] Said polypeptide may include a retro inverse Flg22 polypeptide.

[0099] Said polypeptide may include a retro inverse FlgII-28 polypeptide.

[0100] Any of the flagellin-associated bioactive priming polypeptides contained in Bacillus, or other eubacterial Flg22 or FlgII-28 polypeptides of Table 3, can be used in retro-inverse forms (shown in Table 4).

[0101] The retro-inverse forms of the bioactive Flg priming polypeptides of this document can be any of three forms, where the amino acid chirality inversion includes the normal all-D form (inverse), the all-L-form (retro), and/or the all-D-retro form (retro-inverse), or a combination of these forms to achieve the desired phenotypes in the plant.

[0102] Bacillus-derived L-Flg22 and L-FlgII-28 polypeptides in Table 3 and naturally occurring E.c. L-Flg22 and L-Flg15 in Table 5 were synthetically generated by retro-inverse engineering to form a retro-inverse polypeptide D-Flg22 (SEQ ID NO: 376-450), D-FlgII-28 (SEQ ID NO: 451-525 ) and an E.c. D-Flg22 (SEQ ID NO: 527, 529).

[0103] The inversion of the amino acid chirality (from all-L to all-D) for Bt.4Q7 Flg22 (SEQ ID NO: 376) proposed as a small linear polypeptide fragment, termed retro-inverse modification, was achieved by reversing the direction of the polypeptide backbone described below.

( ^D A ^D IA ^D L ^D G ^D A ^D A ^D D ^D D ^D S ^D A ^D S ^D N ^D I ^D R ^D K ^D G ^D S ^D S ^D L ^D R ^D D)

[0104] The all-D amino acid chain retro-inverse Flg22 polypeptide adopts a "mirror" structure to the three-dimensional structure of the related natural L-Bt.4Q7 Flg 22 polypeptide, and said all-L chain is an equivalent mirror image of the all-D Bt polypeptide .4Q7 Flg22. All L-amino acid residues are replaced by their D-enantiomers, resulting in all-D-peptides or all-D-peptide retroisomers containing amide linkages. The natural L-amino acid form of the Bt.4Q7 Flg22 polypeptide chain is reversed to a synthetic retro-inverse all-D conformation by replacing all L-amino acid residues with the corresponding D-enantiomers.

[0105] In FIG. 1 is a diagram depicting native (all-L) Bt.4Q7 Flg22 and its retro-inverse or mirror image, producing the all-D-enantiomeric Bt.4Q7 Flg22 polypeptide. The retro inverse Flg polypeptide corresponding to Bt.4Q7 Flg22 (SEQ ID NO: 226) is listed as SEQ ID NO: 376.

[0106] In the case of short polypeptides such as Flg22, Flg15, and FlgII-28, mirroring side chain positions upon conformational change from L to D results in mirror-symmetrical transformations of the side chains as well.

[0107] Completely D-retro analogs have been found to have biological activity (Guptasarma, “Reversal of peptide backbone direction may result in mirroring of protein structure, FEBS Letters 310: 205-210, 1992). A retro-inverse D-Flg polypeptide or polypeptides may have a side chain topology in an extended conformation similar to the corresponding sequence of a natural L-Flg polypeptide, thus mimicking the biological activity of the original natural L-molecule, while being completely resistant to proteolytic degradation, thereby increasing the stability upon contact of the polypeptide with the plant or the environment.

[0108] The retro-inverse bioactive Flg priming polypeptides are described in Table 4 or Table 5. The retro-inverse Flg-associated bioactive priming polypeptides shown in Table 4 were selected for enhanced potency and stability, as well as the ability to tolerate varying conditions and environments. . Due to their D-enantiomeric nature, they are more resistant to proteolytic degradation and can tolerate and survive in harsher environmental conditions.

Table 4. Retro-inverse flagellin polypeptides Flg22 and FlgII-28 from Bacillus

SEQID NO: Peptide Flg22 RI Bt.4Q7Flg22
SEQ ID NO: 376
bacillus thuringiensis,
strain 4Q7 AIALGAADDSASNIRKGSSLRD RI Flg22
SEQ ID NO: 377
Bacillus thuringiensis strain
HD1002 AIALGAADDSASNIRKGSSLRD RI Flg22
SEQ ID NO: 378
Bacillus thuringiensis strain
HD-789 AIALGAADDASNIRKGSSLRD RI Flg22
SEQ ID NO: 379
bacillus cereus,
strain G9842 AIALGAADDSASNIRKGSSLRD RI Flg22
SEQ ID NO: 380
Bacillus thuringiensis, serovar indiana,
strain HD521 VIANAPNDSANNLKKGTALHE RI Flg22
SEQ ID NO: 381
Bacillus thuringiensis strain CTC TAIAGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 382
bacillus thuringiensis,
yunnanensis serovar, strain IEBC-T20001 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 383
Bacillus thuringiensis, serovar tolworthi AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 384
Bacillus cereus strain FM1 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 385
Bacillus cereus strain FM1 VIAVNAPNDSAHNLKKGTALHE RI Flg22
SEQ ID NO: 386
Bacillus thuringiensis strain MC28 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 387
bacillus bombysepticus,
Wang strain AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 388
Bacillus thuringiensis, serovar kenyae AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 389
Bacillus thuringiensis, serovar kenyae AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 390
Bacillus cereus AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 391
Bacillus cereus VIAINAPNDASNNLKKGTALHE RI Flg22
SEQ ID NO: 392
Bacillus thuringiensis, serovar finitimus,
strain YBT-020 VIANAPNDSAHNLKKGTALHE RI Flg22
SEQ ID NO: 393
Bacillus thuringiensis, serovar finitimus,
strain YBT-020 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 394
Bacillus cereus strain B4264 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 395
Bacillus thuringiensis, serovar nigeriensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 396
Bacillus thuringiensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 397
Bacillus thuringiensis, serovar konkukian,
strain 97-27 VIANAPNDSAHNLKKGTAFHE RI Flg22
SEQ ID NO: 398
Bacillus thuringiensis, serovar konkukian,
strain 97-27 AIALGAADDSANNRKGSSLRD RI Flg22
SEQ ID NO: 399
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 VIVINAPNDSAHNLKKGTALHE RI Flg22
SEQ ID NO: 400
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 401
Bacillus thuringiensis
strain Bt407 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 402
Bacillus thuringiensis, serovar chinensis CT-43 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 403
Bacillus thuringiensis, serovar canadensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 404
Bacillus thuringiensis, serovar galleriae AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 405
Bacillus weihenstephanensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 406
Bacillus thuringiensis, serovar ostriniae AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 407
Bacillus thuringiensis VIANAPNDSAHNLKKGTALHE RI Flg22
SEQ ID NO: 408
Bacillus thuringiensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 409
Bacillus thuringiensis, serovar pondicheriensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 410
Bacillus thuringiensis, Berliner serovar VIVINAPNDASHNLKKGTALHE RI Flg22
SEQ ID NO: 411
Bacillus thuringiensis, Berliner serovar AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 412
Bacillus cereus strain Q1 VIAVANPNNSAHNLKKGTALHE RI Flg22
SEQ ID NO: 413
Bacillus cereus strain Q1 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 414
Bacillus thuringiensis, serovar morrisoni VIANAPNDSAHNLKKGTALHE RI Flg22
SEQ ID NO: 415
Bacillus thuringiensis, serovar neoleonensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 416
Bacillus thuringiensis, serovar morrisoni AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 417
Bacillus thuringiensis, serovar morrisoni AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 418
Bacillus thuringiensis, jegathesan serovar AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 419
Bacillus cereus strain ATCC 10987 AIALGAADDSANNIRKGSSLRD RI Flg22 from flagellin A
SEQ ID NO: 420
Bacillus thuringiensis, serovar monterrey AIALGAADDASNNIRKGSSLRD RI Flg22
SEQ ID NO: 421
Bacillus cereus strain NC7401 VIANAPNDSANNLKKGTALHE RI Flg22
SEQ ID NO: 422
Bacillus cereus strain NC7401 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 423
Bacillus cereus strain AH820 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 424
Bacillus cereus AH187 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 425
Bacillus cereus AIALGAADDSANNIRKGSSLRD
RI Flg22
SEQ ID NO: 426
Bacillus cereus AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO:427
Bacillus thuringiensis strain HD-771 [51] AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 428
Bacillus thuringiensis, serovar sotto [52] AIALGAADDANNIRKGSSLRD RI Flg22
SEQ ID NO: 429
Bacillus thuringiensis, serovar Novosibirsk AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 430
Bacillus thuringiensis, serovar londrina AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 431
Bacillus cereus strain E33L VIAINAPNNSAHNLKKGTALHE RI Flg22
SEQ ID NO: 432
Bacillus cereus strain E33L AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO:433
Bacillus cereus strain FRI-35 AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 434
Bacillus cereus strain FRI-35 VIAINAPNDSANNLKKGTALHE RI Flg22
SEQ ID NO: 435
Bacillus thuringiensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 436
Bacillus cereus strain ATCC 4342 AIALGAADDANNIRKGSSLRD RI Flg22
SEQ ID NO:437
Bacillus thuringiensis VIANAPNDSAHNLKKGTALHE RI Flg22
SEQ ID NO:438
Bacillus thuringiensis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 439
Bacillus aryabhattai SIALGAADDSASNIRQGSSLKE RI Flg22
SEQ ID NO: 440
Bacillus manliponensis AIALGAADDSASNIQKGSSLRN RI Flg22
SEQ ID NO:441
Lysinibacillus sp., strain BF-4 SIALGAADDAASNIRYGSSLRL RI Flg22
SEQ ID NO:442
Lysinibacillus sp., strain 13S34_air SIALGAADDAASNIRYGSSLRL RI Flg22
SEQ ID NO: 443
Paenibacillus sp., strain HW567 SIAGLAADDSAGNIRLGSSLKG RI Flg22
SEQ ID NO:444
Bacillus anthracis AIALGAADDSANNIRKGSSLRD RI Flg22
SEQ ID NO: 445
Bacillus anthracis AIALGAADDAASNIRKGSSLRN RI Flg22
SEQ ID NO:446
Bacillus anthracis AIALGAADDAASNIRKGSSLRN RI Flg22
SEQ ID NO:447
Bacillus anthracis AIALGAADDAASNIRKGSSLRN RI Flg22
SEQ ID NO:448
Bacillus anthracis strain H9401 AIALGAADDAASNIRKGSSLRN RI Flg22
SEQ ID NO:449
Bacillus megaterium strain WSH-002 SIALGAADDSASNIRQGSSLKE RI Flg22
SEQ ID NO: 450
Aneurinibacillus sp.XH2 SIALGAADDSARNIRYGSSLRE SEQID NO: Peptide Flg15 RI Flg15-Bt4Q7
SEQ ID NO: 767
Modified FLG15-Bt4Q7; Syn01
Bacillus thuringiensis strain 4Q7 AIALGAADDKASNIR

SEQID NO: Peptide FlgII-28 RI FlgII-28-Bt.4Q7
SEQ ID NO:451
Bacillus thuringiensis
strain 4Q7 SAQNGKTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 452
Bacillus thuringiensis strain
HD1002 SAQNGKTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 453
Bacillus thuringiensis strain
HD-789 SAQNGKTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 454
Bacillus cereus strain G9842 SAQNGKTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 455
Bacillus thuringiensis, indiana serovar, strain HD521 SHRNKNSNTGNASQVALDRMRQLINTVT RI FlgII-28
SEQ ID NO:456
Bacillus thuringiensis strain CTC ASKNENTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO:457
Bacillus thuringiensis, serovar yunnanensis, strain IEBC-T20001 AKQNDDTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 458
Bacillus thuringiensis, serovar tolworthi AAKNEDTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO:459
Bacillus cereus strain FM1 LAVQNKDTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 460
Bacillus cereus strain FM1 SDRNKNSNTGNASQVAVDRMRQLINTVT RI FlgII-28
SEQ ID NO:461
Bacillus thuringiensis strain MC28 AQQNDATNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 462
Bacillus bombysepticus strain Wang AAQNKDTNTGSASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 463
Bacillus thuringiensis, serovar kenyae AAQNKDTNTGSASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 464
Bacillus thuringiensis, serovar kenyae AAQNKDTNTGSASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 465
Bacillus cereus AKQNDGTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 466
Bacillus cereus NLSDRNKNSNTGNASQVALDRMRQLINT RI FlgII-28
SEQ ID NO:467
Bacillus thuringiensis, serovar finitimus,
strain YBT-020 NLSDRNKNLNTGNASQVAVDRMRQLVNT RI FlgII-28
SEQ ID NO:468
Bacillus thuringiensis, serovar finitimus,
strain YBT-020 ASKNSDTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 469
Bacillus cereus strain B4264 AAKNEATNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 470
Bacillus thuringiensis, serovar nigeriensis AKQNDSTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO:471
Bacillus thuringiensis AQQNDATNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO:472
Bacillus thuringiensis, serovar konkukian,
strain 97-27 SDRNKNSNTGNASQVALDRMRQLINMVT RI FlgII-28
SEQ ID NO: 473
Bacillus thuringiensis, serovar konkukian,
strain 97-27 AQQNDATNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 474
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 SDRNTNSNTGNASQIAFDRMHQLINTVT RI FlgII-28
SEQ ID NO: 475
Bacillus thuringiensis, serovar thuringiensis, strain IS5056 ASQNKDTNTGNASQNSIDRMRLLINSVS RI FlgII-28
SEQ ID NO:476
Bacillus thuringiensis strain Bt407 ASQNKDTNTGNASQNSIDRMRLLINSVS RI FlgII-28
SEQ ID NO:477
Bacillus thuringiensis, serovar chinensis CT-43 ASQNKDTNTGNASQNSISRMRLLINSVS RI FlgII-28
SEQ ID NO: 478
Bacillus thuringiensis, serovar canadensis AAQNENTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 479
Bacillus thuringiensis, serovar galleriae AQQNEDTNTGNASQNSLDRMRLLINSVS RI FlgII-28
SEQ ID NO: 480
Bacillus weihenstephanensis AQQNEDTNTGNASQNSLDRMRLLINSVS RI FlgII-28
SEQ ID NO: 481
Bacillus thuringiensis, serovar ostriniae AKQNDGTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 482
Bacillus thuringiensis SDRNKNSNTDNSSQVALDRMRQLINAVT RI FlgII-28
SEQ ID NO:483
Bacillus thuringiensis AKQNDDTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 484
Bacillus thuringiensis, serovar pondicheriensis AKQNDDTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 485
Bacillus thuringiensis, Berliner serovar SDRNTNSNTGNASQIAFDRMHQLINTVT RI FlgII-28
SEQ ID NO: 486
Bacillus thuringiensis, Berliner serovar ASQNKDTNTGNASQNSIDRMRLLINSVS RI FlgII-28
SEQ ID NO:487
Bacillus cereus strain Q1 SDRNKSSNTGNASQVAVDRMRQLVNTVT RI FlgII-28
SEQ ID NO: 488
Bacillus cereus strain Q1 AVQKDTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 489
Bacillus thuringiensis, serovar morrisoni SDRNKNSNTSNASQIALDRMRQLINMVT RI FlgII-28
SEQ ID NO: 490
Bacillus thuringiensis, serovar neoleonensis AKQNDSTNIGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO:491
Bacillus thuringiensis, serovar morrisoni AKQNDGTNTFNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 492
Bacillus thuringiensis, serovar morrisoni AKQNDGTNTFNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 493
Bacillus thuringiensis, jegathesan serovar AAQNGNTNTFNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 494
Bacillus cereus strain ATCC 10987 AAQNKDTNTGNASQNAIDRMRLLINSVS RI FlgII-28 from flagellin A
SEQ ID NO: 495
Bacillus thuringiensis, serovar monterrey AAQNENTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 496
Bacillus cereus strain NC7401 SDRNKNSNTDNASQVALDRMRQLVNTVT RI FlgII-28
SEQ ID NO: 497
Bacillus cereus strain NC7401 AAKNENTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 498
Bacillus cereus strain AH820 AAQNDSTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 499
Bacillus cereus AH187 AAKNENTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 500
Bacillus cereus AAKNENTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 501
Bacillus cereus AKQNDGTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 502
Bacillus thuringiensis strain HD-771 [51] AAQNKSTNTESASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 503
Bacillus thuringiensis, serovar sotto [52] AAQNKSTNTESASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 504
Bacillus thuringiensis, serovar Novosibirsk AKQNDGTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 505
Bacillus thuringiensis, serovar londrina AAQNESTNTGNAQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 506
Bacillus cereus strain E33L SNRNKNSNTVNASQVALDRMRQLINTVT RI FlgII-28
SEQ ID NO: 507
Bacillus cereus strain E33L AGQNKDTNTNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 508
Bacillus cereus strain FRI-35 AAQNKDTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 509
Bacillus cereus strain FRI-35 SDRNKNSNTGNASQVALDRMRQLVNTVT RI FlgII-28
SEQ ID NO: 510
Bacillus thuringiensis AEIDTDKNTGNATQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 511
Bacillus cereus strain ATCC 4342 AEIDTDKNTGNATQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 512
Bacillus thuringiensis SDRNKNSNTSNASQIALDRMRQLINMT RI FlgII-28
SEQ ID NO: 513
Bacillus thuringiensis AKQNDGTNTGNASQNAIDRMRLLINSVS RI FlgII-28
SEQ ID NO: 514
Bacillus aryabhattai ADLDETKNTGNGAQVVLERMRQLIDHTE RI FlgII-28
SEQ ID NO: 515
Bacillus manliponensis SERDNGQNTGTAQTALDRRMRLLINSVS RI FlgII-28
SEQ ID NO: 516
Lysinibacillus sp., strain BF-4 KARDDDTNTDTAAQVALERMRQVIAHTE RI FlgII-28
SEQ ID NO: 517
Lysinibacillus sp., strain 13S34_air KARDDDTNTDTAAQVALERMRQVIAHTE RI FlgII-28
SEQ ID NO: 518
Paenibacillus sp., strain HW567 NLRDSGSYTGNSAQVALENMRQLMSHIE RI FlgII-28
SEQ ID NO: 519
Bacillus anthracis ADQNEKTNTGNASQNALDRMRLLINSVS RI FlgII-28
SEQ ID NO: 520
Bacillus anthracis ASQNEATNTGNSSQVAIDRMRTLINSVS RI FlgII-28
SEQ ID NO: 521
Bacillus anthracis ASQNEATNTGNSSQVAIDRMRTLINSVS RI FlgII-28
SEQ ID NO: 522
Bacillus anthracis ASQNEATNTGNSSQVAIDRMRTLINSVS RI FlgII-28
SEQ ID NO: 523
Bacillus anthracis strain H9401 ASQNEATNTGNSSQVIADRMRTLINSVS RI FlgII-28
SEQ ID NO: 524
Bacillus megaterium strain WSH-002 ADLDETKNTGNGAQVVLERMRQLIDHTE RI FlgII-28
SEQ ID NO: 525
Aneurinibacillus sp.XH2 AKKDKSYTGNAAQVALERMRQLMEHIE

Flg sequences from various organisms

Table 5. Flagellin-associated Flg22 and Flg15 polypeptides from other organisms

SEQID NO: Peptide - amino acids Flagellin (Flg22)
SEQ ID NO: 526
Escherichia coli ERLSSGLRINSAKDDAAGQAIA Flagellin (Retro Inverse Flg22)
SEQ ID NO: 527
Escherichia coli AIAQGAADDKASNIRLGSSLRE Flagellin (Flg15)
SEQ ID NO: 528
Escherichia coli RINSAKDDAAGQAIA Flagellin (Retro Inverse Flg15)
SEQ ID NO: 529
Escherichia coli AIAQGAADDKASNIR Flagellin (Flg22)
SEQ ID NO: 530
Pseudomonas aeruginosa QRLSTGSRINSAKDDAAGLQIA Flagellin (Retro Inverse Flg22)
SEQ ID NO: 531
Pseudomonas aeruginosa AIQLGAADDKASNIRSGTSLRQ Flagellin (Flg22)
SEQ ID NO: 532
Xanthomonas spp.
X. campestris and X. citri QRLSSGLRINSAKDDAAGLAIS Flagellin (Retro Inverse Flg22)
SEQ ID NO: 533
Xanthomonas spp.
X. campestris and X. citri SIALGAADDKASNIRLGSSLLRQ Flagellin (Flg22)
SEQ ID NO: 534
Erwinia amylovora QRLSSGLRINSAKDDAAGQAIS Flagellin (Retro Inverse Flg22)
SEQ ID NO: 535
Erwinia amylovora SIAQGAADDKASNIRLGSSLLRQ Flagellin (Flg22)
SEQ ID NO: 536
Burkholderia phytofirmans TRLSSGKRINSAADDAAGLAIS Flagellin (Retro Inverse Flg22)
SEQ ID NO: 537
Burkholderia phytofirmans SIALGAADDAASNIRKGSSLRT Flagellin (Flg22)
SEQ ID NO: 538
Burkholderia ubonensis NRLSSGKRINTAADDAAGLAIS Flagellin (Retro Inverse Flg22)
SEQ ID NO: 539
Burkholderia ubonensis SIALGAADDAATNIRKGSSLRN Flagellin (Flg22)
SEQ ID NO: 540
Pseudomonas syringae TRLSSGLKINSAKDDAAGLQIA Flagellin (Retro Inverse Flg22)
SEQ ID NO: 541
Pseudomonas syringae AIQLGAADDKASNIKLGSSLRT Flagellin (FlgII-28)
(SEQ ID NO: 751)
Pseudomonas syringae ESTNILQRMRELAVQSRNDSNSATDREA Flagellin (Retro Inverse FlgII-28)
(SEQ ID NO: 768)
Pseudomonas syringae AERDTASNSDNRSQVALERMRQLINTSE

Sequences to facilitate the targeting of flagellins or flagellin-associated polypeptides into the plant

[0109] Signature sequences, signal anchor sorting sequences, and secretion sequences can be used alone or together in combination with any of the flagellin or flagellin-associated polypeptides as described herein. These accessory sequences are suitable for efficient delivery of flagellin polypeptides to the membrane surface of plant cells. Other accessory sequences may also assist in the translocation of the Flg polypeptide fragment across the plasma membrane. Delivery of flagellins and flagellin-associated polypeptides to the plasma membrane surface of a plant (or plant part) can contribute to subsequent signaling processes and lead to favorable outcomes for the plant or plant part, such as improved health and increased plant productivity.

[0110] The specified polypeptide may additionally contain an auxiliary polypeptide.

[0111] The specified auxiliary polypeptide may contain a signature polypeptide, while the amino acid sequence of the specified signature polypeptide may contain any of SEQ ID NO: 542-548, shown in table 6, or any combination thereof. For example, the amino acid sequence of said signature polypeptide may comprise SEQ ID NO: 542.

[0112] Said accessory polypeptide may comprise a signal anchor sort polypeptide, and the amino acid sequence of said signal anchor sort polypeptide may comprise any of SEQ ID NOs: 549-562 shown in Table 7, or any combination thereof. For example, the amino acid sequence of said signal anchor sort polypeptide may comprise SEQ ID NO: 549.

[0113] The specified flagellin or flagellin-associated polypeptide can be obtained in a recombinant way using a microorganism. For example, said microorganism may include Bacillus, Pseudomonas, Paenibacillus, Aneurinibacillus, or Lysinibacillus.

[0114] The specified auxiliary polypeptide may contain a secretion polypeptide, while the amino acid sequence of the specified secretion polypeptide may contain any of SEQ ID NO: 563-570, or any combination thereof. For example, the amino acid sequence of said secretion polypeptide may comprise SEQ ID NO: 563.

[0115] These three types of auxiliary sequences are further described in Table 6 (N-terminal Signature Sequences), Table 7 (Signal Anchor Sorting Sequences), and Table 8 (Secretion Sequences).

[0116] Also provided are "helper" sequences containing conserved signature (Table 6; SEQ ID NOs: 542-548), signal anchor sorting sequences (Table 7; SEQ ID NOs: 549-562), and secretion sequences (Table 8; SEQ ID NO: 563-570) in combination with any of the flagellin-associated polypeptides as described herein. In particular, combinations of auxiliary signature, signal anchor sorting and secretion sequences with natural Flg L-polypeptides (Table 3. SEQ ID NOs: 226-375) or any of the retro-inverse Flg22 polypeptides (Table 4. SEQ ID NOs: 226-375) are suitable. 376-525) to ensure efficient delivery of Flg polypeptides to the extracellular surface of the plant membrane, such as the surface of a plant or plant part.

N-terminal signature sequences

[0117] "Signature" amino acid sequences conserved in the bacteria (genus) Bacillus, Lysinibacillus, Paenibacillus or Aneurinibacillus, and other eubacterial genera may be involved in targeting flagellin polypeptides to the appropriate Flg-associated receptor protein or proteins, such as FLS receptors containing a binding site exposed on the surface of the plant cell membrane, and can be used to improve the binding of the Flg polypeptide and the receptor, providing an increased potential for activation of the Flg-associated receptor or receptors. The flagellin signature sequences identified in Table 6 are suitable for targeting and stable delivery of Flg polypeptides for binding to FLS or FLS-like(s) receptor(s), thereby increasing contact and binding between the membrane receptor and the Flg polypeptide.

[0118] Conservative N-terminal signature sequences (SEQ ID NOs: 542-548) can be used in combination with any of the flagellin-associated polypeptides as described herein. In particular, signature sequences are suitable for use in combination with naturally occurring Flg L-polypeptides (L-Flg22 SEQ ID NOs: 226-300; L-FlgII-28 SEQ ID NOs: 301-375) or any of the retro-inverse D polypeptides Flg (D-Flg22 SEQ ID NO: 376-450; FlgII-28 SEQ ID NO: 451-525) or any other Flg-associated sequences shown in Table 5 (SEQ ID NO: 526-541) to ensure efficient delivery of Flg -associated polypeptides on the surface of the plant membrane.

[0119] The signature sequences facilitate binding of the bioactive Flg22 and FlgII-28 polypeptide priming sequences to the appropriate Flg-associated receptor or receptors to activate the receptor or receptors, rendering it(them) functionally active(s).

Table 6. Flagellin-associated N-terminal signature sequences

SEQID NO: Flagellin signature sequences SEQ ID NO: 542 GFLN SEQ ID NO: 543 WGFLI SEQ ID NO: 544 MGVLN SEQ ID NO: 545 GVLN SEQ ID NO: 546 WGFFY SEQ ID NO: 547 LVPFAVWLA SEQ ID NO: 548 AVWLA

N-terminal signal anchor sorting sequences

[0120] "Signal anchor sorting" amino acid sequences conserved in the genera Bacillus, Lysinibacillus, Aneurinibacillus and Paenibacillus and other eubacterial genera of bacteria, may be involved in the anchoring and localization of flagellin-associated polypeptides on the plant cell membrane surface and promote high affinity binding to the appropriate (and ) Flg-associated(s) receptor(s), thus increasing the activation potential of the associated receptor or receptors.

[0121] Conserved signal anchor sequences (SEQ ID NO: 549-562; Table 7) are located in the 3' direction relative to pre-cleaved or full-length flagellin coding sequences, for example, as described herein (SEQ ID NO: 1 -75; table 1).

[0122] Signal anchor sorting domains as described herein are suitable for attachment to a membrane. They can be used to promote the localization and binding of Flg-associated polypeptides to a receptor on the membrane surface and have some functional similarity at the amino acid level to endosomal (vesicular), migrating or secretory-targeting proteins. Such signal anchor sorting sequences as described herein, suitable for anchoring bioactive Flg priming polypeptides on the plant cell membrane, are also used to improve membrane integration of bioactive Flg priming polypeptides in the plant cell.

[0123] Such sequences as described in Table 7 can further be operably annotated as import receptor signal anchor sequences, which can be used to improve targeting or delivery, efficient membrane anchoring of Flg-associated polypeptides in a plant, and promote membrane integration into the plant cell cytosol.

[0124] Combining signal anchor sequences (SEQ ID NOs: 549-562; Table 7) with any of the flagellins or flagellin-associated bioactive priming polypeptides as described herein is suitable to facilitate attachment and import of said flagellin-associated polypeptide or polypeptides into a plant .

[0125] Such signal anchor sorting sequences can be used in combination with Flg-associated polypeptides, and are suitable for targeting, efficient membrane anchoring, membrane integration, and Golgi-to-lysosome/vacuolar migration. Said signal anchor sorting sequences are used to stably deliver Flg polypeptides to the surface of the plant membrane and integrate them into the plant.

[0126] Such sequences as described herein contain dileucine amino acids, which are reported to confer endocytosis capability in plant systems (Pond et al. 1995, “A role for acidic residues in di-leucine motif-based targeting to the endocytic pathway”, Journal of Biological Chemistry 270: 19989-19997, 1995).

[0127] Such described signal anchor sorting sequences can also be used to efficiently deliver systemic signals to infection sites and stimulate innate plant immunity in plant cells.

Table 7. Flagellin-associated signal anchor sorting sequences

SEQID NO: Signal Anchor Sequence SEQ ID NO: 549 LLGTADKKIKIQ SEQ ID NO: 550 LLKSTQEIKIQ SEQ ID NO: 551 LLNEDSEVKIQ SEQ ID NO: 552 LGVAANNTQ SEQ ID NO: 553 LLRRDLANQ SEQ ID NO: 554 LQRMRDVAVQ SEQ ID NO: 555 LLRMRDISNQ SEQ ID NO: 556 LLRMRDIANQ SEQ ID NO: 557 LQKQIDYIAGNTQ SEQ ID NO: 558 LLIRLPLD SEQ ID NO: 559 QRMRELAVQ SEQ ID NO: 560 TRMRDIAVQ SEQ ID NO: 561 TRMRDIAVQ SEQ ID NO: 562 QRMRELVVQ

C-terminal secretion sequences

[0128] Conserved sequences located at the C-terminus of flagellin(s) are further described as secretion sequences (SEQ ID NOs: 563-570; Table 8).

[0129] Conservative sequences have been identified at the C-terminus of proteins derived from flagellin of bacteria Bacillus, Lysinibacillus and Paenibacillus (genera) and other genera of eubacteria; they contain 6 amino acids, such as LGATLN, LGSMIN or LGAMIN. These sequences were functionally annotated by BLAST against bacterial databases as motifs with the highest homology to the secretion polypeptides. These 6 amino acid conserved polypeptides identified were found to be most similar to those found in E. coli type III secretion systems. Type III export systems have been reported to be involved in the translocation of polypeptides across the plant cell membrane. The assembly of filaments from flagellin depends on the availability of flagellins to be secreted and may require the presence of chaperones to aid the secretory process.

[0130] Said secretion polypeptides as described herein can be used in combination with any of the flagellin-associated polypeptides as described herein to deliver said polypeptides/peptides to the cytosol of a host plant, thus providing plant-friendly outcomes.

Table 8. C-terminal sequences for the secretion of flagellin-associated polypeptides

SEQID NO: flagellin secretion polypeptides SEQ ID NO: 563 LGATLN SEQ ID NO: 564 LGATQN SEQ ID NO: 565 LAQANQ SEQ ID NO: 566 LGAMIN SEQ ID NO: 567 LGSMIN SEQ ID NO: 568 MGAYQN SEQ ID NO: 569 LGAYQN SEQ ID NO: 570 YGSQLN

[0131] Signature sequences (SEQ ID NOs: 542-548; Table 6), signal anchor sorting sequences (SEQ ID NOs: 549-562; Table 7), and secretion sequences (SEQ ID NOs: 563-570; Table 8) according to The present invention may be used with any of the flagellin polypeptides or flagellin-associated polypeptides to promote growth and provide health and protection benefits to a plant or plant part.

Function modification of Flg polypeptide sequences

[0132] Any of the Flg-associated L or D sequences shown in Tables 3, 4 or 5 can be similarly modified by fusion with any of the ancillary sequences as described in Table 6-8. In one example, fusion with any of these accessory sequences results in modification of the bioactive Bt.4Q7Flg22 priming polypeptide sequence identified as SEQ ID NO: 226.

Mutations in Flg-associated polypeptides to increase reactive oxygen species responsiveness or polypeptide stability

[0133] The specified polypeptide may contain a mutant flagellin or flagellin-associated polypeptide.

[0134] Said mutant flagellin or flagellin-associated polypeptide may be from a bacterium of the genus Bacillus, Lysinibacillus, Paenibacillus, or Aneurinibacillus. Other polypeptides from other classes of eubacteria, including Enterobacteraciae, may also be used in the same manner. Other genera of interest include Pseudomonas, Escherichia, Xanthomonas, Burkholderia, Erwinia, and others.

[0135] The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226, 289, 290, 291, 293, 294, 295, 300, 437, 532, 534, 536, 538, 540, 571- 586 and 751-768. For example, the amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226, 293, 295, 300, 540, 571, 574, and 752, or any combination thereof.

[0136] Any bioactive priming polypeptide, naturally occurring or not, can be further modified by chemical modification to increase the performance as well as the stability of said polypeptides. Such bioactive priming polypeptides include flagellin polypeptides, retro-inverse polypeptides, harpin-derived polypeptides, harpin-like polypeptides, EF-Tu polypeptides, thionine polypeptides, RHPP polypeptides, and CSF polypeptides. Specific sequences that may be chemically modified include SEQ ID NOs: 226-592, 594-601, 603-749 and 751-766.

[0137] These bioactive priming polypeptides may also be conjugated to other moieties, including a plant-binding domain and polypeptide, a plant-part-binding domain and polypeptide, and other carriers such as oils, plastics, granules, ceramics, soil, fertilizers , pellets and most construction materials.

[0138] Said flagellin or flagellin-associated polypeptide may be chemically modified at the N- or C-terminus. Common N- and C-terminal modifications include: acetylation, lipid addition, urea addition, pyroglutamyl addition, carbamate addition, sulfonamide addition, alkylamide addition, biotinylation, phosphorylation, glycosylation, pegylation, methylation, biotinylation, acid addition, amide addition, compound addition ether, addition of aldehyde, addition of hydrazide, addition of hydroxamic acid, addition of chloromethyl ketones, or addition of purification marks. Said labels can increase the activity of said polypeptides, increase stability, render said polypeptides protease inhibitory properties, directly block proteases, allow tracking, and aid binding to plant tissues.

[0139] The specified flagellin or flagellin-associated polypeptide can be modified by cross-linking or cyclization. When crosslinked, the polypeptides can either bind to each other or to a secondary surface or fragment, which aids in the delivery or stability of said polypeptides. Can be performed cyclization, for example, to simultaneously increase the activity of the specified polypeptide and prevent the interaction of proteases with the specified polypeptide.

[0140] Sequence modifications or mutations can be made to any amino acid sequence or sequences as described in Tables 4 and 5, with any of the 20 standard amino acids known in nature, or non-standard or non-canonical amino acids such as selenocysteine, pyrrolysine, N-formylmethionine, and the like. For example, modifications or mutations can be made to internal sequences as shown in SEQ ID NO: 571, to the C-terminus as shown in SEQ ID NO: 572 or SEQ ID NO: 753 , or at the N-terminus, as shown in SEQ ID NO: 573, to obtain Flg polypeptides with enhanced ROS activation and increased functionality in the plant or plant part. Modified polypeptides may also be N- or C-terminally truncated as shown in SEQ ID NO: 752 (N-terminal truncation) to further enhance functionality in the plant or plant part. Table 9A summarizes the identified flagellin polypeptides that provide modified ROS activity.

Table 9A. Identified Flg22 flagellin polypeptides from Bacillus or other bacteria with mutations that confer modified ROS activity

SEQID NO: Peptide Flg22 Flg22-Bt4Q7
SEQ ID NO: 571
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (S13K); Syn01 DRLSSGKRINSAKDDAAGLAIA Flg22-Bt4Q7
SEQ ID NO: 572
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (A20Q); Syn02 DRLSSGKRINSASDDAAGLQIA Flg22-Bt4Q7
SEQ ID NO: 573
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (D1Q); Syn03 QRLSSGKRINSASDDAAGLAIA Flg22-Bt4Q7
SEQ ID NO: 574
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (D1N); Syn06 NRLSSGKRINSASDDAAGLAIA Caballeronia megalochromosomata
SEQ ID NO: 575 TRLSSGKRINSASDDAAGLAIA Flg22-Bt4Q7
SEQ ID NO: 576
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (K7Y); Syn07 DRLSSGYRINSASDDAAGLAIA Flg22-Bt4Q7
SEQ ID NO: 577
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (K7F); Syn08 DRLSSGFRINSASDDAAGLAIA Flg22-Bt4Q7
SEQ ID NO: 578
Bacillus thuringiensis
Modified FLG22-Bt4Q7 (A16P); Syn05 DRLSSGKRINSASDDPAGLAIA Flg22-Bt4Q7
SEQ ID NO: 579
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (K7Q); Syn09 DRLSSGQRINSASDDAAGLAIA Flg22-Bt4Q7
SEQ ID NO: 753
Bacillus thuringiensis strain 4Q7
Modified FLG22-Bt4Q7 (D15P); Syn04 DRLSSGKRINSASDPAAGLAIA Flg15-Bt4Q7
SEQ ID NO: 752
Bacillus thuringiensis
N-terminally truncated Syn01 RINSAKDDAAGLAIA Bm.Flg22-B1
Bacillus manliponensis
SEQ ID NO: 290 NRLSSGKQINSASDDAAGLAIA Ba.Flg22-B2
Bacillus anthracis
SEQ ID NO: 295 NRLSSGKRINSAADDAAGLAIA Bc.Flg22-B3
Bacillus cereus
SEQ ID NO:294 DRLSSGKRINNASDDAAGLAIA A. spp.Flg22-B4
Aneurinibacillus spp.XH2
SEQ ID NO: 300 ERLSSGYRINRASDDAAGLAIS Ba.Flg22-B5
Bacillus aryabhattai
SEQ ID NO: 289 EKLSSGQRINSASDDAAGLAIS P spp.Flg22-B6
Paenibacillus spp. strain HW567
SEQ ID NO: 293 GKLSSGLRINGASDDAAGLAIS L spp.Flg22-L1
Lysinibacillus spp.
SEQ ID NO: 291 LRLSSGYRINSAADDAAGLAIS L spp.Flg22-L2
Lysinibacillus spp.
SEQ ID NO: 580 EKLSSGLRINRAGDDAAGLAIS L spp.Flg22-L3
Lysinibacillus spp.
SEQ ID NO:-581 EKLSSGYKINRASDDAAGLAIS L spp.Flg22-L4
Lysinibacillus spp.SG9
SEQ ID NO: 582 LRISSGYRINSAADDPAGLAIS Lf.Flg22-L5
Lysinibacillus fusiformis
SEQ ID NO: 583 LRISTGYRINSAADDPAGLAIS Lm.Flg22-L6
Lysinibacillus macroides
SEQ ID NO: 584 EKLSSGFRINRAGDDAAGLAIS Lx.Flg22-L6
Lysinibacillus
xylanilyticus
SEQ ID NO: 585 EKLSSGYKINRAGDDAAGLAIS Pa.Flg22
Pseudomonas aeruginosa
SEQ ID NO: 530 QRLSTGSRINSAKDDAAGLQIA Ec.Flg22
Escherichia coli
SEQ ID NO: 586 ERLSSGLRINSAKDDAAGQAIA Xcc.Flg22
Xanthomonas campestris, patovar campestris, strain 305 or
(Xanthomonas citri, patovar citri)
SEQ ID NO: 532 QRLSSGLRINSAKDDAAGLAIS Ea.Flg22
Erwinia amylovora
SEQ ID NO: 534 QRLSSGLRINSAKDDAAGQAIS Bp.Flg22
Burkholderia phytofirmans strain PsJN
SEQ ID NO: 536 TRLSSGKRINSAADDAAGLAIS Bu.Flg22
Burkholderia ubonensis
SEQ ID NO: 538 NRLSSGKRINTAADDAAGLAIS Ps.Flg22
Pseudomonas syringae, patovar actinidiae ICMP 19096
SEQ ID NO: 540 TRLSSGLKINSAKDDAAGLQIA

Flg22 core active domain

[0141] The underlined parts of the sequences in Table 9A correspond to the Flg22 core active domain. The specified core domain contains, for example, SEQ ID NO: 754 with up to one, two or three amino acid substitutions (represented by SEQ ID NO: 755-765), which can promote the growth, reduction and/or prevention of diseases in plant and ornamental crops. plants. For ease of reference, said core domain is shown as a consensus sequence containing SEQ ID NO: 766. Various natural and mutant Flg22 polypeptides containing SEQ ID NO: 754-765 are described along with said consensus sequence in Table 9B below. Accordingly, said polypeptides may further comprise a core sequence. The specified core sequence may contain any of SEQ ID NO: 754-766.

[0142] The specified polypeptide may also contain any polypeptide containing any of SEQ ID NO: 1-753 or 767-768, characterized in that it additionally contains a core sequence containing any of SEQ ID NO: 754-766. Incorporation of said core sequence into said polypeptide or a full-length protein with a different function may increase the conjugating bioactivity of said polypeptide.

Table 9B Flg22 core sequence with variants.

SEQID NO: FLG22 core sequence Polypeptides containing the core sequence SEQ ID NO: 754 RINSASDD SEQ ID NO: 226-229
SEQ ID NO: 289
SEQ ID NO: 299
SEQ ID NO: 536
SEQ ID NO: 572-579 SEQ ID NO: 755 RINNASDD SEQ ID NO: 231-234
SEQ ID NO: 236-240
SEQ ID NO: 243-246
SEQ ID NO: 248
SEQ ID NO: 250-256
SEQ ID NO: 258-259
SEQ ID NO: 261
SEQ ID NO: 263
SEQ ID NO: 265-270
SEQ ID NO: 272-280
SEQ ID NO: 282-283
SEQ ID NO: 285-286
SEQ ID NO: 288
SEQ ID NO: 294 SEQ ID NO: 756 QINSASDD SEQ ID NO: 290 SEQ ID NO: 757 RINSAADD SEQ ID NO: 291-292
SEQ ID NO: 295-298
SEQ ID NO: 582-583
SEQ ID NO: 536
SEQ ID NO: 582-583 SEQ ID NO: 758 RINGASDD SEQ ID NO: 293 SEQ ID NO: 759 RINRASDD SEQ ID NO: 300 SEQ ID NO: 760 RINSAKDD SEQ ID NO: 526
SEQ ID NO: 528
SEQ ID NO: 530
SEQ ID NO: 532
SEQ ID NO: 534
SEQ ID NO: 571
SEQ ID NO: 586 SEQ ID NO: 761 RINTAADD SEQ ID NO: 538 SEQ ID NO: 762 KINSAKDD SEQ ID NO: 540 SEQ ID NO: 763 RINRAGDD SEQ ID NO: 580
SEQ ID NO: 584 SEQ ID NO: 764 KINRSDDD SEQ ID NO: 581 SEQ ID NO: 765 KINRAGDD SEQ ID NO: 585 SEQ ID NO: 766 (R/Q/K)IN(S/N/G/R/T)A(S/A/K/G)DD Consensus sequence for SEQ ID NO: 755-765 (sequences identified in said table)

Harpin or Harpin-like polypeptides

[0143] Said polypeptide may include a harpin or a harpin-like polypeptide.

[0144] The amino acid sequence of said harpin or harpin-like polypeptide may comprise SEQ ID NOs: 587-592 and 594-597 (Tables 10 and 11),

[0145] Said harpins or harpin-like polypeptides may be derived from the Xanthomonas species or from various genera of bacteria, including Pantoea sesami, Erwinia gerudensis, Pantoea sesami, or Erwinia gerudensis

[0146] Additional harpin-like bioactive priming polypeptides can be derived from a full-length HpaG-like protein from Xanthamonas citri containing SEQ ID NO: 593.

[0147] The use of HpaG-like polypeptides using the natural form of the L-harpine-like (SEQ ID NO: 587) or retro-inverse form of the D-harpine-like sequence (SEQ ID NO: 588) sequence of the bioactive primer polypeptides shown in Tables 10 or 11, suitable for improving growth and immune responses in plants when applied exogenously or endogenously to a plant or plant part. A retro-inverse HpaG-like (eg SEQ ID NO: 588) bioactive priming polypeptide is particularly suitable for enhancing the activity and stability of an HpaG-like polypeptide when applied to plants growing under or exposed to abiotic stress conditions. The retro-inverse form of the HpaG-like polypeptide can be used to improve growth and defense responses in plants growing in such an environment.

Table 10. Harpin-like (HpaG-like) polypeptides

SEQID NO: Amino acid sequence of the peptide Harpin-like (HpaG-like)
SEQ ID NO: 587
Species Xanthomonas
MW 2626.35 Yes NQGISEKQLDQLLTQLIMALLQQ Harpin-like (Retro-inverse HpaG-like)
SEQ ID NO: 588
Species Xanthomonas
MW 2626.35 Yes QQLLAMILQTLLQDLQKESIGQN Harpin-like (HpaG-like)
SEQ ID NO: 589
Species Xanthomonas
MW 2626.35 Yes LDQLLTQLIMAL Harpin-like (Retro-inverse HpaG-like)
SEQ ID NO: 590
Species Xanthomonas
MW 2626.35 Yes LAMILQTLLQDL Harpin-like (HpaG-like)
SEQ ID NO: 591
Species Xanthomonas
MW 2626.35 Yes SEKQLDQLLTQLIMALLQQ Harpin-like (Retro-inverse HpaG-like)
SEQ ID NO: 592
Species Xanthomonas
MW 2626.35 Yes QQLLAMILQTLLQDLQKES HpaG-like protein
SEQ ID NO: 593
Xanthamonas citri MMNSLNTQLGANSSFFQVDPSQNTQSGSNQGNQGISEKQLDQLLTQLIMALLQQSNNAEQGQGQGQGGDSGGQGGNRQQAGQSNGSPSQYTQMLMNIVGDILQAQNGGGFGGGFGGGGGLGTSLGGFTSLGTSLASDTGSMQ

Table 11. HpaG-like homologues from various genera of bacteria

SEQID NO: Amino acid sequence of the peptide Active HpaG homologue fraction
SEQ ID NO: 594
Pantoea sesami QLEQLMTQLRARLCRLAM Active HpaG homologue fraction
SEQ ID NO: 595
Erwinia gerudensis QLEQLMTQLRARLKRLMAM Active fraction of the retro-inverse homologue of HpaG
SEQ ID NO: 596
Pantoea sesami MAMLRCLRARLQTMLQELQ Active fraction of the retro-inverse homologue of HpaG
SEQ ID NO: 597
Erwinia gerudensis MAMLRKLRARLQTMLQELQ

Phytosulfokine (FSK-α) polypeptides

[0148] The specified polypeptide may contain a CSF polypeptide.

[0149] The amino acid sequence of said CSF polypeptide may comprise SEQ ID NOs: 598-599.

[0150] Phytosulfokin-alpha (FSK-α) was first obtained from Arabidopsis thaliana and is a sulfonated bioactive priming polypeptide. The bioactive FSK-α priming polypeptide or polypeptides are shown in Table 11.

[0151] CSF-α is presented either as a synthetic polypeptide or as a natural polypeptide expressed in a recombinant microorganism, purified and used in agricultural formulations for application to plants or plant parts.

Table 12. Phytosulfokin-alpha (FSK-α), sulfonated bioactive priming polypeptides presented as natural and retro-inverse amino acid sequences

SEQID NO: Amino acid peptide sequence Phytosulfokin (FSK-α)
SEQ ID NO: 598
Arabidopsis thaliana
MW 845 Yes Tyr(SO ₃ H)-I-Tyr(SO ₃ H)-TQ Phytosulfokin (Retro-Inverse FSK-α)
SEQ ID NO: 599
Arabidopsis thaliana
MW 845 Yes QT-Tyr(SO ₃ H)-I-Tyr(SO ₃ H)

Root Spike Stimulator Polypeptide (RHPP)

[0152] The specified polypeptide may contain RHPP

[0153] The amino acid sequence of said RHPP may comprise SEQ ID NOs: 600-601 and 603-606. For example, the amino acid sequence of said RHPP may comprise SEQ ID NO: 600.

[0154] Also provided is a combination of said RHPP-containing polypeptide and a flagellin- or flagellin-associated polypeptide-containing polypeptide. Said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226, 752, and 571. In some instances, said polypeptide contains RHPP containing SEQ ID NO: 600 and flagellin containing SEQ ID NO: 226.

[0155] Said polypeptide may comprise an FSK, RHPP, harpin or harpin-like polypeptide, or a combination thereof.

[0156] Additional bioactive RHPP priming polypeptides may be derived from the full-length Kunitz trypsin inhibitor protein from Glycine max containing SEQ ID NO: 602. Said RHPP polypeptide may be modified by C-terminal amidation, N-terminal acetylation, or other modification. Said bioactive RHPP priming polypeptide can be prepared by adding a crude protease hydrolysate of the Kunitz trypsin inhibitor and/or soybean meal.

[0157] Raw soybean RHPP (Glycine max) can be provided, for example, as a foliar application to obtain favorable phenotypes in corn, soybean and other crops.

Table 13. Amino acid sequence of forward and retro inverse RHPP sequences

SEQID NO: Amino acid peptide sequence Root Stimulant Peptide (RHPP)
SEQ ID NO: 600
Glycinemax
MW 1198.20 Yes GGIRAAPTGNER Root Spike Stimulator Peptide (Retro-Inverse RHPP)
SEQ ID NO: 601
Glycinemax
MW 1198.20 Yes RENGTPAARIGG Trypsin inhibitor Kunitz
SEQ ID NO: 602
Glycinemax MKSTIFFALFLFCAFTTSYLPSAIADFVLDNEGNPLENGGTYYILSDITAFGGIRAAPTGNERCPLTVVQSRNELDKGIETIISSPYRIRFIAEGHPLSLKFDSFAVIMLCVGIPTEWSVVEDLPEGPAVKIGENKDAMDGWFRLERVSDDEFNNYKLVFCPQQAEDDKCGDIGISIDHDDGTRRLVVSKNKPLVVQFQKLDKESLAKKNHGLSE

Table 14 RHPP homologues from Glycine spp.

SEQID NO: Amino acid peptide sequence RHPP homologue
SEQ ID NO: 603
Glycinemax GGIRATPTENER RHPP homologue
SEQ ID NO: 604
Glycine max/Glycine soja GGIRVAATGKER

[0158] The specified polypeptide may include retro-inverse (RI) RHPP.

[0159] Said retro inverse RHPP may comprise SEQ ID NO: 601, 605, or 606.

[0160] This retro-inverse (RI) RHPP can be modified by C-terminal amidation or N-terminal acetylation.

Table 15 Retro-inverse amino acid sequences of RHPP homologues from Glycine spp.

SEQID NO: Amino acid peptide sequence RHPP homologue
SEQ ID NO: 605
Glycinemax RENETPTARIGG RHPP homologue
SEQ ID NO: 606
Glycine max/Glycine soja REKGTAAVRIGG

Tu elongation factor polypeptides (EF-Tu)

[0161] Said polypeptide may comprise an EF-Tu polypeptide.

[0162] Peptides derived from the Tu elongation factor (EF-Tu) can be used alone or in combination with other bioactive priming polypeptides as described herein, for example, in combination with Flg22 polypeptides to provide several modes of protection against pathogenic organisms, typically bacterial and fungal microorganisms, but also other infectious agents such as viruses.

[0163] Table 16 lists preferred N-terminal polypeptides derived from various bioactive EF-Tu priming polypeptides selected from both plant and bacterial EF-Tu polypeptides. Said EF-Tu-derived polypeptides can be any length from 18 to 26 amino acids, or less than 26 amino acids. Table 17 also lists retro-inverse (fully D-) variants of bacterial and algal-derived EF-Tu polypeptides.

[0164] The amino acid sequence of said EF-Tu polypeptide may comprise any of SEQ ID NOs: 607-640.

[0165] The amino acid sequence of said EF-Tu polypeptide may comprise SEQ ID NO: 616 or 617.

[0166] The EF-Tu polypeptide can be modified by N-terminal acetylation. For example, said EF-Tu polypeptide may be modified by N-terminal acetylation and comprise any of SEQ ID NOs: 607, 608, 610, 611, 613, 614, 616, 617, 619, or 622.

Table 16 N-terminal acetylated and central polypeptides derived from elongation factors (EF-Tu) present in plant, bacterial and algal species

SEQID NO: Amino acid sequence length Amino acid sequence of the peptide EF-Tu chloroplast
SEQ ID NO: 607 (acetylated)
Arabidopsis lyrata eighteen Ac-ARGKFERKKPHVNIGTIG EF-Tu chloroplast
SEQ ID NO: 608 (acetylated)
Arabidopsis lyrata 26 Ac-ARGKFERKKPHVNIGTIGHVDHGKTT EF-Tu chloroplast
SEQ ID NO: 609
Arabidopsis lyrata fifty EKPNVKRGENKWVDKIYELMDSVDSYIPIPTRQTELPFLAVEDVFSITG N-terminus of EF-Tu
SEQ ID NO: 610 (acetylated)
Euglena gracilis eighteen Ac-ARQKFERTKPHINIGTIG N-terminus of EF-Tu
SEQ ID NO: 611 (acetylated)
Euglena gracilis 26 Ac-ARQKFERTKPHINIGTIGHVDHGKTT EF-Tu fragment
SEQ ID NO: 612
Euglena gracilis fifty KNPKITKGENKWVDKILNLMDQVDSYIPTPTRDTEKDFLMAIEDVLSITG N-terminus of EF-Tu
SEQ ID NO: 613 (acetylated)
Acidovorax avenae eighteen Ac-AKGKFERTKPHVNVGTIG N-terminus of EF-Tu
SEQ ID NO: 614 (acetylated)
Acidovorax avenae 26 Ac-AKGKFERTKPHVNVGTIGHVDHGKTT EF-Tu fragment
SEQ ID NO: 615
Acidovorax spp. fifty KLALEGDKGPLGEQAIDKLAEALDTYIPTPERAVDGAFLMPVEDVFSISG N-terminus of EF-Tu
SEQ ID NO: 616 (acetylated)
Bacillus cereus eighteen Ac-AKAKFERSKPHVNIGTIG N-terminus of EF-Tu
SEQ ID NO: 617 (acetylated)
Bacillus cereus 26 Ac-AKAKFERSKPHVNIGTIGHVDHGKTT Fragment of EF-Tu
SEQ ID NO:618
Bacillus cereus fifty SALKALQGEAEWEEKIIELMAEVDAYIPTPERETDKPFLMPIEDVFSITG N-terminus of EF-Tu
SEQ ID NO: 619 (acetylated)
Burkholderia spp. 26 Ac-AKGKFERTKPHVNVGTIGHVDHGKTT Fragment of EF-Tu
SEQ ID NO: 620
Burkholderia spp. fifty KLALEGDTGELGEVAIMNLADALDTYIPTPERAVDGAFLMPVEDVFSISG Fragment of EF-Tu
SEQ ID NO: 621
Xanthomonas campestris fifty RLALDGDQSEIGVPAILKLVDALDTFIPEPTRDVDRPFLMPVEDVFSISG N-terminus of EF-Tu
SEQ ID NO: 622 (acetylated)
Pseudomonas spp. 26 Ac-AKEKFERSKPHVNVGTIGHVDHGKTT EF Tu
SEQ ID NO: 623
Pseudomonas spp. fifty MALEGKDDNEMGTTAVKKLVETLDSYIPEPERAIDKPFLMPIEDVFSISG

Table 17 Retro-inverse polypeptides derived from elongation factors (EF-Tu) present in bacterial and algal species

SEQID NO: Amino acid sequence length Amino acid sequence of the peptide RI EF-Tu chloroplasts
SEQ ID NO: 624
Arabidopsis lyrata eighteen GITGINVHPKKREFKGRA RI EF-Tu chloroplasts
SEQ ID NO: 625
Arabidopsis lyrata 26 TTKGHDVHGITGINVHPKKREFKGRA RI EF-Tu chloroplasts
SEQ ID NO: 626
Arabidopsis lyrata fifty GTISFVDEVALLFPLETQRTPIPIYSDVSDMLEYIKDVWKNEGRKVNPKE RI N-terminus EF-Tu
SEQ ID NO: 627
Euglena gracilis eighteen GITGINIHPKTREFKQRA RI N-terminus EF-Tu
SEQ ID NO: 628
Euglena gracilis 26 TTKGHDVHGITGINIHPKTREFKQRA RI EF-Tu fragment
SEQ ID NO: 629
Euglena gracilis fifty GTISLVDEIAMLFDKETDRTPTPIYSDVQDMLNLIKDVWKNEGKTIKPNK RI N-terminus EF-Tu
SEQ ID NO: 630
Acidovorax avenae eighteen GITGVNVHPKTREFKGKA RI N-terminus EF-Tu
SEQ ID NO: 631
Acidovorax avenae 26 TTKGHDVHGITGVNVHPKTREFKGKA RI EF-Tu fragment
SEQ ID NO: 632
Acidovorax spp. fifty GSISFVDEVPMLFAGDVAREPTPIYTDLAEAALKDIAQEGLPGKDGELALK RI N-terminus EF-Tu
SEQ ID NO: 633
Bacillus cereus eighteen GITGINVHPKSREFKAKA RI N-terminus EF-Tu
SEQ ID NO: 634
Bacillus cereus 26 TTKGHDVHGITGINVHPKSREFKAKA RI EF-Tu fragment
SEQID NO:
635
Bacillus cereus fifty GITSFVDEIPMLFPKDTEREPTPIYADVEAMLEIIIKEEWEAEGQLAKLAS RI N-terminus EF-Tu
SEQ ID NO: 636
Burkholderia spp. 26 TTKGHDVHGITGVNVHPKTREFKGKA RI EF-Tu fragment
SEQ ID NO: 637
Burkholderia spp. fifty GSISFVDEVPLMLFAGDVAREPTPIYTDLADALNMIAVEGLEGTDGELALK RI EF-Tu fragment
SEQ ID NO: 638
Xanthomonas campestris fifty GSISFVDEVPMLFPRDVDRTPEPIFTDLADVLKLIAPVGIESQDGDLALR RI N-terminus EF-Tu
SEQ ID NO: 639
Pseudomonas spp. 26 TTKGHDVHGITGVNVHPKSREFKEKA RI EF Tu
SEQ ID NO: 640
Pseudomonas spp. fifty GSISFVDEIPMLFPKDIAREPEPIYSDLTEVLKKVATTGMENDDKGELAM

Thionins and Thionin Targeting Polypeptides

[0167] Said polypeptide may contain a thionine or a thionine-like polypeptide.

[0168] Said thionin or thionin-like polypeptide may be fused to a phloem-targeting sequence to form a fusion polypeptide, wherein the amino acid sequence of said phloem-targeting sequence comprises any of SEQ ID NOs: 641-649, or any combination thereof, to deliver said fusion polypeptide into vascular tissue or vascular cells, and/or into phloem, or into phloem-associated tissue or phloem-associated cells in a plant or plant part.

[0169] The amino acid sequence of said phloem targeting sequence may comprise SEQ ID NO: 641.

[0170] More specifically, targeting sequences suitable for targeting PMP polypeptides, such as thionins or Flg polypeptides, to vascular tissues (xylem and phloem) may be extremely suitable for the treatment of diseases involving limited tissues involved in the transport of fluids and nutrients. substances (eg, water-soluble nutrients, sugars, amino acids, hormones, etc.). Vascular tissues such as xylem transport and store water and water-soluble nutrients, while phloem cells transport sugars, proteins, amino acids, hormones, and other organic molecules in plants.

[0171] Preferred vascular/phloem targeting polypeptides suitable for targeting thionins and flagellin-associated polypeptides as described herein are shown in Table 18.

Table 18. Phloem-Targeting Polypeptides

SEQID NO: Vascular/phloem targeting polypeptides Phloem-targeting peptide
synthetic
SEQ ID NO: 641 MSTATFVDIIIAILLPPLGVFLRFGCGVEFWICLVLTLLGYIPGIIYAIYVLTK Salt stress-induced targeting peptide
Citrus clementina
SEQ ID NO: 642 MGSETFLEVILAILLPPVGVFLRYGCGVEFWICLLLTVLGYIPGIIYAIYVLVG Hypothetical CICLE protein
Citrus trifoliata
SEQ ID NO: 643 MGTATCVDIILAVILPPLGVFLKFGCKAEFWICLLLTILGYIPGIIYAVYVITK Hypothetical CICLE protein
Citrus sinensis
SEQ ID NO: 644 MADEGTATCIDIILAIILPPLGVFLKFGCKVEFWICLLLTIFGYIPGIIYAVYAITKN Low temperature and salinity responsive protein
Citrus sinensis
SEQ ID NO: 645 MADGSTATCVDILLAVILPPLGVFLKFGCKAEFWICLLLTILGYIPGIIYAVYAITKK Hypothetical CICLE protein
Citrus
clementina
SEQ ID NO: 646 FYKQKYQVQITKAVTQNPKHFFNQSSCFLTLNFILFHFTLFKNQSKMADGSTATCVDILLAVILPPLGVFLKFGCKAEFWICLLLTILGYIPGIIYAVYAITKK Low temperature and salinity responsive protein
Arabidopsis thaliana
SEQ ID NO: 647 MSTATFVDIIIAILLPPLGVFLRFGCGVEFWICLVLTLLGYIPGIIYAIYVLTK cold inducible protein
Camelina sativa
SEQ ID NO: 648 MSTATFVDIIIAVLLPPLGVFLRFGCCGVEFWICLVLTLLGYIPGIIYAIYVLTK Low temperature and salinity responsive protein
Arabidopsis lyrata
SEQ ID NO: 649 MGTATCVDIIIAILLPPLGVFLRFGCGVEFWICLVLTLLGYIPGILYALYVLTK

[0172] A synthetic variant of a phloem-targeting polypeptide (SEQ ID NO: 641) is particularly suitable for use in targeting antimicrobial polypeptides to phloem sieve tubes and companion cells.

[0173] Also provided are antimicrobial thionin polypeptides (Table 19) that are used with the phloem targeting sequences shown in Table 18 to target thionin sequences to citrus phloem tissue as well as other plants.

[0174] The amino acid sequence of said thionin or thionin-like polypeptide may comprise any of SEQ ID NOs: 650-749, for example, SEQ ID NOs: 651.

Table 19. Thionin and thionin-like sequences

SEQID NO: Thionin or thionin-like sequences - amino acids Thionin-like protein
Synthetic
SEQ ID NO: 650 RTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCRCTRPCVFDEK Thionin-like protein
Citrus sinensis
SEQ ID NO: 651 RVCQSQSHHFHGACFSHHNCAFVCRNEGFSGGKCRGVRRRCFCSKLC Thionin-like protein
Avena sativa
SEQ ID NO: 652 KSCCKDIMARNCYNVCRIPGTPRPVCATTCRCKIISGNKCPKDYPK Thionin-like protein
Synthetic
SEQ ID NO: 653 RTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCRCTRPCVFDEK Thionin-like protein
Citrus sinensis
SEQ ID NO: 654 MDSRSFGLLPLLLLILLTSQMTVLQTEARLCESQSHRFHGTCVRSHNCDLVCRTEGFTGGRCRGFRRRCFCTRIC Proteinase inhibitor se60-like protein
Citrus Paradise
SEQ ID NO: 655 MKSFFGIFLLLLILFASQEIMVPAEGRVCQSQSHHFHGACFSHHNCAFVCRNEGFSGGKCRGVRRRCFCSKLC defensin precursor
Citrus clementina
SEQ ID NO: 656 MKSFFGIFLLLLILFASQMMVPAEGRVCQSQSHHFHGACFSHHNCAFVCRNEGFSGGKCRGARRRCFCSKLC defensin precursor
Citrus clementina
SEQ ID NO: 657 MKSFFGIFLLLLILFASQEMMVPAEGRVCQSQSHHFHGACFSHHNCAFVCRNEGFSGGKCRGARRRCFCSKLC Thionin-like protein
Citrus clementina
SEQ ID NO: 658 MKSFFGIFLLLLILFASQMMVPAEGRVCQSQSHHFHGACFSHHNCAFVCRNEGFSGGKCRGARRRCFCSKLC Thionin-like peptide
Nicotiana benthamiana
SEQ ID NO: 659 MANSMRFFATVLLLALLVMATEMGPMTIAEARTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC Thionin-like protein
Nicotiana sylvestris
SEQ ID NO: 660 MAKSMRFFATVLLLALLVMATEMGPTTIAEARTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC Thionin-like protein
Nicotiana tabaccum
SEQ ID NO: 661 MANSMRFFATVLLLTLLVMATEMGPMTIAEARTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC Thionin-like protein
Nicotiana tomentosiformis
SEQ ID NO: 662 MANSMRFFATVLLIALLVMATEMGPMTIAEARTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC Thionin-like protein
Nicotiana tabaccum
SEQ ID NO: 663 MANSMRFFATVLLIALLVTATEMGPMTIAEARTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC Class I defensin
Nicotiana alata
SEQ ID NO: 664 MANSMRFFATVLLLTLLFMATEMGPMTIAEARTCESQSHRFKGPCARDSNCATVCLTEGFSGGDCRGFRRRCFCTRPC leaf thionine
Avena sativa
SEQ ID NO: 665 MGSIKGLKSVVICVLVLGIVLEQVQVEGKSCCKDIMARNCYNVCRIPGTPRPVCATTCRCKIISGNKCPKDYPKLHGDPD leaf thionine
Avena sativa
SEQ ID NO: 666 MGSIKGLKSVVICVLVLGIVLEHVQVEGKSCCKDTTARNCYNVCRIPGTPRPVCATTCRCKIISGNKCPKDYPKLHGDLD Thionine Class I
Tulipa gesneriana
SEQ ID NO: 667 LGLVVAQTQVDAKSCCPSTAARNCYNVCRFPGTPRPVCAATCGCKIITGTKCPPDYPKLGWSTFQNSDVADKALDVVDEALHVAKEVMKEAVERCNNACSEVCTKGSYAVTA Thionin-like protein class I
Vitis vinifera
SEQ ID NO: 668 MERKSLGFFFFLLLILLASQEMVVPSEARVCESQSHKFEGACMGDHNCALVCRNEGFSGGKCKGLRRRCFCTKLC Thionin-like protein class I
Vitis vinifera
SEQ ID NO: 669 MERKSLGFFFFLLILLASQMVVPSEARVCESQSHKFEGACMGDHNCALVCRNEGFSGGKCKGLRRRCFCTKLC Defensin Ec-AMP-D1
Citrus sinensis
SEQ ID NO: 670 MERSVRLFSTVLLVLLLASEMGLRAAEARICESQSHRFKGPCVSKSNCAAVCQTEGFHGGHCRGFRRRCFCTKRC Antimicrobial protein 1 (Ah-Amp1)
Aesculus hippocastanum
SEQ ID NO: 671 LCNERPSQTWSGNCGNTAHCDKQCQDWEKASHGACHKRENHWKCFCYFNC Hypothetical DCAR protein
Dacus carota
SEQ ID NO: 672 MAKNSTSPVSLFAISLIFFLLANSGSITEVDGKVCEKPSLTWSGKCGNTQHCDKQCQDWEGAKHGACHSRGGWKCFCYFEC Cysteine-rich antimicrobial protein
Clitoria ternatea
SEQ ID NO: 673 NLCERASLTWTGNCGNTGHCDTQCRNWESAKHGACHKRGNWKCFCYFNC Hypothetical DCAR protein
Dacus carota
SEQ ID NO: 674 MAKKSSSFCLSAILVLLLVANTGMVREVDGALCEKPSLTWSGNCRNTQHCDKQCQSWEGAKHGACHKRGNWKCFCYHAC Thionin-like
Bupleurum kaoi
SEQ ID NO: 675 MAKKLNAVTVSAIFLVVFLIASYSVGAAKEAGAEGEVVFPEQLCERASQTWSGDCKNTKNCDNQCIQWEKARHGACHKRGGKWMCFCYFDKC Defensin Dm-AMP1=cysteine-rich antimicrobial protein
Dahlia merckii
SEQ ID NO: 676 ELCEKASKTWSGNCGNTGHCDNQCKSWEGAAHGACHVRNGKHMCFCYFNC Thionin-like
Helianthus annuus
SEQ ID NO: 677 MAKISVAFNAFLLLLFVLAISEIGSVKGELCEKASQTWSGTCGKTKHCDDQCKSWEGAAHGACHVRDGKHMCFCYFNCSKAQKLAQDKLRAEELAKEKIEPEKATAKP Thionin
Cynara cardunculus, var. scolymus
SEQ ID NO: 678 MAKNSVAFFALLLLICILTISEFAVVKGELCEKASKTWSGNCGNTRHCDDQCKAWEGAAHGACHTRNKKHMCFCYFNCPKAEKLAQDKLKAEELARDKVEAKEVPHFKHPIEPIHHP Thionin
Cynara cardunculus, var. scolymus
SEQ ID NO: 679 MAKQWVSFFALAFIVFVLAISETQTVKGELCEKASKTWSGNCGNTKHCDDQCKSWEGAAHGACHVRNGKHMCFCYFNSCAEADKLSEDQIEAGKLAFEKAEKLDRDVKKAVPNVDHP Defensin-like protein 1 - DCAR-like
Daucus carota, subsp. Sativus
SEQ ID NO: 680 MAQKVNSALIFSAIFVLFLVASYSVTVAEGARAGAEGEVVYPEALCERASQTWTGKCQHTDHCDNQCIQWENARHGACHKRGGNWKCFCYFDHC Cysteine-rich, low molecular weight defensin
Arabidopsis lyrata
SEQ ID NO: 681 MASSYTLMLFLCLSIFLIASTEMMAVEARICERRSKTWTGFCGNTRGCDSQCKSWERASHGACHAQFPGFACFCYFNC Thionin-like protein
Parthenium hysterophorus
SEQ ID NO: 682 MAKSSTSYLVFLLLVLVVAISEIASVNGKVCEKPSKTWFGNCKDTEKCDKRCMEWEGAKHGACHQRESKYMCFCYFDCDP putative protein defensin AMP1
Arabidopsis thaliana
SEQ ID NO: 683 MASSYTLMLFLCLSIFLIASTEMMAVEGRICERRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Thionin-like
Eutrema salsugineum
SEQ ID NO: 684 MASSYTLLLFVCLSIFFIASTEMMMVEGRVCERRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Defensin-like
Vitis vinifera
SEQ ID NO: 685 MAKLLGYLLSYALSFLTLFALLVSTEMVMLEAKVCQRPSKTWSGFCGSSKNCDRQCKNWEGAKHGACHAKFPGVACFCYFNC Nottin
Corchorus olitorius
SEQ ID NO: 686 MAKSLSSFATFLALLCLFFLLSTPNEMKMAEAKICEKRSQTWSGWCGNSSHCDRQCKNWENARHGSCHADGLGWACFCYFNC Nottin
Corchorus olitorius
SEQ ID NO: 687 MEMKMAEGKICEKRSQTWSGWCGNSSHCDRQCKNWENARHGSCHADGLGWACFCYFNC Thionin-like protein Camelina sativa
SEQ ID NO: 688 MASSLKLMLFLCLSIFLIASTEMMTVEGRTCERRSKTWTGFCGNTRGCDSQCRSWEGASHGACHAQFPGFACFCYFNC Thionin-like protein of Cucumis sativus
SEQ ID NO: 689 MAKVVGNSAKMIVALLFLLALMLSMNEKQGVVEAKVCERRSKTWSGWCGNTKHCDRQCKNWEGATHGACHAQFPGRACFCYFNC Thionin-like protein
Cynara cardunculus, var. scolymus
SEQ ID NO: 690 MIDAFNYKQFSTVKGKICEKPSKTWFGKCQDTTKCDKQCIEWEDAKHGACHERESKLMCFCYYNCGPPKNTPPGTPPSPP Thionin-like
Capsella rubella
SEQ ID NO: 691 MASSYKLILFLCLSIFLIASFEMMAVEGRICQRRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Thionin
Arabidopsis thaliana
SEQ ID NO: 692 MMAVEGRICERRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Thionin
Brassica napus
SEQ ID NO: 693 MASSYTRLLLLCLSIFLIASTEVMMVEGRVCQRRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Thionin-like protein of Brassica rapa
SEQ ID NO: 694 MASSYARLLLLCLSIFLIASTEVMMVEGRVCQRRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Thionin-like protein Camelina sativa
SEQ ID NO: 695 MASSLKLMLFLCLSIFLIASTEMMTVEGRTCERRSKTWTGFCGNTRGCDSQCRRWEHASHGACHAQFPGFACFCYFNC Brassica napus defensin-like protein
SEQ ID NO:696 MASYTRLLLLCLSIFLIASTEVMMVEGRVCQRRSKTWTGFCGNTRGCDSQCKRWERASHGACHAQFPGFACFCYFNC Vitis vinifera thionin-like protein
SEQ ID NO: 697 MVMLEAKVCQRPSKTWSGFCGSSKNCDRQCKNWEGAKHGACHAKFPGVACFCYFNC Thionin-like protein
Brassica napus
SEQ ID NO: 698 MTKSFILVALLCICFILLSPTEMRLTLNACLKLAEAKICEKYSQTWSGRCTKTSHCDRQCINWEDARHGACHQDKHGRACFCYFNCKK Thionin-like protein
Raphanus sativus
SEQ ID NO: 699 MASSYTVFLLLCLSIFLIASTEVMMVEGRVCQRRSKTWTGFCGNTRGCDSQCKRWEHASHGACHAQFPGFACFCYFNC Thionin-like
Arabis alpine
SEQ ID NO: 700 MASSYTLLLFLCLSIFLIVSTEMMMVEGRICERRSKTWTGFCANTRGCDSQCKRWERASHGACHAQFPGVACFCYFNC Thionin-like protein
Cucumis melo
SEQ ID NO: 701 MAKVVGNSAKMIVAFLFLLALTLSMNEKQGVVEAKVCERRSKTWSGWCGDTKHCDRQCKNWEGAKHGACHAQFPGRACFCYFNC Thionin-like protein
Erythranthe guttate
SEQ ID NO: 702 MAASLVYRLSSVILIVLLFIMLNNEVMVVESRLCERRSKTWTGFCGSSNNCNNQCRNWERASHGACHAQFPGFACFCYFNC Thionin-like protein of Sesamum indicum
SEQ ID NO: 703 MAKFQVSSTIFFALFFCFLLLASNEAKICQRMSKTWSGVCLNSGNCDRQCRNWERAQHGACHRRGLGFACLCYFKC Thionin-like protein
Eclipta prostrata
SEQ ID NO: 704 MAKNSVAFFAFLLILFVLAISEIGSVKGELCEKASQTWSGTCRITSHCDNQCKSWEGAAHGACHVRGGKHMCFCYFSHCAKAEKLTQDKLKAGHLVNEKSEADQKVPVTP Gamma-thionin Cynara cardunculus, var. scolymus
SEQ ID NO: 705 MAKNTKVSAFLFVFLFVFFLVVHSVTAFAIRFKCFDTDMLLKVIADMVVGMKGIEKVCRRRSKTWSGYCGDSKHCDQQCREWEGAEHGACHHEGLGRACFCYFNC Predecessor of Art v 1 Ambrosia artemisiifolia
SEQ ID NO: 706 MAAGLLVFVLAISEIASVKGKLCEKPSVTWSGKCKVKQTDKCDKRCIEWEGAKHGACHKRDSKASCFCYFDCDPTKNPGPPPGAPKGKAPAPSPPSGGGGEGGGEGGGER Predecessor of Art v 1 Ambrosia artemisiifolia
SEQ ID NO: 707 MAAGLLVFVLAISEIASVKGKLCEKPSLTWSGKCKVKQTDKCDKRCIEWEGAKHGACHKRDSKATCFCYFDCDPTKNPGPPPGAPKGKAPAPSPPSGGGAPPPSGGEGGER Thionin-like protein Jatropha curcas
SEQ ID NO: 708 MAKLHSSALCFLIIFLFLLVSKEMAVTEAKLCQRRSKTWSGFCGDPGKCNRQCRNWEGASHGACHAQFPGFACFCYFKC Thionin-like protein of Nelumbo nucifera
SEQ ID NO: 709 MAKAPKSVSYFAFFFILFLASSEIQKTKKLCERRSKTWSGRCTKTQNCDKQCKDWEYAKHGACHGSWFNKKCYCYFDC Thionin-like protein Pyrus×bretschneideri
SEQ ID NO: 710 MAKLLSRLSIPLIVFVFLLILLASTEVAMVEARICQRRSKTWSGFCANTGNCNRQCTNWEGALHGACHAQFPGVACFCYFRC Low molecular weight cysteine-rich protein precursor LCR78
Ricinus communi
SEQ ID NO: 711 MAKLHFPTLLCLFIFLFLLVSTEMQVTQAKVCQRRSKTWSGFCGSTKNCDRQCKNWEGALHGACHAQFPGVACFCYFKCGGER Art v 1 precursor homologue Ambrosia artemisiifolia
SEQ ID NO: 712 KLCEKPSVTWSGKCKVKQTDKCDKRCIEWEGAKHGACHKRDSKASCFCYFDCDPTKNPGPPPGAPKGKAPAPSPPSGGGAPPPSGGEGGGD Art v 1 precursor homologue Ambrosia artemisiifolia
SEQ ID NO: 713 KLCEKPSVTWSGNNKVKQTDKCDKRCIEWEGAKHGACHKRDSKASCFCYFDCDPTKNPGPPPGAPKGKAPAPSPPSGGGAPPPSGGEGGGDGGGGRR Thionin-like protein
Prunus mume
SEQ ID NO: 714 MAKLLSHLLFYPILFLFLFIFLASTEVAILEARICQRRSKTWSGFCGNTRNCNRQCRNWEGALRGACHAQFPGFACFCYFRC Nottin
Corchorus olitorius
SEQ ID NO: 715 MAKTLQLFALFFIVILLANQEIPVAEAKLCQKRSKTWTGICIKTKNCDNQCKKWEKAEHGACHRQGIGFACFCYFNQKKC Nottin
Corchorus olitorius
SEQ ID NO: 716 MAKFVSTVALLFALFILLASFDEGMMPMAEAKVCSKRSKTWSGFCNSSANCNKQCREWEDAKHGACHFEFPGFACFCYFNC Thionin-like protein Solanum pennellii
SEQ ID NO: 717 MNSKVILALLVCFLLIASNEMQGGEAKVCGRRSSTWSGLCLNTGNCNTQCIKWEHASSGACHRDGFGFACFCYFNC Thionin-like protein
Fragaria vesca, subspecies Vesca
SEQ ID NO: 718 MAKLLGYHLVYPILFLFIFLLLASTEMGMLEARICQRRSKTWTGLCANTGNCHRQCRNWEGAQRGACHAQFPGFACFCYFNC Nottin
Corchorus capsularis
SEQ ID NO: 719 MAKFVSVALLLALFILVASFDEGMVPMAEAKLCSKRSKTWSGFCNSSANCNRQCREWEDAKHGACHFEFPGFACFCYFDC Thionin-like protein Solanum tuberosum
SEQ ID NO: 720 MQGGEARVCERRSSTWSGPCFDTGNCNRQCINWEHASSGACHREGIGSACFCYFNC Defensin 1,2-like protein PDF1.2-1
Dimocarpus longan
SEQ ID NO: 721 MAKTLKSVQFFALFFLVILLAGSEMTAVEALCSKRSKTWSGPCFITSRCDRQCKRWENAKHGACHRSGWGFACFCYFNKC Thionin-like protein Camelina sativa
SEQ ID NO: 722 MAKAATIVTLLFAALVFFAALETPTMVEAQKLCERPSGTWSGVCGNSNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Arabis alpine
SEQ ID NO: 723 MAKFASIIAFLFAALVLFASFEAPTMVEAQKYCEKPSGTWSGVCGNSNACNNQCINLEGARHGSCNYVFPYYRCICYFQC Thionin-like
Theobroma cacao
SEQ ID NO: 724 MAMSLKSVHFFALFFIVVLLANQEMPVAEAKLCQKRSKTWTGPCIKTKNCDHQCRKWEKAQHGACHWQWPGFACFCYVNC Thionin-like
Amborella trichopoda
SEQ ID NO: 725 MAKLVSPKAFFVFLFVFLLISASEFSGSEAKLCQKRSRTWSGFCANSNNCSRQCKNLEGARFGACHRQRIGLACFCYFNC Cysteine-rich, low molecular weight 67 Arabidopsis thaliana
SEQ ID NO: 726 MAKSATIVTLFFAALVFFAALEAPMVVEAQKLCERPSGTWSGVCGNSNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Arabis alpine
SEQ ID NO: 727 MAKFASIITLLFAALVLFASLEAPTMVEAQKLCQRPSGTWSGVCGNNGACKNQCINLEKARHGSCNYVFPYHRCICYFPC Thionin-like
Brassica juncea
SEQ ID NO: 728 MAKVASIIALLFAALVLFAAFEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Brassica oleracea, var. oleracea
SEQ ID NO: 729 MAKFASIIALLFAALVLFAALEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Camelina sativa
SEQ ID NO: 730 MAKPATIVTLLFAALVFFAALETPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Camelina sativa
SEQ ID NO: 731 MAKSATIVTLLFAALVFFAALETPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Brassica napus
SEQ ID NO:732 MAKFASIIAPLFAVLVLFAAFEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Eutrema salsugineum
SEQ ID NO: 733 MAKFASIITLLFAALVLFAVFEGPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Cysteine-rich fungicidal protein
Raphanus sativus
SEQ ID NO: 734 MAKFASIIALLFAALVLFAAFEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like protein 1 Raphanus sativus
SEQ ID NO: 735 MAKFASIVSLLFAALVLFTAFEAPAMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like protein 1 Raphanus sativus
SEQ ID NO: 736 MNTKVILALLFCFLLVASNEMQVGEAKVCQRRSKTWSGPCINTGNCSRQCKQQEDARFGACHRSGFGFACFCYFKC Thionin-like
Brassica rapa
SEQ ID NO: 737 MAKFASIIAPLFAALVLFAAFEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Solanum pennellii
SEQ ID NO: 738 MNTKLILALMFCFLLIASNEMQVGEAKVCQRRSKTWSGPCINTGNCSRQCKQQEDARFGACHRSGFGFACFCYFKC Thionin-like
Citrus clementina
SEQ ID NO: 739 MAKFTTTFALLFAFFILFAAFDVPMAEAAKVCQRRSKTWSGLCLNTGNCSRQCKQQEDARFGACHRQGIGFACFCYFKC Thionin-like
Brassica rapa
SEQ ID NO: 740 MAKFTSIIVLLFAALVLFAGFEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPARKCICYFPC Thionin-like
Eutrema salsugineum
SEQ ID NO: 741 MAKFASIITLLFAALVLFATFAPTMVEAKLCERPSGTWSGVCGNNNACKSQCQRLEGARHGSCNYVFPAHKCICYFPC Thionin-like
Eutrema salsugineum
SEQ ID NO: 742 MAKFASIITLLFAALVLFATFEAPTMVEAKLCERPSGTWSGVCGNNNACKSQCQRLEGARHGSCNYVFPAHKCICYFPC Thionin-like
Heliophila coronopifolia
SEQ ID NO: 743 MAKFASIIAFFFAALVLFAAFEAPTIVEAQKLCERPSGTWSGVCGNNNACRNQCINLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Brassica oleracea
SEQ ID NO: 744 MAKVASIVALLFPALVIFAAFEAPTMVEAQKLCERPSGTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPAHKCICYFPC Thionin-like
Cicer arietinum
SEQ ID NO: 745 MSKFYTVFMFLCLALLLISSWEVEAKLCQRRSKTWSGPCIITGNCKNQCKNVEHATFGACHRQGFGFACFCYFNCH Thionin-like
Citrus clementina
SEQ ID NO: 746 MAKSVASITTAFALIFAFFFILFASFGVPMAEAKVCQRRSKTWSGPCLNTGKCSRQCKQQEYARYGACYRQGAGYACYCYFNC Thionin-like
Citrus sinensis
SEQ ID NO: 747 MAKSVASITTAFALIFAFFILFASFEVPMAEAKVCQRRSKTWSGPCLNTGKCSRHCKQQEDARYGACYRQGTGYACFCYFEC Thionin-like
Citrus sinensis
SEQ ID NO: 748 MAKFTTTFALLFAFFILFAAFDVPMAEAAKVCQLRSKTWSGLCLNTGNCSRQCKQQEDARFGACHRQGIGFACFCYFKC Ec-AMP-D1
Citrus sinensis
SEQ ID NO: 749 MERSVRLFSTVLLVLLLASEMGLRAAEARICESQSHRFKGPCVSKSNCAAVCQTEGFHGGHCRGFRRRCFCTKRC

[0175] The specified polypeptide may contain a fusion protein.

[0176] Table 20 (SEQ ID NO: 750) describes sequences used for translational fusion using a nucleotide sequence that encodes a synthetic phloem targeting polypeptide (SEQ ID NO: 641) and a synthetic thionine polypeptide (SEQ ID NO: 650) . Capital letters (non-bold) indicate the phloem-targeting sequence, capital letters in bold indicate the fusion of the two peptide sequences (Table 20) encoding the phloem-targeted bioactive priming polypeptide.

Table 20. Translational fusion of a phloem targeting sequence with a thionin-derived polypeptide

Translational fusion of a phloem targeting sequence to a thionin polypeptide (synthetic) SEQ ID NO: 750 MSTATFVDIIIAILLPPLGVFLRFGCGVEFWICLVLTLLGYIPGIIYAIYVLTKRTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCRCTRPCVFDEK

Additional modifications

[0177] In addition, polypeptides with D-amino acids, β2-amino acids, β3-amino acids, homoamino acids, gamma amino acids, peptidoids, N-methylamino acids, and other non-naturally occurring amino acid mimetics and derivatives can be chemically synthesized.

[0178] These polypeptides can be modified either by natural processes, such as post-translational processing, or using chemical modification techniques well known in the art. Modifications can occur anywhere on the polypeptide, including at the polypeptide backbone, at the amino acid side chains, and at the amino or carboxyl terminus. The same type of modification may be carried out equally or to varying degrees at multiple sites on a polypeptide. Also, the polypeptide may contain many types of modifications.

[0179] Peptides can be branched, for example, as a result of ubiquitination, and can be cyclic, with or without branching. Cyclic, branched and branched cyclic polypeptides may arise from natural post-translational processes or may be produced by synthetic means.

[0180] Modifications include acetylation, acid addition, acylation, ADP-ribosylation, aldehyde addition, alkylamide addition, amidation, amination, biotinylation, carbamate addition, addition of chloromethyl ketones, covalent attachment of a nucleotide or nucleotide derivative, cross-linking, cyclization, formation of disulfide bonds, demethylation, ester addition, covalent crosslinking, cysteine-cysteine disulfide formation, pyroglutamate formation, formylation, gamma-carboxylation, glycosylation, GPI-anchor formation, hydrazide addition, hydroxamic acid addition, hydroxylation, iodination, lipid addition, methylation, myristiolation, oxidation, pegylation, proteolytic processing, phosphorylation, prenylation, palmitoylation, purification label addition, pyroglutamyl addition, racemization, selenoylation, sulfonamide addition, sulfation e, transfer RNA mediated addition of amino acids to proteins, such as arginylation, ubiquitination, and urea addition. (See, for example, Creighton et al. (1993) Proteins - Structure and Molecular Properties, 2nd Ed., T. E. Creighton, W. H. Freeman and Company, New York; Johnson, ed. (1983) Posttranslational Covalent Modification Of Proteins, Academic Press , New York; Seifter et al. (1990) Meth. Enzymol., 182: 626-646; Rattan et al. (1992) Ann. N. Y. Acad. Sci., 663: 48-62; etc.).

[0181] Using known methods for constructing proteins and recombinant DNA technology, variants can be obtained to improve or change the characteristics of the polypeptides described herein. Such variants include deletions, insertions, inversions, repeats, duplications, extensions, and substitutions (eg, conservative substitutions) chosen according to general rules well known in the art so as to have little effect on activity.

[01892] The specified polypeptide may contain an amino acid sequence at least 70% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0183] The specified polypeptide may contain an amino acid sequence at least 75% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0184] The specified polypeptide may contain an amino acid sequence at least 80% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0185] The specified polypeptide may contain an amino acid sequence at least 85% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0186] The specified polypeptide may contain an amino acid sequence at least 90% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0187] The specified polypeptide may contain an amino acid sequence at least 95% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0188] The specified polypeptide may contain an amino acid sequence at least 98% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

[0189] The specified polypeptide may contain an amino acid sequence at least 99% identical to any of SEQ ID NO: 1-768, while the specified polypeptide has primer bioactivity.

II. Production of bioactive priming polypeptides

[0190] Methods and approaches are provided for cloning, genetic modification, and expression of bioactive priming polypeptides (e.g., flagellins), and said bioactive priming polypeptides (e.g., Bt.4Q7Flg22) using methods well known and widely used by one of skill in the art. The methods described herein may be used with any of the bioactive priming polypeptides as described herein, including, respectively, any of flagellins, flagellin-associated polypeptides, thionins, harpin-like (HpaG-like) polypeptides, EF-Tu, CSF-α, or RHPP, and/or any combination thereof.

[0191] Bioactive priming polypeptides can be presented as a free polypeptide, immobilized on the surface of a particle, or impregnated onto a matrix or into a matrix. A number of expression systems can be used to generate a free polypeptide.

[0192] Flagellin-derived full coding sequences, partial coding sequences (flagellin polypeptides), and flagellin-associated polypeptides can be overexpressed in a Bacillus strain, such as Bacillus thuringiensis strain BT013A, Bacillus cereus, or Bacillus subtilis. Flagellins and flagellin-derived polypeptides are cloned using an appropriate expression vector to produce significant amounts of said polypeptide.

[0193] For example, to facilitate cloning of target nucleotides that encode a bioactive priming polypeptide or polypeptides as described herein, an E. coli compatible pSUPER shuttle vector was constructed by fusing the backbone of the pBC plasmid described above with the E. coli cloning vector pUC57 in compatible restriction sites of the BamHI endonuclease. The resulting pSUPER vector carries dual selectable markers (for selection on ampicillin in E. coli and selection on tetracycline in Bacillus spp). Cloning was performed by PCR amplification of target nucleotides with specific primers synthesized with 15 bp spanning the pSUPER insertion site. The specific gene encoding polypeptides were fused to the pSUPER vector using an In-Fusion HD Cloning Kit (Clontech). Sequence verified pSUPER constructs were amplified using reverse and forward primers suitable for the pBC backbone. The resulting PCR products were self-ligated to generate the pBC plasmid, which was used to transform the B30 donor strain of Bacillus spp. The final construct was verified to be completely intrageneric using Sanger sequencing.

[0194] Bioactive primer polypeptides/peptides as described herein are produced in large quantities for use in fields and orchards using a free expression system that can use a strain of Bacillus subtilis and/or Bacillus thuringiensis as a strain for putative heterologous expression. The base expression plasmid, called pFEe4B, consists of an E. coli region (=e) and a Bacillus region (=pFE). The e region is derived from pUC19 and allows selection and amplification of the vector from E. coli for cloning purposes. It contains the beta-lactamase gene (bla), which confers resistance to beta-lactam antibiotics such as ampicillin and other penicillin derivatives, and an E. coli origin of replication, which allows the vector to propagate. The pFE region allows selection and amplification of the plasmid from Bacillus spp. and directs the expression of the heterologous polypeptide/peptide of interest. Accordingly, it contains a gene conferring resistance to tetracycline (tetL) as well as a replication protein gene (repU) responsible for amplifying the plasmid in Bacillus spp., both of which are derived from the natural plasmid pBC16 of Bacillus cereus. The pFEe4B expression cassette contains a secretion signal (amyQ), a cloning site and a terminator (rspD), where the former ensures the secretion of the expressed protein/peptide from the cells of the host strain into the environment around the cells, and the latter prevents transcription outside of the open reading frame of interest. Expression in pFEe4B is driven by a modified auto-inducible promoter that initiates expression after the culture reaches sufficient optical density. In the pFEe4b expression system, expression is controlled by the IPTG-inducible promoter sequence from Bacillus subtilis. Said promoter consists of a modified constitutive promoter in combination with an E. coli lac repressor (lacI) and a ribosome binding site. Accordingly, expression from pFEe4B encoded polypeptides/peptides is dependent on the presence of suitable inducing agents such as isopropyl-beta-D-1-thiogalactopyranoside (IPTG). However, other pFe systems suitable for the expression of polypeptides as described herein do not require induction for expression of such systems. The pFEe4 plasmid further carries the E. coli lacI gene under the control of the Bacillus licheniformis penicillase promoter to prevent expression of the polypeptide/peptide as described herein in the absence of any inducing agent.

[0195] Other commercially available expression vectors, for example, any derived from Bacillus subtilis, may also be suitable for use. Other expression vectors were chosen to generate recombinant bioactive priming polypeptides based on the following essential criteria: the recombinant microorganism is non-pathogenic and is considered a "generally regarded as safe" (GRAS) organism, does not exhibit significant codon shift, and is capable of secreting extracellular proteins directly into the culture medium , providing a cell-free variant or variants of bioactive primer polypeptides.

[0196] Other expression systems common in the art can be used to express bioactive primer polypeptides in a similar manner.

[0197] Bioactive priming polypeptides as described herein can be generated and purified either using protein tag(s) by affinity purification or using protease digestion column methods to release unlabeled polypeptide or polypeptide. Methods for applying this approach to obtain unbound variants of bioactive primer polypeptides are well known and understood by a person skilled in the art.

[0198] Protein tags typically contain a relatively small sequence of amino acids embedded in the translated polypeptide, essentially providing a molecular "tether" for the bioactive priming polypeptide of interest. They are widely used to promote the expression and purification of recombinant polypeptides. The polyhistidine (His) tag was chosen for affinity purification of the bioactive priming polypeptides as described. The His-tag can be fused to either the N-terminus or the C-terminus of the polypeptide. His tags are often combined with other tags for dual tagging. Labels for bioactive primer polypeptides may be suitable for affinity purification. These labels can also be cleaved from bioactive priming polypeptides using specific proteases and specific protease column cleavage methods to release a purified, unlabeled, bioactive priming polypeptide or full-length precursor protein of interest. These methods are also common and well known to one of skill in the art. Other labels that can be used are known in the art and include FLAG tags, antibody epitopes, streptavidin/biotin, and other purification tools. Another suitable label is the glutathione-S-transferase (GST) label.

[0199] Protein labels can be incorporated into a plasmid to produce a polypeptide. Ideally, said plasmid contains, in addition to the sequence encoding the polypeptide of interest, a secretion signal (eg, amyE or amyQ secretion signal) to promote secretion, and a protein tag (eg, glutathione-S-transferase) to increase the stability of said polypeptide, with thus improving production and stability. In preferred cases, a protein tag (eg, GST) is linked to the polypeptide using a linker sequence containing a consensus cleavage sequence. This may provide for the addition of a targeted kinase capable of cleaving said tag and releasing the purified, isolated polypeptide. A suitable consensus cleavage sequence may include an enterokinase cleavage sequence (SEQ ID NO: 772), which can be cleaved, for example, simply using bovine enterokinase.

[0200] Accordingly, a method for producing a polypeptide is provided, comprising producing a fusion protein containing any polypeptide as described herein and an enterokinase (EK) cleavage site by fermentation, which serves to increase the activity and stability of said polypeptide. The fusion protein encoded by said plasmid may further comprise a protein tag (e.g., a polyhistidine (His) tag, FLAG tag, antibody epitope, streptavidin/biotin, glutathione S-transferase (GST), or any combination of the above), wherein the enterokinase cleavage site contains a connecting region connecting the polypeptide and the protein label. Said fusion protein may also contain a secretion signal. Said secretion signal may comprise an amyE or amyQ secretion signal (eg, SEQ ID NO: 769), or may comprise any of SEQ ID NO: 563-570 as described above. Said polypeptide containing an enterokinase (EK) cleavage site may be more stable and can be produced in a higher fermentation yield than a polypeptide lacking an enterokinase (EK) cleavage site. If desired, an enterokinase (eg, bovine enterokinase) can be used to activate (eg, isolate) the polypeptide of interest from said fusion protein. Said enterokinase can be applied "in situ" to maximize the stability of the bioactive priming polypeptide prior to administration.

[0201] Bioactive primer polypeptides can be obtained in synthetic form using commercially available peptide synthesis technologies that provide high purity polypeptides. Synthetic production of bioactive primer polypeptides involves the general methods of solid phase peptide synthesis, well known to the person skilled in the art. Methods of chemical synthesis include: staged assembly of peptides from amino acid precursors, during which the elongation of the peptide continues due to the amino acid conjugation reaction, followed by the removal of the reversible protective group. Solid-phase peptide synthesis is used to add a covalent bonding step, which attaches the synthesized peptide chain to an insoluble polymeric support, due to which the anchored peptide can be completed in several cycles. These extension reactions are brought to completion and then the synthesized polypeptide is recovered from the solid support by filtration and washing steps. MS and HPLC analyzes are performed after completion of synthesis and purification.

[0202] Any of the bioactive priming polypeptides as described herein for flagellin-associated polypeptides (Tables 1-5), harpin-like (HpaG-like) polypeptides (Tables 10 and 11), phytosulfokine (FSK-α) polypeptides (Table 12) , RHPP (Table 13-15), elongation factor Tu (EF-Tu polypeptides) (Tables 16 and 17), thionin and thionin-like polypeptides (Table 19) can be presented in synthetic forms.

[0203] In addition, such methods can be used to obtain and use conserved auxiliary sequences, preferably referred to as signature (SEQ ID NO: 542-548), signal anchor sort (SEQ ID NO: 549-562) sequences, and secretion sequences (SEQ ID NO: 563-570).

[0204] Retro-inverse variants can also be obtained synthetically or produced chemically. Synthetic polypeptides produced in the all-D conformation are prepared by replacing all L-amino acid residues with their D-enantiomers, resulting in the reversed or all-D retroisomer of the Flg polypeptide. Solid phase synthesis is used to obtain retro-inverse variants of the Flg polypeptide or polypeptides. After synthesis and purification of the retro-inverse polypeptide or polypeptides, the amino acid composition is confirmed using mass spectrometry of the Flg polypeptide or polypeptides. The purity of the retro-inverse polypeptide or polypeptides is then confirmed to be greater than or equal to 95% using HPLC analysis. Retro-inverse variants of the Flg polypeptide or polypeptides are further characterized using HPLC retention time, relative molecular weight and amino acid composition (IC50, μM). The production of retro-inverse variants using recombinant DNA technology typically involves the use of non-ribosomal protein synthesis mechanisms.

[0205] Retro-inverse synthetic bioactive Flg priming polypeptides obtained using solid-phase synthesis are tested for the ability to bind FLS2 or alternative FLS receptors, for example, FLS3, also found in plants. Competitive ELISA ELISA experiments are used to confirm the binding affinity of retro-inverse Flg-associated polypeptides to plant FLS receptors.

Recombinant bacteria expressing bioactive priming polypeptides

[0206] Also provided is a recombinant microorganism that expresses or overexpresses the polypeptide. The specified polypeptide contains polypeptides as described above for the specified composition. For example, the specified polypeptide may contain: the specified flagellin or flagellin-associated polypeptide according to (a); or a mutant flagellin or flagellin-associated polypeptide according to (b); or a mutant flagellin or flagellin-associated polypeptide according to (c); or the harpin or harpin-like polypeptide of (g); or RHPP according to (i); or a KTI polypeptide according to (j); or the EF-Tu polypeptide of (l); or a fusion polypeptide at (n); or the FSK polypeptide according to (o); or the thionin or thionin-like polypeptide of (q).

[0207] Said polypeptide may be overexpressed by said microorganism. Said recombinant microorganism may include a microorganism capable of producing recombinant bioactive primer polypeptides or precursors thereof in an efficient manner. The preferred microorganism is of the genus Bacillus, is a bacterium of the genus Paenibacillus, a fungus of the genus Penicillium, a bacterium of the genus Glomus, a bacterium of the genus Pseudomonas, a bacterium of the genus Arthrobacter, a bacterium of the genus Paracoccus, a bacterium of the genus Rhizobium, a bacterium of the genus Bradyrhizobium, a bacterium from the genus Azosprillium, a bacterium from the genus Enterobacter, a bacterium from the genus Escherichia, or any combination thereof.

[0208] Said recombinant microorganism may include a bacterium from the genus Bacillus, a bacterium from the genus Paenibacillus, or any combination thereof.

[0209] For example, said microorganism may include a bacterium of the genus Bacillus mycoides, Bacillus pseudomycoides, Bacillus cereus, Bacillus thuringiensis, Bacillus megaterium, Bacillus subtilis, Bacillus firmus, Bacillus aryabhattai, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus circulans, Bacillus flexus, Bacillus nealsonii, Bacillus pumulis, Paenibacillus, or a combination thereof.

[0210] A person skilled in the art often uses methods and approaches to determine and verify the genus and species of bacteria. The general method involves obtaining chromosomal DNA isolated from bacteria and PCR amplification of the 16s rRNA region using universal primers (ACTCCTACGGGAGGCAGCAGT) and (GGGTTGCGCTCGTTG/AC). The PCR amplicons are then purified and sequenced to correctly identify a suitable bacterial strain, such as a specific strain of the genus Bacillus.

[0211] A person skilled in the art is generally aware of protocols for processing samples to obtain chromosomal DNA, transforming the DNA of genes encoding polypeptides using a plasmid that produces these polypeptides in a host bacterium, for example, a strain of Bacillus.

[0212] The proposed Bacillus strains can produce any bioactive priming polypeptide as described herein, or a combination thereof. For example, said strain may include:

(a) Bacillus aryabhattai CAP53 (NRRL No. B-50819),

(b) Bacillus aryabhattai CAP56 (NRRL No. B-50817),

(c) Bacillus flexus BT054 (NRRL No. B-50816),

(d) Paracoccus kondratievae NC35 (NRRL No. B-50820),

(e) Bacillus mycoides BT155 (NRRL No. B-50921),

(f) Enterobacter cloacae CAP12 (NRRL No. B-50822),

(g) Bacillus nealsonii BOBA57 (NRRL No. NRRL B-50821),

(h) Bacillus mycoides EE118 (NRRL No. B-50918),

(i) Bacillus subtilis EE148 (NRRL No. B-50927),

(j) Alcaligenes faecalis EE107 (NRRL No. B-50920),

(k) Bacillus mycoides EE141 (NRRL NO. B-50916),

(l) Bacillus mycoides BT46-3 (NRRL No. B-50922),

(m) a member of the family Bacillus cereus EE128 (NRRL No. B-50917),

(n) Paenibacillus massiliensis BT23 (NRRL No. B-50923),

(o) a member of the family Bacillus cereus EE349 (NRRL No. B-50928),

(p) Bacillus subtilis EE218 (NRRL No. B-50926),

(q) Bacillus megaterium EE281 (NRRL No. B-50925),

(r) Bacillus cereus EE-B00377 (NRRL B-67119);

(s) Bacillus pseudomycoides EE-B00366 (NRRL B-67120),

(t) Bacillus mycoides EE-B00363 (NRRL B-67121),

(u) Bacillus pumilus EE-B00143 (NRRL B-67123),

(v) Bacillus thuringiensis EE-B00184 (NRRL B-67122),

(w) Bacillus mycoides EE116 (NRRL No. B-50919),

(x) a member of the family Bacillus cereus EE417 (NRRL No. B-50974),

(y) Bacillus subtilis EE442 (NRRL No. B-50975),

(z) Bacillus subtilis EE443 (NRRL No. B-50976),

(aa) a member of the family Bacillus cereus EE444 (NRRL No. B-50977),

(bb) Bacillus subtilis EE405 (NRRL No. B-50978),

(cc) a member of the family Bacillus cereus EE439 (NRRL No. B-50979),

(dd) Bacillus megaterium EE385 (NRRL No. B-50980),

(ee) a member of the family Bacillus cereus EE387 (NRRL No. B-50981),

(ff) Bacillus circulans EE388 (NRRL No. B-50982),

(gg) Bacillus thuringiensis EE319 (NRRL No. B-50983),

(hh) a member of the family Bacillus cereus EE377 (NRRL No. B-67119),

(ii) Bacillus mycoides EE363 (NRRL No. B-67121),

(jj) Bacillus pseudomycoides EE366 (NRRL No. B-67120);

(kk) Bacillus thuringiensis BT013A (NRRL No. B-50924);

[0213] or any combination thereof. Each of these strains was deposited with the United States Department of Agriculture (USDA) Agricultural Research Service (ARS) located at 1815 North University Street, Peoria, Illinois 61604 U.S.A. and assigned the NRRL deposit numbers listed in round brackets. Strains (a)-(d), (f) and (g) were deposited on March 11, 2013. Strains (e), (h)-(q), (w) and (kk) were deposited on March 10, 2014. Strains (x)-(ff) were deposited on September 10, 2014 Strain (gg) was deposited on September 17, 2014 Strains (r)-(v), (hh), (ii) and (jj) were deposited on August 19 2015 Bacillus thuringiensis BT013A also known as Bacillus thuringiensis 4Q7.

[0214] The isolation and characterization of these strains are described in the examples given in international publication WO/2017/161091, incorporated herein in its entirety by reference. For ease of identification of the organism, international publication WO/2017/161091 A1 also provides partial sequences of 16S ribosomal RNA for each of these strains in the sequence listing and in Table 17.

[0215] Any of the recombinant microorganisms can be used to overexpress the bioactive priming polypeptide as described herein for flagellin-associated polypeptide (Tables 1-5), harpin or harpin-like (HpaG-like) polypeptide (Table 10 or 11), phytosulfokines (FSK -α) polypeptide (Table 12), RHPP (Table 13-15), EF-Tu polypeptide (Table 16-17), and thionin or thionin-like polypeptide (Table 19).

[0216] Said recombinant microorganism may include a mixture of two or more of any of the recombinant microorganisms described herein.

[0217] The specified recombinant microorganism can be inactivated. Inactivation leads to the production of microorganisms that are unable to reproduce. Microbial inactivation can be beneficial, for example, because it allows the microorganism to be delivered to a plant or plant growth medium while reducing or eliminating any detrimental effects that the living microorganism may have on the plant or the environment. Said recombinant microorganism may be inactivated by any physical or chemical means such as heat treatment, gamma irradiation, X-ray irradiation, UV-A irradiation, UV-B irradiation, or treatment with a solvent such as glutaraldehyde, formaldehyde, hydrogen peroxide, acetic acid, bleach, chloroform or phenol, or any combination of these.

III. Compositions

[0218] A composition is provided for bioactively priming a plant or plant part to improve growth, yield, health, increase longevity, productivity, and/or vitality of a plant or plant part, and/or reduce abiotic stress in a plant or plant part, and/ or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering plant architecture. Said composition contains any of the following: a polypeptide as described herein, or any combination of said polypeptides, and an agrochemical or carrier; or any combination of these polypeptides as described herein.

[0219] Said composition may consist essentially of bioactive primer polypeptides or polypeptides as described herein.

[0220] Said composition may consist primarily of bioactive primer polypeptides, with the remainder of the composition being agrochemicals or carriers. More specifically, said composition may contain from about 0.00001% to about 95% of said polypeptides, from about 0.1 to about 80 wt. % agrochemicals, and from about 5 to about 50 wt. % carrier based on the total weight of the composition. Alternatively, said composition may contain from about 0.01 to about 5 wt. % of these polypeptides, from about 0.2 to about 70 wt. % agrochemicals, and from about 10 to about 30 wt. % carrier based on the total weight of the composition, or the specified composition may contain from about 0.05 wt. % to about 1 wt. % of these polypeptides, from about 30 to about 60 wt. % agrochemicals, and from about 40 to about 69 wt. % carrier based on the total weight of the composition. Alternatively, said composition may contain any detectable amount of said polypeptides, and from about 0.1 to about 80 wt. % agrochemicals, and from about 5 to about 50 wt. % carrier based on the total weight of the composition.

[0221] The specified composition may include either an agrochemical or a carrier that is associated with the specified polypeptide in nature.

[0222] Said agrochemical may not occur naturally in combination with said polypeptide.

[0223] Said agrochemical may include, but is not limited to, a preservative, a buffering agent, a wetting agent, a surfactant, a coating agent, a monosaccharide, a polysaccharide, an abrasive, a pesticide, an insecticide, a herbicide, a nematocide, a bactericide, a fungicide, a miticide, a fertilizer, a biostimulant, a coloring agent, a humectant, an osmoprotectant, an antibiotic, an amino acid, a biological control agent, or a combination thereof.

[0224] If the specified composition includes an amino acid, the specified amino acid can be provided separately from the amino acids that contains the specified polypeptide. For example, an isolated amino acid may be used. Suitable amino acids include any naturally occurring or non-naturally occurring amino acids. For example, said composition may contain cysteine.

[0225] Said agrochemical may contain an acid, such as an acid present in the chemical synthesis of any of the polypeptides described herein. For example, hydrochloric acid, acetic acid, or trifluoroacetic acid may be present when the polypeptide is synthesized, for example, by fermentation.

[0226] In cases where the specified agrochemical is an acid, it can be from about 0.001 to about 30 wt. %, from about 0.01 to about 20 wt. %, or from about 0.1 to about 5 wt. % of the total weight of the composition.

[0227] Unless otherwise indicated, each agrochemical can be from about 0.1 to about 60 wt. %, from about 0.5 to about 50 wt. %, or from about 10 to about 30 wt. % of the total weight of the composition.

[0228] Where said composition includes a preservative, said preservative may include dichlorophene and benzyl alcohol semiformal preservatives (PROXEL from ICI or ACTICIDE RS from Thor Chemie, and KATHON MK from Dow Chemical), and isothiazolinone derivatives such as alkylisothiazolinones and benzisothiazolinones (ACTICIDE MBS from Thor Chemie). Additional examples of suitable preservatives include MIT (2-methyl-4-isothiazolin-3-one), BIT (1,2-benzisothiazolin-3-one, which can be purchased from Avecia, Inc. as PROXEL GXL as a solution in sodium hydroxide and dipropylene glycol), 5-chloro-2-(4-chlorobenzyl)-3(2H)-isothiazolone, 5-chloro-2-methyl-2H-isothiazol-3-one, 5-chloro-2-methyl-2H-isothiazole -3-one, 5-chloro-2-methyl-2H-isothiazol-3-one-hydrochloride, 4,5-dichloro-2-cyclohexyl-4-isothiazolin-3-one, 4,5-dichloro-2-octyl -2H-isothiazol-3-one, 2-methyl-2H-isothiazol-3-one, 2-methyl-2H-isothiazol-3-one-calcium chloride complex, 2-octyl-2H-isothiazol-3-one, semiformal benzyl alcohol or any combination of the above.

[0229] Where said composition includes a buffering agent, said buffering agent may contain potassium, phosphoric acid, phosphate salt, citric acid, citrate salt, sulfate salt, MOPS, or HEPES. The specified buffer agent can stabilize the polypeptide in the composition.

[0230] Where said composition includes a wetting agent, said wetting agent may contain silicones, polyoxyethoxylates, polysorbates, polyethylene glycol and derivatives thereof, ethoxylates, plant treatment oils, and polysaccharides.

[0231] Where said composition includes a surfactant, said surfactant may contain a dark petroleum oil, a dark petroleum distillate, a fatty acid polyol ester, a polyethoxylated fatty acid ester, an arylalkyl polyoxyethylene glycol, a monobutyl polyoxyethylene polyoxypropylene monobutyl ether, alkylamine acetate, alkylarylsulfonate, polyhydric alcohol, alkyl phosphate, alcohol ethoxylate, alkylphenol ethoxylate, alkylphenol ethoxylate, alkoxylated polyhydric alcohol, aolkylpolyethoxyether, alkyl polyoxyethylene glycerin, ethoxylated soybean oil derivatives, silicone surfactant; or any combination of the above. Surfactants can be included in various compositions, including foliar treatment compositions.

[0232] Where said composition includes a coating agent, said coating agent may contain a tackifier, polymers, fillers, or bulking agents.

[0233] Said tackifier may include, but is not limited to, carboxymethyl cellulose, natural and synthetic polymers in the form of powders, granules, or latexes such as gum arabic, chitin, polyvinyl alcohol, and polyvinyl acetate, and natural phospholipids such as cephalins and lecithins. , and synthetic phospholipids. Tackifying agents include agents, preferably consisting of an adhesive polymer, which may be natural or synthetic, that does not have a phytotoxic effect on the seed to be coated. Additional tackifying agents that may be included, singly or in combination, include, for example, polyesters, polyester ethers, polyanhydrides, polyether urethanes, polyester amides; polyvinyl acetates; polyvinyl acetate copolymers; polyvinyl alcohols and tylose; polyvinyl alcohol copolymers; polyvinylpyrrolidones; polysaccharides, including starches, modified starches and starch derivatives, dextrins, maltodextrins, alginates, chitosan and cellulose, cellulose esters, cellulose ethers and esters of cellulose ethers, including ethylcellulose, methylcellulose, hydroxymethylcellulose, hydroxypropylcellulose and carboxymethylcellulose; fats; oils; proteins, including casein, gelatin, and zeins; gum arabic; shellacs; vinylidene chloride and vinylidene chloride copolymers; lignosulfonates, in particular calcium lignosulfonates; polyacrylates, polymethacrylates and acrylic copolymers; polyvinyl acrylates; polyethylene oxide; polybutenes, polyisobutenes, polystyrene, polybutadiene, polyethyleneamines, polyethyleneamides; polymers and copolymers of acrylamide; polyhydroxyethyl acrylate, methylacrylamide monomers; and polychloroprene, or any combination thereof. Tackifying agents can be used in a number of compositions, including those used in a seed treatment.

[0234] Where said composition includes an abrasive agent, said abrasive agent may contain talc, graphite, or a combination of the former and the latter.

[0235] A humectant is a hygroscopic substance that helps retain moisture. Where said composition includes a humectant, said humectant may contain: glycerol, glycerol, a glycerol derivative (e.g., glycerol monostearate, glycerol triacetate, triacetin, propylene glycol, hexylene glycol, or butylene glycol), triethylene glycol, tripopolypropylene glycol, glyceryl triacetate, sucrose, tagatose, sugar an alcohol or polyhydric sugar alcohol (eg, glycerin, sorbitol, xylitol, mannitol, or manthitol), a polymeric polyhydric alcohol (eg, polydextrose, collagen, aloe, or aloe vera gel), or an alpha hydroxy acid (eg, lactic acid, honey, molasses, quillia, hexametaphosphate sodium, lithium chloride or urea). Synthetic moisturizers may also include butylene glycol and tremella extract.

[0236] Where said composition includes a pesticide, said pesticide may contain an insecticide, herbicide, fungicide, bactericide, nematocide, miticide, or any combination thereof.

[0237] Where said composition includes an insecticide, said insecticide may contain clothianidin, imidacloprid, an organophosphorus compound, carbamate, pyrethroid, acaricide, alkyl phthalate, boric acid, borate, fluoride, sulfur, haloaromatic urea, hydrocarbon ester, biological insecticide or any combination of the above. For example, said insecticide may contain clothianidin or imidacloprid.

[0238] Said agrochemical may contain a herbicide. Said herbicide may contain 2,4-D, 2,4-DB, acetochlor, acifluorfen, alachlor, ametrine, atrazine, aminopyralid, benefin, bensulfuron, bensulfuron-methyl, bensulide, bentazone, bispyribac sodium, bromacil, bromoxynil, butylate, carfentrazone , chlorimuron, 2-chlorophenoxyacetic acid, chlorsulfuron, chlorimuron-ethyl, cletodim, clomazone, clopyralid, cloransulam, chloro-2-methylphenoxypropanoic acid dimethylamine salt (CMPP-P_DMA), cycloate, DCPC, desmedifam, dicambu, dichlobenil, diclofop, 2, 4-dichlorophenol, dichlorophenoxyacetic acid, dichlorprop, dichloroprop-P, diclosulam, diflufenzopyr, dimethenamide, 2,4-dichlorophenoxyacetic acid dimethylamine salt, diquat, diuron, DSMA, endotal, EPTC, ethalfluralin, etofumesate, fenoxaprop, fluazifop-P, flucarbazone, flufeacet, flumetsulam, flumiclorac, flumioxazine, fluometuron, fluroxypyr, fluoroxypyr 1-methylheptyl ether, fomesafen, fomesafen sodium, foramsulfuron, glufosinate, ammonium glufosinate, glyphosate, halosulfuron, halosul furon-methyl, hexazinon, 2-hydroxyphenoxyacetic acid, 4-hydroxyphenoxyacetic acid, imazametabenz, imazamox, imazapic, imazakquin, imazethapir, isoxaben, isoxaflutol, lactofen, linuron, mazapyr, MCPA, MCPB, mecoprop, mecoprop-P, mesotrione, C- metolachlor, metribuzin, metsulfuron, metsulfuron-methyl, molinate, MSMA, napropamide, naptalam, nicosulfuron, norflurazon, oryzalin, oxadiazon, oxyfluorophen, paraquat, pelargonic acid, pendimethalin, phenmedifam, picloram, primisulfuron, prodiamine, promethrin, pronamide, propanil, prosulfuron , pyrazon, pyrithiobac, pyroxasulfone, quinclorac, quizalofop, rimsulfuron, sethoxydim, siduron, simazine, sulfentrazone, sulfometuron, sulfosulfuron, tebuthiuron, terbacil, thiazopyr, thifensulfuron, thifensulfuron-methyl, thiobencarb, trialkoxydim, trimethyl, triasulfuron, triasulfuron , triclopyr, trifluralin, triflusulfuron, or any combination thereof.

[0239] Where said composition includes a nematocide, said nematocide may contain Bacillus firmus, fluopyram, nematicide antibiotics such as abamectin; carbamate nematicides such as acetoprol, Bacillus chitonosporus, chloropicrin, benclothiaz, benomyl, Burholderia cepacia, carbofuran, carbosulfan and cleotocard; dazomet, dibromochlorpropane (DBCP), DCIP, alanicarb, aldicarb, aldoxycarb, oxamyl, diamidaphos, fenamiphos, fostietan, phosphamidon, cadusafos, chlorpyrifos, diclofenthion, dimethoate, etoprofos, fensulfothion, fostiazate, harpins, heterophos, imicyafos, isamidophos, methomylazophos , mecarfon, Myrothecium verrucaria, Paecilomyces lilacinus, Pasteuria nishizawae (including their spores), phorate, phosphocarb, terbufos, thionazine, triazophos, thioxazafen, dazomet, 1,2-dichloropropane, 1,3-dichloropropene, furfural, iodomethane, metam , methyl bromide, methyl isothiocyanate, xylenol, or any combination thereof. For example, said nematocide may include a strain of Bacillus firmus i-2580, Pasteuria nishizawae (including their spores), or fluopyram.

[0240] Where said composition includes a bactericide, said bactericide may contain streptomycin, penicillins, tetracyclines, oxytetracycline, kasugamycin, ampicillin, oxolinic acid, chlortetracycline, copper oxide, or any combination thereof. For example, said bactericide may contain oxytetracycline.

[0241] Biological control agents are broadly defined as microorganisms that can be used in place of synthetic pesticides or fertilizers. Where said composition includes a biological control agent, said biological control agent may contain Bacillus thuringiensis, Bacillus megaterium, Bacillus mycoides, isolate J, Bacillus methylotrophicus, Bacillus vallismortis, Chromobacterium subtsugae, Delftia acidovorans, Streptomyces lydicus, Streptomyces colombiensis, Streptomyces galbus K61, Penicillium bilaii, Bacillus subtilis lipopeptide producing strain, Bacillus amyloliquefaciens lipopeptide producing strain, Bacillus firmus strain or Bacillus pumilus strain.

[0242] Said agrochemical may include a fungicide. Said fungicide may contain aldimorph, ampropylphos, potassium ampropylphos, andoprim, anilazine, azaconazole, azoxystrobin, benalaxyl, benodanil, benomyl, benzamacryl, benzamacryl-isobutyl, benzovindiflupyr, bialaphos, binapacryl, biphenyl, bitertalone, blasticidin-S, boscalidine, burimatone , butiobate, calcium polysulfide, capsimycin, captafol, captan, carbendazim, carvone, quinomethionate, chlobentiazone, chlorphenazole, chloroneb, chlorpicrin, chlorothalonil, chlosolinate, closilacone, kufraneb, cymoxanil, cyproconazole, cyprodinil, cyprofuram, debacarb, diclofluanid, dicloflunid, dicloflunid diclomezin, dicloran, diethofencarb, dimethirimol, dimethomorph, dimoxystrobin, dinikonazole, dinikonazole-M, dinocap, diphenylamine, dipyrithione, dithalymphos, dithianone, dodemorph, dodin, drazoxolone, edifenphos, epoxyconazole, etaconazole, etirimol, etridiasol, famoxadone, fenapanil, phenarimol, fenbuconazole, fenfuram, fenitropan, fenpiclonil, fenpropidine, fenpropimorph, fentin acetate, fentin hydroxide, ferbam, fe rimzon, fluazinam, fludioxonil, flumetover, fluoromide, fluoxastrobin, fluquinconazole, flurprimidol, flusilazole, flusulfamide, flutolanil, flutriafol, folpet, fosetyl-aluminum, fosetyl sodium, phthalide, fuberidazole, furalaxil, furametpyr, furametpyr, furazol, cyconacarbonil, furazol, furs furmecyclox, guazatin, hexachlorobenzene, hexaconazole, hymexazole, imazalil, imibenconazole, iminoctadine, iminoctadine albesilate, iminoctadine triacetate, iodocarb, iprobenphos (IBP), iprodione, irumamycin, isoprothiolane, isovaledione, kasugamycin, kresoxim-methyl, copper formulations such as: copper hydroxide, copper naphthenate, copper oxychloride, copper sulfate, copper oxide, copper oxinate and bordeaux liquid, mancopper, mancozeb, maneb, meferimzone, mepanipyrim, mepronil, metconazole, metazyl, metasulfocarb, metfuroxam, metiram, metomeclam, metsulfax, mildiomycin, myclobutanil , myclozolin, nickel dimethyldithiocarbamate, nitrotal-isopropyl, nuarimol, ofuraz, oxadixyl, oxamocarb, oxolinic acid, oxycarboxy, oxyphene thiin, paclobutrazol, pefurazoate, penconazole, pencycuron, fosdifen, picoxystrobin, pimaricin, piperalin, polyoxin, polyoxorim, probenazole, prochloraz, procymidone, propamocarb, propanosine sodium, propiconazole, propineb, prothiocinazole, pyrazophos, pyrifenox, pyrimethanil, pyrochilon, pyroxyfur, quinconazole, quintosine (PCNB), strobilurin, sulfur and sulfur formulations, tebuconazole, tecloftalam, technasine, tetcyclacis, tetraconazole, thiabendazole, thiocyophene, thifluzamide, thiophanate-methyl, thioximide, tolclofos-methyl, tolylfluanid, triadimefon, triadimenol, triazol triazbutyl, triazbutyl , triazoxide, trichlamide, tricyclazole, triclopyr, tridemorph, trifloxystrobin, triflumizole, triforin, uniconazole, validamycin A, vinclozolin, viniconazole, zarilamide, cineb, cyram, and Dagger G, OK-8705, OK-8801, a-(1, 1-dimethylethyl)-(3-(2-phenoxyethyl)-1H-1,2,4-triazole-1-ethanol, a-(2,4-dichlorophenyl)-[3-fluoro-3-propyl-1H- -1,2,4-triazole-1-ethanol, a-(2,4-dichlorophenyl)-[3-methoxy-a-methyl-1H-1,2,4-triazole-1-ethanol, a-(5 -methyl-1,3-dioxane-5- yl)-[3-[[4-(trifluoromethyl)-phenyl]-methylene]-1 H-1,2,4-triazole-1-ethanol, (5RS,6RS)-6-hydroxy-2,2,7 ,7-tetramethyl-5-(1H-1,2,4-triazol-1-yl)-3-octanone, (E)-a-(methoxyimino)-N-methyl-2-phenoxy-phenylacetamide, 1-isopropyl {2-methyl-1-[[[1-(4-methylphenyl)-ethyl]-amino]-carbonyl]-propyl}carbamate, 1-(2,4-dichlorophenyl)-2-(1 H-1,2 ,4-triazol-1-yl)-ethanone-O-(phenyl methyl)-oxime, 1-(2-methyl-1-naphthalenyl)-1H-pyrrole-2,5-dione, 1-(3,5- dichlorophenyl)-3-(2-propenyl)-2,5-pyrrolidinedione, 1-[(diiodomethyl)-sulfonyl]-4-methylbenzene, 1-[[2-(2,4-dichlorophenyl)-1,3-dioxolane -2-yl]-methyl]-1H-imidazole, 1-[[2-(4-chlorophenyl)-3-phenyloxiranyl]-methyl]-1 H-1,2,4-triazole, 1-[1-[ 2-[(2,4-dichlorophenyl)-methoxy]-phenyl]-ethenyl]-1H-imidazole, 1-methyl-5-nonyl-2-(phenylmethyl)-3-pyrrolidinol, 2',6'-dibromo- 2-methyl-4'-trifluoromethoxy-4'-trifluoromethyl-1, 3-thiazolecarboxanilide, 2,2-dichloro-N-[1-(4-chlorophenyl)-ethyl]-1-ethyl-3-methylcyclopropanecarboxamide, 2, 6-dichloro-5-(methylthio)-4-pyrimidinylthiocyanate, 2,6-dichloro-N-(4-trifluoromethylbenzyl)-benzamide, 2,6-dix lor-N-[[4-(trifluoromethyl)-phenyl]-methyl]-benzamide, 2-(2,3,3-triiodo-2-propenyl)-2H-tetrazole, 2-[(1-methylethyl)-sulfonyl ]-5-(trichloromethyl)-1,3,4-thiadiazole, 2-[[6-deoxy-4-O-(4-0-methyl-(3-D-glycopyranosyl)-a-D-glucopyranosyl]-amino] -4-methoxy-1H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile, 2-aminobutane, 2-bromo-2-(bromomethyl)pentanedinitrile, 2-chloro-N-(2,3-dihydro- 1,1,3-trimethyl-1 H-inden-4-yl)-3-pyridinecarboxamide, 2-chloro-N-(2,6-dimethylphenyl)-N-(isothiocyanatomethyl)-acetamide, 2-phenylphenol (OPP) , 3,4-dichloro-1-[4-(difluoromethoxy)-phenyl]-pyrrole-2,5-dione, 3,5-dichloro-N-[cyano[(1-methyl-2-propynyl)-oxy] -methyl]-benzamide, 3-(1,1-dimethylpropyl-1-oxo-1H-indene-2-carbonitrile, 3-[2-(4-chlorophenyl)-5-ethoxy-3-isoxazolidinyl]-pyridine, 4 -chloro-2-cyano-N,N-dimethyl-5-(4-methylphenyl)-1 H-imidazole-l-sulfonamide, 4-methyl-tetrazolo[1,5-a]quinazolin-5(4H)-one , 8-(1,1-dimethylethyl)-N-ethyl-N-propyl-1,4-dioxaspiro[4,5]decan-2-methanamine, 8-hydroxyquinoline sulfate, 9H-xanthene-2-[(phenylamino)- carbonyl]-9-carboxylic hydrazide, bis -(1-methylethyl)-3-methyl-4-[(3-methylbenzoyl)-oxy]-2,5-thiophene dicarboxylate, cis-1-(4-chlorophenyl)-2-(1H-1,2,4- triazol-1-yl)-cycloheptanol, cis-4-[3-[4-(1,1-dimethylpropyl)-phenyl-2-methylpropyl]-2,6-dimethyl-morpholine hydrochloride, ethyl[(4-chlorophenyl) -azo]-cyanoacetate, potassium bicarbonate, sodium methanetetrathiol, methyl-1-(2,3-dihydro-2,2-dimethyl-inden-1-yl)-1H-imidazole-5-carboxylate, methyl-N-( 2,6-dimethylphenyl)-N-(5-isoxazolylcarbonyl)-DL-alaninate, methyl N-(chloroacetyl)-N-(2,6-dimethylphenyl)-DL-alaninate, N-(2,3-dichloro-4 -hydroxyphenyl)-1-methylcyclohexanecarboxamide, N-(2,6-dimethylphenyl)-2-methoxy-N-(tetrahydro-2-oxo-3-furanyl)-acetamide, N-(2,6-dimethylphenyl)-2- methoxy-N-(tetrahydro-2-oxo-3-thienyl)-acetamide, N-(2-chloro-4-nitrophenyl)-4-methyl-3-nitrobenzenesulfonamide, N-(4-cyclohexylphenyl)-1,4, 5,6-tetrahydro-2-pyrimidinamine, N-(4-hexylphenyl)-1,4,5,6-tetrahydro-2-pyrimidinamine, N-(5-chloro-2-methylphenyl)-2-methoxy-N- (2-oxo-3-oxazolidinyl)-acetamide, N-(6-methoxy)-3-pyridinyl)-cyclopropanecarboxymes e, N-[2,2,2-trichloro-1-[(chloroacetyl)-amino]-ethyl]-benzamide, N-[3-chloro-4,5-bis(2-propynyloxy)-phenyl]-N '-methoxymethanimidamide, N-formyl-N-hydroxy-DL-alanine sodium salt, 0,0-diethyl[2-(dipropylamino)-2-oxoethyl]-ethylphosphoramidothioate, 0-methyl-S-phenyl-phenylpropylphosphoramidothioate, S-methyl -1,2,3-benzothiadiazol-7-carbothioate and spiro[2H]-1-benzopyran-2,1'(3'H)-isobenzofuran]-3'-one, N-trichloromethyl)thio-4-cyclohexane- 1,2-dicarboximide, tetramethylthioperoxydicarboxylic acid diamide, methyl-N-(2,6-dimethylphenyl)-N-(methoxyacetyl)-DL-alaninate, 4-(2,2-difluoro-1,3-benzodioxol-4-yl )-1-H-pyrrole-3-carbonitrile, or any combination of the above.

[0243] When these polypeptides are formulated or used in combination with commercially available fungicides, these compositions can further increase the level of protection to improve the prevention or spread of the disease in the plant. The combination of these polypeptides with a fungicide can protect the plant from primary or secondary fungal infection, which can occur if the plant has been damaged or weakened by abiotic stress or disease.

[0244] The strobilurin fungicide may comprise strobilurin A, strobilurin B, strobilurin C, strobilurin D, strobilurin E, strobilurin F, strobilurin G, strobilurin H, azoxystrobin, trifloxystrobin, kresoxim methyl, fluoxastrobin, picoxystrobin, or any combination thereof.

[0245] The strobilurin fungicide may contain a non-naturally occurring strobilurin fungicide such as azoxystrobin, trifloxystrobin, kresoxim-methyl, fluoxastrobin, or any combination thereof. For example, the strobilurin fungicide may contain trifloxystrobin, fluoxastrobin, or picoxystrobin. Strobilurin fungicides are used to control a number of fungal diseases, including water mold, downy mildew, powdery mildew, leaf spot and leaf rot fungi, fruit rot fungi, and rust fungi. They are suitable for processing a variety of crops, including cereals, field crops, fruits, tree nuts, vegetables, lawns and ornamental plants.

[0246] The triazole fungicide may contain prothioconazole, imidazole, imidazyl, prochloraz, propiconazole, triflumizole, diniconazole, flusilazole, penconazole, hexaconazole, cyproconazole, myclobutanil, tebuconazole, difenoconazole, tetraconazole, fenbuconazole, epoxiconazole, metconazole, fluquinconazole, or any combination of these .

[0247] Bioactive primer polypeptides can be delivered in combination with strobilurins and triazole fungicides, in particular fluoxastrobin or trifloxystrobin in combination with prothioconazole.

[0248] In addition, said fungicide may contain azoxystrobin, carboxin, difenoconazole, fludioxonil, fluxapiroxad, ipconazole, mefenoxam, pyraclostrobin, silthiopham, sedaxan, thiram, triticonazole, or any combination thereof.

[0249] In addition to foliar fungicides as described herein, bioactive priming polypeptides can be provided in combination with a fungicide, insecticide, nematicide, bactericide, and miticide, or any agrochemical that is a biological agent.

[0250] Said agrochemical may include a fertilizer. Said fertilizer may include ammonium sulfate, ammonium nitrate, ammonium sulfate nitrate, ammonium chloride, ammonium bisulfate, ammonium polysulfide, ammonium thiosulfate, aqueous ammonia, anhydrous ammonia, ammonium polyphosphate, aluminum sulfate, calcium nitrate, calcium ammonium nitrate, calcium sulfate, calcined magnesite, calcite limestone, calcium oxide, calcium nitrate, dolomitic limestone, hydrated lime, calcium carbonate, diammonium phosphate, monoammonium phosphate, magnesium nitrate, magnesium sulfate, potassium nitrate, potassium chloride, magnesium potassium sulfate, potassium sulfate, sodium nitrates, magnesian limestone, magnesia, urea, formaldehyde ureas, ammonium urea nitrate, sulfur-coated urea, polymer-coated urea, isobutylidene-diurea, K ₂ SO4-Mg ₂ SO ₄ , kainite, sylvinite, kieserite, Epsom salts, elemental sulfur, marl, ground oyster shells, fish meal, cake, fish fat, blood meal, phosphate ore, superphosphates, slag, bone meal, wood ash, manure, volatile droppings mice, peat moss, compost, wet sand, cottonseed meal, feather meal, crab meal, fish emulsion, humic acid, or any combination thereof.

[0251] Said fertilizer may include liquid fertilizer or dry fertilizer.

[0252] Said agrochemical may contain a microfertilizer containing boric acid, borate, boric frit, copper sulfate, copper frit, copper chelate, sodium tetraborate decahydrate, iron sulfate, iron oxide, iron ammonium sulfate, iron frit, iron chelate, manganese sulfate , manganese oxide, manganese chelate, manganese chloride, manganese frit, sodium molybdate, molybdic acid, zinc sulfate, zinc oxide, zinc carbonate, zinc frit, zinc phosphate, zinc chelate, or any combination thereof.

[0253] Said agrochemical may contain an insecticide, wherein said insecticide comprises an organophosphorus compound, a carbamate, a pyrethroid, an acaricide, an alkyl phthalate, boric acid, a borate, fluoride, sulfur, a haloaromatic urea, a hydrocarbon ester, a biological insecticide, or any combination thereof.

[0254] Where said composition includes a biostimulant, said biostimulant may comprise a seaweed extract, elicitor, polysaccharide, monosaccharide, protein extract, soy extract, humic acid, plant hormone, plant growth regulator, or any combination thereof.

[0255] Various coloring agents can be used, including organic chromophores classified as nitroso, nitro, azo, including monoazo, bisazo, and polyazo, diphenylmethane, triarylmethane, xanthene, methane, acridine, thiazole, thiazine, indamine, indophenol, azine, oxazine, anthraquinone, phthalocyanine, or any combination thereof.

[0256] The specified composition may additionally contain a carrier.

[0257] The carrier of said composition may include, but is not limited to, water, peat, wheat, bran, vermiculite, clay, pasteurized soil, calcium carbonate, calcium bicarbonate, dolomite, gypsum, bentonite, clay, phosphorite, phosphorus compound, titanium dioxide , humus, talc, alginate, activated carbon, or a combination thereof.

[0258] Said composition may be in the form of an aqueous solution, slurry or dispersion, emulsion, solid such as powder or granules, or any other form required for the application of said composition to a plant or plant part.

[0259] Bioactive priming polypeptides such as flagellin and flagellin-associated polypeptides, thionin (defensin family), harpin-like HpaG, EF-Tu, or other growth-promoting or growth-altering bioactive priming polypeptides such as CSF-α and RHPP can be represented in the form of compositions that can be applied exogenously and/or endogenously to a plant or plant part, and provide enhanced plant growth, plant productivity and improved health status in said plant or plant part, as described in more detail below.

[0260] These bioactive primer polypeptides may be added singly or in combination as a composition suitable for use as a benefit agent for plants and/or plant parts.

[0261] To obtain a combination, these polypeptides can be prepared and delivered in the form of a purified polypeptide, either as a genetically fused sequence on a single recombinant vector, or separately using different recombinant vectors.

[0262] Bioactive primer polypeptides can also be produced and delivered to a plant or plant part as polypeptides from multiple active constructs in a fusion protein. Examples include the delivery of multiple flagellin-associated polypeptides produced in sequence, with protease cleavage sites separating all polypeptides, as is known to those skilled in the art. Such fusion proteins may include any combination of bioactive priming polypeptides as described herein, including bioactive priming polypeptides from different classes, such as combinations of flagellin-associated polypeptides with RHPP. Bioactive priming polypeptides can also be used as fusion proteins with plant binding domains that can target said polypeptides to specific locations in the plant where they are most needed or needed for their activity to be beneficial.

[0263] In addition, these polypeptides can be added to the proposed compositions in the form of synthetic compounds.

[0264] The flagellin and flagellin-associated bioactive priming polypeptides as described herein may be provided singly or in combination containing at least two and up to more bioactive priming polypeptides to provide a composition that meets the specific needs of the plant for a wide range of desired responses. at the host and agricultural systems.

[0265] If the composition includes a retro-inverse form of a bioactive Flg priming polypeptide (e.g., RI Bt.4Q7 Flg 22 (SEQ ID NO: 376), said polypeptide exhibits improved stability and less degradation over time, providing greater activity on the plant membrane surface cells, which enhances the ability of said polypeptide to bind to the receptor and uptake by the plant Retro-inverse forms of such Flg-associated bioactive primer polypeptides are used to provide improved stability of the agricultural composition, provided that the specified Flg polypeptide or polypeptides show improved protection against proteolytic cleavage, which contributes to the overall higher activity and longer shelf life of the composition.

[0266] Where said polypeptide comprises an RHPP polypeptide, said composition may further comprise flagellin or a flagellin-associated polypeptide. Said RHPP polypeptide may comprise SEQ ID NO: 600. The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 1-525, 532, 534, 536, 538, 540, 571-586, and 751-752, or any combination of them. For example, said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226, 571, and 752. In some instances, said RHPP polypeptide may comprise SEQ ID NO: 600, and said flagellin or flagellin-associated polypeptide may comprise SEQ ID NOs: 226.

[0267] These polypeptides may be formulated in combination with an accessory polypeptide. Signature polypeptides (SEQ ID NOs: 542-548), signal anchor sorting polypeptides (SEQ ID NOs: 549-562), and secretion polypeptides (SEQ ID NOs: 563-570) can be combined with bioactive priming polypeptides as described to target these polypeptides/peptides (tables 1-5) on the surface of the plant cell membrane for improved binding and activation of Flg-associated receptors. Said method for efficiently delivering and binding said polypeptide to a plant provides growth promotion benefits as well as enhanced protection for the plant or plant part.

[0268] For example, harpin or HpaG-like bioactive priming polypeptides as described herein can be used in combination with accessory polypeptides as described in Tables 6-8), signature polypeptides (SEQ ID NOs: 542-548), signal anchor sorting polypeptides (SEQ ID NO: 549-562) and/or secretion polypeptides (SEQ ID NO: 563-570). These accessory polypeptides, when used in combination with HpaG-like bioactive priming polypeptides, are suitable for targeting and delivering harpin-like bioactive priming polypeptides to the surface of plant cell membranes, improving contact with the plant cell membrane, and provide a means of transmission facilitating effective contact and penetration of the harpin-like (HpaG- similar) polypeptide in the plant or in the environment of the plant cell (apoplast).

[0269] One or more of said EF-Tu polypeptides may optionally be combined with said flagellin or flagellin-associated polypeptide. The amino acid sequence of said EF-Tu polypeptide or polypeptides may comprise SEQ ID NOs: 616 and/or 617. The amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 1-525, 532, 534, 536, 538, 540, 571-586 and 751-753, or any combination thereof. For example, the amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise SEQ ID NO: 571. In another example, said composition may comprise EF-Tu polypeptides comprising SEQ ID NOs: 616 and 617, and flagellin or flagellin-associated polypeptide comprising SEQ ID NO: 226, 571, 572, or combinations thereof. In another example, an EF-Tu polypeptide or polypeptides comprising SEQ ID NO: 616 and/or 617 may be combined with flagellin or a flagellin-associated polypeptide comprising SEQ ID NO: 226. Alternatively, said composition may comprise one or more EF-Tu polypeptides alone (eg, containing SEQ ID NO: 616 and/or 617). These EF-Tu polypeptides (eg, SEQ ID NOs: 616 and 617) can be further modified by N-terminal acetylation.

[0270] In addition, the EF-Tu polypeptide or EF-Tu polypeptide and flagellin or flagellin-associated polypeptide can be combined with a harpin or harpin-like polypeptide. For example, the amino acid sequence of said harpin or harpin-like polypeptide may comprise SEQ ID NO: 587.

[0271] Said composition may contain any of the following combinations: (a) flagellin or flagellin-associated polypeptides, wherein the amino acid sequences of said flagellin or flagellin-associated polypeptides comprise SEQ ID NOs: 571, 295, 300, 293, and 580; or 295, 300, 293 and 580; or 571, 295, 293 and 580; or 571, 300, 293 and 580; or 571, 293 and 580; or 571, 295, 293; or (b) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, and cellobiose, cellulose, chitin, chitosan, or any combination thereof; or (c) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, and a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises SEQ ID NO: 591 ; or (d) a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises SEQ ID NO: 587, and a CSF polypeptide, wherein the amino acid sequence of said CSF polypeptide comprises SEQ ID NO: 598; or (e) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, 752, or 571 or any combination thereof, and EF-Tu polypeptides, wherein the amino acid sequences of said EF polypeptides -Tu contain SEQ ID NO: 616 and 617; or (f) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, 540, 752, or 571, or any combination thereof; or (g) an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide comprises SEQ ID NO: 600; or (h) flagellin or flagellin-associated polypeptide, wherein the amino acid sequences of said flagellin or flagellin-associated polypeptide comprise SEQ ID NO: 226, 540, 226, 752, or 571, or any combination thereof, and an RHPP polypeptide, wherein the amino acid sequence of said the RHPP polypeptide contains SEQ ID NO: 600; or (i) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide contains SEQ ID NO: 226, and an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide contains SEQ ID NO: 600.

IV. Application

[0272] The composition and methods for agricultural use described herein can be applied to any plant species and/or their seeds. These compositions and methods are generally used with agronomically important seeds.

[0273] Said seed may be a transgenic seed from which a transgenic plant can be grown in which a transgenic event occurs that provides, for example, tolerance to a particular herbicide or herbicide combination, increased disease resistance, improved tolerance to insect attack, drought, stress and/or increased yield.

[0274] Said seed may include a selection trait, including, for example, a selection trait for disease tolerance.

[0275] In some cases, the seed includes at least one transgenic trait and at least one selection trait.

[0276] Compositions of bioactive primer polypeptides and methods of using said polypeptides can be used to treat any suitable type of seed, including, but not limited to, row and vegetable crops. For example, one or more plants or one or more plant parts or seeds of one or more plants may include textile banana (Manila hemp) (Musa textilis), forage alfalfa (Medicago sativa), alfalfa in seed (Medicago sativa), almond (Prunus dulcis), aniseed (Pimpinella anisum), apple (Malus sylvestris), apricot (Prunus armeniaca), areca palm (Areca catechu), arracacchu (Arracacia xanthorrhiza), arrowroot (Maranta arundinacea), artichoke (Cynara scolymus) , asparagus (Asparagus officinalis), avocado (Persea americana), millet (American millet) (Pennisetum americanum), Bambara groundnut (Vigna subterranea), banana (Musa paradisiaca), barley (Hordeum vulgare), dry, edible, grain beans (Phaseolus vulgaris), green beans (Phaseolus and Vigna spp.), fodder beet (Beta vulgaris), red beet (Beta vulgaris), sugar beet (Beta vulgaris), fodder sugar beet (Beta vulgaris), sugar beet seed (Beta vu lgaris), bergamot (Citrus bergamia), betel nut (Areca catechu), black pepper (Piper nigrum), black locust (Acacia mearnsii), various blackberries (Rubus spp.), blueberries (Vaccinium spp.), brazil nuts ( Bertholletia excelsa), breadfruit (Artocarpus altilis), garden beans, dried (Vicia faba), garden beans, green (Vicia faba), broccoli (Brassica oleracea, var. botrytis), bicolor sorghum (Sorghum bicolor), broom sorghum (Sorghum bicolor), Brussels sprouts (Brassica oleracea, var. gemmifera), buckwheat (Fagopyrum esculentum), red cabbage, white cabbage, savoy cabbage (Brassica oleracea, var. capitata) , Chinese cabbage (Brassica chinensis), fodder cabbage (Brassica spp.), cocoa (Theobroma cacao), cantaloupe (Cucumis melo), cumin seeds (Carum carvi), cardamom (Elettaria cardamomum), Spanish artichoke (Cynara cardunculus), carob (Ceratonia siliqua), food carrot (Daucus carota spp.sativa), feed carrot (Daucus carota sativa), cashew nut (Anacardium occidentale), cassava (manioc) (Manihot esculenta), castor bean (Ricinus communis), cauliflower (Brassica oleracea , var. botrytis), root celery (Apium graveolens, var. rapaceum), celery (Apium graveolens), chayote (Sechium edule), any kind of cherry (Prunus spp.), edible chestnut (Castanea sativa), chickpeas (mutton peas) (Cicer arietinum), chicory (Cichorium intybus), chicory greens (Cichorium intybus), dry chili pepper (all varieties) (Capsicum spp.(annuum)), fresh chili pepper (all varieties) (Capsicum spp.(annuum)), cinnamon (Cinnamomum verum), citron (Citrus medica) , citronella (Cymbopogon citrates; Cymbopogon nardus), clementine (Citrus reticulata), clove (Eugenia aromatica; Syzygium aromaticum), fodder clover (all varieties) (Trifolium spp.), seeded clover (all varieties) (Trifolium spp.), cocoa (Theobroma cacao), coconut (Cocos nucifera), taro (Colocasia esculenta), coffee (Coffea spp.), kola nut, all varieties (Cola acuminata), colza (rapeseed) (Brassica napus), grain corn (maize) (Zea mays), corn ( maize) for silage (Zea mays), corn (maize) as a vegetable crop (Zea mays), mung bean (Valerianella locusta), cotton, all varieties (Gossypium spp.), cottonseed, all varieties (Gossypium spp.), grain cowpea (Vigna unguiculata), green cowpea (Vigna unguiculata), cranberry (Vaccinium spp.), watercress (Lepidium sativum), cucumber (Cucumis sativus), currant, all varieties (Ribes spp.), cream apple (Annona reticulate ), taro (Colocasia esculenta), dates (Phoenix dactylifera), oleifera moringa (Moringa oleifera), durra (sorghum) (Sorghum bicolour), durum wheat (Triticum durum), bambar groundnut (Vigna subterranea), edo (eddo) (Xanthosoma spp.; Colocasia spp.), Eggplant (Solanum melongena), Endive (Cichorium endivia), Fennel (Foeniculum vulgare), Fenugreek (Trigonella foenum-graecum), Fig (Ficus carica), Hazelnut (Corylus avellana), Furcraea (Furcraea macrophylla) ), flax for fiber (Linum usitatissimum), oil flax (flaxseed) (Linum usitatissimum), formium (New Zealand flax) (Phormium tenax), garlic, dry (Allium sativum), garlic, green (Allium sativum), geranium (Pelargonium spp.; Geranium spp.), ginger (Zingiber officinale), gooseberry, all varieties (Ribes spp.), gourd (Lagenaria spp; Cucurbita spp.), mutton peas (chickpeas) (Cicer arietinum), grapes (Vitis vinifera), grapefruit (Citrus paradisi), raisin grapes (Vitis vinifera), table grapes (Vitis vinifera), wine grapes (Vitis vinifera), esparto grass (Lygeum spartum), cocksfoot (Dactylis glomerata), bicolor sorghum (Sorghum bicolor , var. sudanense), groundnut (peanut) (Arachis hypogaea), guava (Psidium guajava ), Guinean corn (Guinea sorghum) (Sorghum bicolor), hazelnut (hazel) (Corylus avellana), hemp fiber (Cannabis sativa spp.indica), manila hemp (abaca) (Musa textilis), Bombay hemp (Crotalaria juncea), hemp seed (marijuana) (Cannabis sativa), henequen (Agave fourcroydes), henna (Lawsonia inermis), hops (Humulus lupulus), horse bean (Vicia faba), horseradish (Armoracia rusticana), hybrid corn (Zea mays), indigo (Indigofera tinctoria), jasmine (Jasminum spp.), Jerusalem artichoke (Helianthus tuberosus), jovar (sorghum) (Sorghum bicolor), jute (Corchorus spp.), kale (Brassica oleracea, var. acephala), kapok (Ceiba pentandra), kenaf (Hibiscus cannabinus), kohlrabi (Brassica oleracea var. gongylodes), lavender (Lavandula spp.), leek (Allium ampeloprasum; Allium porrum), lemon (Citrus limon), lemongrass ( Cymbopogon citratus), lentils (Lens culinaris), lespedeza, all varieties (Lespedeza spp.), lettuce (Lactuca sativa var. capitata), lime, sour (Citrus aurantifolia), lime, sweet (Citrus limetta), linseed (oil flax crop) (Linum usitatissimum), licorice (Glycyrrhiza glabra), lychee (Litchi chinensis), loquat (Eriobotrya japonica), lupine, all varieties (Lupinus spp.), macadamia (Australian nut) (Macadamia spp.ternifolia), nutmeg (Myristica fragrans), magway (Agave atrovirens), maize (maize) (Zea mays), maize (corn) for silage (Zea mays), corn (hybrid) (Zea mays), common corn (Zea mays), mandarin (Citrus reticulata), common beet (fodder beet) (Beta vulgaris), mango (Mangifera indica), cassava (cassava) (Manihot esculenta), sourju ( mixture of cereals) (mixture of Triticum spp. and Secale cereale), pine cone (Mespilus germanica), gourds (melon, Cucumis melo), not including watermelon, broom sorghum (Sorghum bicolor), American millet, common millet (Pennisetum americanum), millet cane (Pennisetum americanum), finger millet (Eleusine coracana), Italian millet (Setaria italica), Japanese barnyard grass (Echinochloa esculenta), African millet (Pennisetum americanum), common millet (Panicum miliaceum), mint, all varieties (Mentha spp.), mulberries for berries, all varieties (Morus spp.), mulberries for breeding silkworms (Morus alba), higher fungi (Agaricus spp.); Pleurotus spp.; Volvariella), mustard (Brassica nigra; Sinapis alba), nectarine (Prunus persica, var. nectarina), New Zealand flax (Phormium tenax), Abyssinian guizotia (Guizotia abyssinica), nutmeg (Myristica fragrans), fodder oats (Avena spp.), oil palm (Elaeis guineensis), okra (Abelmoschus esculentus), olive (Olea europaea), onion seed (Allium cepa), dry onion (Allium cepa), spring onion (Allium cepa), opium poppy (Papaver somniferum ), orange (Citrus sinensis), bitter orange (Citrus aurantium), ornamentals (various), palm (Borassus flabellifer), oil palm for palm kernel oil (Elaeis guineensis), oil palm (Elaeis guineensis), sago palm (Metroxylon sagu), papaya (melon tree) (Carica papaya), parsnip (Pastinaca sativa), peas, food dry, for cereals (Pisum sativum), green peas (Pisum sativum), peach (Prunus persica), peanut (peanut) (Arachis hypogaea), pear (Pyrus communis), pecan (Carya illinoensis), black pepper (Piper nigrum), dry pepper (Capsicum spp.), persimmon (Diospyros kaki; Diospyros virginiana), pigeon pea (Cajanus cajan), pineapple (Ananas comosus), pistachio tree (Pistacia vera), plantain (Musa sapientum), plum (Prunus domestica), pomegranate (Punica granatum), pomelo (Citrus grandis), poppy seed (Papaver somniferum), potato (Solamum tuberosum), oil palm for palm kernel oil (Elaeis guineensis), sweet potato (Ipomoea batatas), plum (Prunus domestica), food gourd (Cucurbita spp.), gourd (Cucurbita spp. ), feverfew (Chrysanthemum cinerariaefolium), quebracho (Aspidosperma spp.), Australian walnut (Macadamia spp.ternifolia), quince (Cydonia oblonga), cinchona (Cinchona spp.), quinoa (Chenopodium quinoa), ramie (Boehmeria nivea), colza (Brassica napus), raspberry, all varieties (Rubus spp.), red beet (Beta vulgaris), bent grass (Agrostis spp.), Chinese nettle (Boehmeria nivea), rhubarb (Rheum spp.), rice (Oryza sativa; Oryza glaberrima), rose (Rose spp.), rubber tree (Hevea brasiliensis), w Swedish turnip (rutabaga) (Brassica napus, var. napobrassica), rye (Secale cereale), chaff seed (Lolium spp.), safflower (Carthamus tinctorius), sainfoin (Onobrychis viciifolia), oat root (Tragopogon porrifolius), sapodilla (Achras sapota), satsuma (tangerine/tangerine) (Citrus reticulata), scorzonera (black root) (Scorzonera hispanica), sesame (Sesamum indicum), shea butter (nut) (Vitellaria paradoxa), sisal (Agave sisalana), sorghum (Sorghum bicolor), sorghum, broom (Sorghum bicolor), sorghum , durra (Sorghum bicolor), sorghum, guinea (Sorghum bicolor), sorghum, jowar (Sorghum bicolor), sorghum, sweet (Sorghum bicolor), soy (Glycine max), soy hay (Glycine max), spelled (Triticum spelta), spinach (Spinacia oleracea), pumpkin (Cucurbita spp.), wild strawberry (Fragaria spp.), sugar beet (Beta vulgaris), fodder sugar beet (Beta vulgaris), sugar beet seed (Beta vulgaris), fodder sugar cane (Saccharum officinarum ), sugar cane for the production of sugar or alcohol (Saccharum officinarum), sugar tr Roof thatch (Saccharum officinarum), fodder sunflower (Helianthus annuus), oil sunflower (Helianthus annuus), Bombay hemp (Crotalaria juncea), swede (Brassica napus, var. napobrassica), swede (Brassica napus var. napobrassica), sweet corn (Zea mays), sweet lime (Citrus limetta), sweet pepper (Capsicum annuum), sweet potato (Iopmoea batatas), sweet sorghum (Sorghum bicolor), tangerine (Citrus reticulata), malanga (Xanthosoma sagittifolium), tapioca (cassava) (Manihot esculenta), taro (Colocasia esculenta), tea (Camelia sinensis), Abyssinian grass (Eragrostis abyssinica), timothy grass (Phleum pratense), tobacco (Nicotiana tabacum) ), tomato (Lycopersicon esculentum), lotus bird (Lotus spp.), triticale wheat, fodder (hybrid of Triticum aestivum and Secale cereale), tung tree (Aleurites spp.; Fordii), food turnip (Brassica rapa), fodder turnip (Brassica rapa ), urena (Congolese jute) (Urena lobata), vanilla (Vanilla planifolia), common vetch (Vicia sativa), walnut (Juglans spp., in particular Juglans regia), watermelon (Citrullus lanatus), wheat (Triticum aestivum), yam (Dioscorea spp.) or mate (Ilex paraguariensis) .

[0277] The compositions and methods as described herein may also be applied to lawn grass, ornamental grass, flowers, ornamental plants, trees, and shrubs.

[0278] Compositions containing these bioactive priming polypeptides are also suitable for use in nurseries, lawns and gardens, for floriculture or industrial cut flowers, and provide benefits for increased productivity, improved health protection, increased vitality and longevity plants. For example, they can be used for perennials, annuals, forcing bulbs or pseudobulbs, grasses, ground covers, trees, shrubs, ornamental plants (eg orchids, etc.), tropical plants and seedlings.

[0279] Compositions containing these bioactive primer polypeptides are suitable for treating plants, plant parts, and plant propagation material(s), e.g., any plant or plant part, such as seeds, roots, stems, flowering organs, rootstocks, grafts, bulbs, false bulbs, rhizomes, tubers, etc.

[0280] Bioactive primer polypeptides can be used as seed treatments to treat a variety of pests, diseases, nutrient deficiencies, while improving plant growth and productivity.

[0281] The seed coat or treatment compositions can be, for example, a composition in a liquid carrier, a slurry composition, or a powder composition that is applied along with standard additives that are used to make the seed treatment agent tacky to adhere to the seeds and their coverage. Suitable seed composition additives include: talcs, graphites, gums, stabilizing polymers, coating polymers, finishing polymers, glidants to promote seed flow and plantability, cosmetic agents, and cellulosic materials such as carboxymethyl cellulose, and etc. The bioactive seed treatment priming polypeptide may further comprise coloring agents and other such additives.

[0282] These bioactive primer polypeptides can be used alone as seed treatments or in combination with other additives such as fungicides, insecticides, inoculants, plant growth regulators, plant growth promoting microbes, fertilizers and fertilizer enhancers, seed nutrients, biological control agents, herbicide safeners and seedling diseases agents, and other conventional seed treatments.

[0283] The seed treatment composition as described herein may be applied to the seed in a suitable carrier such as water or a powder that is not harmful to the seed or the environment. Then the seeds are planted in the standard way.

[0284] Preferred seed treatments such as Bt.4Q7Flg22 (SEQ ID NO: 226 or SEQ ID NO: 571), Ec.Flg22 (SEQ ID NO: 526) and Gm.RHPP (SEQ ID NO: 600), are suitable for improving seedling development, accelerating germination, increasing the number of germinating seeds and improving seedling survival. In addition, these seed treatment compositions improve seed protection against microbial-associated diseases known to contact the seed or the soil around the seed and spread during the early stages of seedling development.

[0285] Said seed treatment composition may comprise a polypeptide as described herein and a fungicide, insecticide, nematocide, biological control agent, biostimulant, microbe, or any combination of the foregoing.

[0286] Said seed treatment composition may contain a polypeptide as described herein and clothianidin, Bacillus firmus, metalaxyl, or any combination of the above.

[0287] Said seed treatment composition may contain a polypeptide as described herein, clothianidin, and fluopyram.

[0288] Said seed treatment may contain a polypeptide as described herein, metalaxyl, and fluopyram.

[0289] Bioactive priming polypeptides can be applied directly to seeds as a solution or in combination with other commercially available additives. Solutions containing the water-soluble polypeptide may be sprayed or otherwise applied to the seed as a seed dressing or seed soak. Solids or dry materials containing soluble bioactive primer polypeptides are also suitable for promoting effective germination, growth and early seedling protection.

[0290] Bioactive primer polypeptides can be formulated with a solubilizing carrier such as water, a buffer (eg, citrate or phosphate buffer), and other auxiliary agents (ie, alcohol, other solvents), or any solubilizing agent. In addition, minor amounts of drying enhancers such as lower alcohols and the like can be used in the composition. Surfactants, emulsifiers and preservatives may also be added in minor (0.5% by volume or less) amounts to improve the stability of the seed coating product.

[0291] Seed treatments containing bioactive primer polypeptides may be applied using any commercially available seed treatment apparatus, or may also be applied using any acceptable non-commercial method or methods, such as using syringes or any other seed treatment device. . General treatments for coated seeds using bioactive primer polypeptides can be performed with Wintersteiger HEGE 11 (Wintersteiger AG, Austria, Germany) on seeds of major crops, namely corn, soybeans, wheat, rice and various vegetables. The performance of said seed treatment equipment can process a significant number of different types, sizes and volumes of seeds (20-3000 grams). The seeds are loaded into the tanks of the seed treatment apparatus. The choice of tank depends on the amount of seed to be processed and the size of the tank chosen: large tank 14.5L (covering 500-3000g seeds at a time); medium tank 7L (covering 80-800g seeds at a time); and a small tank of 1L (covering 20-100g seeds at a time). Other larger seed treatment systems are also available.

[0292] The seeds are guided towards the radial periphery of the rotating tanks by the centrifugal force generated by the centrifugal coater. A rotating disk located at the bottom of the tank distributes the seed treatment evenly over the surface of the seed. At this point, the centrifugation cycle begins, which causes the seeds to move in a circle around the center of the tank, coating the seeds evenly. The seed coater process begins when the seeds are evenly dispersed around the spreader. The seed treatment sample material (e.g., powder, semi-liquid, liquid; or slurry) may be applied to a rotating disc within rotating vessels used to evenly distribute the seed treatment to ensure uniform coating and dressing of the seed surface.

[0293] A constant airflow generated using compressed air (2-6 bar) can be used when coating the seeds to promote even coating of the seeds in the tank. The time required to coat the seeds depends on the number of seeds, the viscosity of the seed treater, and the type of seed being treated. The Seed Treatment Calculator is used to adjust all volumes for most major and cultivated commercial crops and the type of seed treatment applied.

[0294] The coating can be applied to seeds using a variety of methods, including, but not limited to, pouring or pumping, spraying or spraying to apply an aqueous solution containing bioactive primer polypeptides to or over the seed, spraying or applying to layer of seeds with or without the use of a conveyor system. Suitable mixing devices include drum mixers, mixing tanks or tumblers, or other fluid application devices, including troughs or drums where the seeds are placed during the coating process.

[0295] After processing and drying the seeds, they are transferred to a larger storage container(s). The seeds are dried either in air or in a continuous stream of air passed over the seeds. The seeds are then transferred to a separate container or bag for transport, transfer or storage.

[0296] Bioactive primer polypeptides can also be provided for delivery to the plant surface or plasma membrane of a plant as a foliar spray or seed treatment in the area around the plant or part of the plant.

[0297] The composition(s) with the bioactive primer polypeptide(s) may also be presented as a seed treatment or on a support, such as immobilized or impregnated on a particle, or as granules, such as those used for broadcast applications.

[0298] The bioactive primer polypeptides as described herein can be applied to plants and plant parts as an exogenous agent, by spraying, tillage, furrow at planting, seed treatment, dipping, or rinsing, or as an endogenous agent, by injection, inoculation , irrigation, infiltration, etc.

[0299] These polypeptides can be applied directly to the plant or to the area around the plant or part of the plant.

[0300] They may also be applied to a support material, which is then applied to the plant or plant part.

[0301] Compositions containing flagellin-associated bioactive priming polypeptides can also be used for direct delivery to a plant, plant tissue, or plant cell by various delivery methods, such as injection, inoculation, or infiltration (e.g., stomatal infiltration on a leaf). These polypeptides can also be used in such a way that they can move systemically through the plant and affect the signaling cascades in the plant, thus providing favorable and productive outcomes for the plant or plant part.

[0302] The retro-inverse bioactive Flg priming polypeptides as described in Table 4 or Table 5 can be used alone or in combination with any other flagellin, flagellin-associated, or other bioactive priming polypeptide sequences as described herein. Combinations of such flagellin and flagellin-associated bioactive RI primer polypeptides are suitable for use as plant protection agents and plant growth promoters.

[0303] Ancillary signature polypeptides (SEQ ID NOs: 542-548; Table 6), signal anchor sorting polypeptides (SEQ ID NOs: 549-562, Table 7), and secretion polypeptides (SEQ ID NOs: 563-570; Table 8) can be used in combination with any of the flagellin-encoding (Table 1) N- and/or C-terminal conserved sequences from Bacillus-derived flagellins (Table 2), flagellin-associated polypeptides: Flg22 and FlgII-28 (Table 3), retro- inverse forms of Flg22 and FlgII-28 (Table 4) or any other Flg (Table 5) as described herein.

[0304] For example, any of the Flg-associated bioactive priming polypeptides, or any combination thereof, may be presented in individual formulations and used either simultaneously or sequentially in separate formulations, or may be presented as a fusion protein(s). ) with ancillary sequences as described in Tables 6-8, and applied directly or individually to a plant or plant part.

[0305] Harpin-like polypeptides or RHPP polypeptides can provide functional benefits when applied both exogenously, for example, on the surface of a plant as a foliar spray, and apoplasticly (in the space outside the plant cell membrane) and endogenously (inside the plant cell/s the inner side of the plant cell membrane). RHPP polypeptides may also provide functional benefits when applied as a seed treatment.

[0306] Foliar or in-furrow application at planting harpin-like, HpaG-like polypeptides is suitable for enhancing growth, increasing biomass, greening or chlorophyll production in the plant.

[0307] A bioactive FSK-α priming polypeptide or polypeptides can be provided for delivery to the plant surface/plant plasma membrane as a foliar spray or seed treatment in the area around the plant, plant part or plant cell.

[0308] Compositions containing bioactive CSF-α primer polypeptides can also be provided for delivery to a plant, plant tissue, or plant cell by various means, for example, by injection, inoculation, or infiltration (for example, adding directly or pre-into cell culture).

V. Methods of application

[0309] Methods are provided for increasing growth, yield, improving health, increasing longevity, productivity, and/or vitality of a plant or plant part, and/or reducing abiotic stress in a plant or plant part, and/or protecting a plant or plant part from diseases, insects and/or nematodes, and/or enhancement of the innate immune response of the plant or plant part, and/or changes in plant architecture. Said method may include the use of said polypeptide or said composition as described herein on a plant, on a plant part or plant growth medium, or in the rhizosphere in an area surrounding the plant or plant part, to improve growth, yield, health, increase longevity, productivity and/or vitality of the plant or plant part, and/or reduction of abiotic stress in the plant or plant part; and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering the architecture of the plant.

[0310] Alternatively, said method may include using said polypeptide or said composition as described herein in a plant growth medium to improve growth, yield, health, lifespan, productivity, and/or vitality of a plant or plant part. , which is intended to grow in said plant growth medium, and/or reduce abiotic stress in a plant or plant part, which is intended to be grown in said plant growth medium, and/or protect a plant or plant part, which is intended to be grown in said growth medium for plants, disease, insects and/or nematodes, and/or enhancement of the innate immune response, and/or alteration of the architecture of the plant or plant part to be grown in said plant growth medium.

[0311] Another method includes the use of a recombinant microorganism as described herein on a plant, on a plant part or in a plant growth medium, or in the rhizosphere in the area surrounding the plant or plant part, to improve growth, yield, health, increase the duration life, productivity and/or vitality of the plant or plant part, and/or reduction of abiotic stress in the plant or plant part; and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering the architecture of the plant. Said recombinant microorganism expresses a polypeptide, and the expression of said polypeptide is increased compared to the level of expression of said polypeptide in a wild-type microorganism of the same species under the same conditions.

[0312] Also provided are methods using said bioactive primer polypeptides to increase the overall productivity of a plant in fields, orchards, flower beds, nurseries, woodlots, farms, lawns, orchards, garden centers, or seed plots. Embodiments and uses using these bioactive primer polypeptides are also suitable for improving plant growth, health, and productivity in a variety of crops (monocots and dicots), e.g., corn, wheat, rice, sugarcane, soybeans, sorghum, potatoes, and various vegetables.

[0313] Also provided is a method of "priming with a bioactive polypeptide" by directly applying said polypeptides, which can be applied either exogenously on the surface of plant cells or endogenously within a plant and/or plant cell. Polypeptides are provided for delivery to a plant surface or plant plasma membrane, or into a plant, plant tissue or cell, and are suitable for regulating developmental processes that lead to improved growth phenotypes, e.g., increased total biomass, vegetative growth, seed filling, seed size. and the number of seeds that contribute to the increase in the overall yield of agricultural plants.

[0314] The use of retro-inverse Flg polypeptides in the form of agricultural formulations can provide improved protection of plants from diseases and abiotic stresses, while synergistically improving growth, productivity and yield while maintaining improved plant health and performance over longer periods of time.

[0315] The choice of natural L-form (table 3) or retro-inverse D-form (table 4) Flg-associated polypeptides may depend on the environment, plant/crop or combination of plant/culture and environment. In addition, the timing of the application (eg foliar spray) during the growing season is important. Retro-inverse bioactive Flg priming polypeptides are characterized by increased binding affinity to the surface of cell membranes. Because of these features, the RI forms of bioactive Flg primer polypeptides can be used to improve abiotic stress tolerance in a plant or plant part.

[0316] In addition, retro-inverse forms of RI Ec.Flg22 and RI Bt.4Q7Flg22 may be suitable for promoting stomatal closure under drought and heat stress conditions and improving yield under these conditions. Controlling stomatal closure using a Flg-associated bioactive priming polypeptide in a plant during periods of environmental stress can help regulate water loss and stabilize turgor pressure in the plant under adverse environmental conditions.

[0317] According to these methods, the specified polypeptide or the specified composition may contain: the Flg22 polypeptide, while the amino acid sequence of the specified Flg22 polypeptide contains any of SEQ ID NO: 226-300 and 571-573; a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450; or any combination of the above, to protect the plant or plant part from disease and/or enhance the innate immune response of the plant or plant part.

[0318] According to the specified methods, the specified polypeptide or the specified composition may contain: the FlgII-28 polypeptide, while the amino acid sequence of the specified FlgII-28 polypeptide contains any of SEQ ID NO: 301-375; retro-inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro-inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525; or any combination of the above, to protect the plant or plant part from disease and/or enhance the innate immune response of the plant or plant part.

[0319] According to these methods, the specified polypeptide or the specified composition may contain a FlgII-28 polypeptide, while the amino acid sequence of the specified Flg22 polypeptide may contain any of SEQ ID NO: 226, 571 or 752, and/or EF-Tu polypeptides, while the sequence amino acids of these polypeptides EF-Tu contains SEQ ID NOS: 616 and 617, to protect the plant or plant part from disease and/or enhance the innate immunity of the plant or plant part. According to said methods, the amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226, 289, 290, 291, 293, 294, 295, 300, 437, 532, 534, 536, 538, 540, 571- 586 and 751-766, or any combination thereof, to protect a plant or plant part from disease, insects, or nematodes. They are polypeptides with mutant sequences showing increased activity against reactive oxygen species. For example, the amino acid sequence of said flagellin or flagellin-associated polypeptide may comprise any of SEQ ID NOs: 226, 293, 295, 300, 540, 571,574, 751, and 752, or any combination thereof.

[0320] Said disease may include Asian citrus greening, Huanglong disease (HLB), Asian soybean rust, Sclerotinia stem rot (or white mold), Pseudomonas leaf spot, or leaf cercosporiosis.

[0321] According to these methods, said polypeptide or said composition may comprise a Flg22 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide comprises any of SEQ ID NOs: 226-300 and 571-573, or any combination thereof.

[0322] According to said methods, said polypeptide or said composition may comprise a FlgII-28 polypeptide, wherein the amino acid sequence of said FlgII-28 polypeptide comprises any of SEQ ID NOs: 301-375 or 751, or any combination thereof.

[0323] According to these methods, said polypeptide or said composition may comprise a Flg22 polypeptide and a FlgII-28 polypeptide, wherein the amino acid sequence of the Flg22 polypeptide comprises any of SEQ ID NOs: 226-300 and 571-573, or any combination thereof, and the amino acid sequence of said polypeptide FlgII-28 contains any of SEQ ID NO: 301-375 or 751, or any combination thereof. Said polypeptide or said composition may further comprise a retro inverse Flg22 polypeptide, a retro inverse FlgII-28 polypeptide, or a combination thereof, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450 or any combination thereof, and the amino acid sequence of said FlgII-28 retro-inverse polypeptide comprises any of SEQ ID NOs: 451-525 or any combination thereof.

[0324] In said methods, said polypeptide or said composition may comprise an RHPP polypeptide and/or an RHPP RI polypeptide to increase yield, improve growth and/or productivity of a plant or plant part, and/or alter plant architecture.

[0325] Where said method comprises a polypeptide or composition comprising an RHPP polypeptide and/or an RHPP RI polypeptide, growth may include root growth, root length, root biomass, nodulation, total biomass, above ground biomass, or any a combination of the above. Where said polypeptide or composition contains an RHPP polypeptide, the amino acid sequence of said RHPP polypeptide may comprise SEQ ID NO: 600.

[0326] Where said method comprises a polypeptide or composition comprising an RHPP polypeptide and/or an RHPP RI polypeptide, the plant may include soybean, growth may include total root length, root biomass, nodulation, number of nodules per plant, total biomass, above-ground biomass, or any combination of the above, and productivity may include the total number of pods or the number of pods per node.

[0327] The architecture of a plant may include favorable outcomes for a plant or plant part. For example, favorable outcomes may include the possibility of increased planting density in a crop field.

[0328] According to said methods, said polypeptide or said composition may comprise a harpin-like polypeptide or an RHPP polypeptide to protect the plant or plant part from disease, insects and/or nematodes, and/or enhance the innate immune response of the plant or plant part.

[0329] According to said methods, said polypeptide or said composition may comprise a CSF polypeptide to increase the yield of a plant or plant part in an environment with a predisposition to heat and drought.

[0330] The specified polypeptide, the specified composition or the specified recombinant microorganism can be applied immediately before the formation of flowers or in the pre-flowering phase.

[0331] According to these methods, the specified polypeptide or the specified composition may contain a CSF polypeptide, RHPP, harpin or harpin-like polypeptide, or a combination thereof to improve the growth of a plant or plant part.

[0332] Growth may include root and flower apical meristems, flower organ formation, fruit development, fruit formation, number of flower organs, size of flower organs, or a combination of these.

[0333] According to said methods, said polypeptide or said composition may comprise a CSF polypeptide and a harpin or harpin-like polypeptide to improve the growth and productivity of a plant or plant part in an environment prone to both stressful and non-stressful plant growth conditions.

[0334] According to these methods, the specified polypeptide or the specified composition may contain thionine or thionine-like polypeptide.

[0335] Said thionin or thionin-like polypeptide can be fused to a phloem targeting sequence to form a fusion polypeptide, wherein the amino acid sequence of said phloem targeting sequence comprises any of SEQ ID NOs: 641-649 or any combination thereof, to deliver said fusion polypeptide to vascular tissue or vascular cells, and/or phloem, or phloem-associated tissue or phloem-associated cells in a plant or plant part.

[0336] According to these methods, protecting a plant or plant part from a disease may include prophylactic treatment (treatment), treatment (treatment), prevention and reduction of disease progression on the plant or in the plant or plant part.

[0337] Said disease may include Asian citrus greening (HLB), citrus canker, leaf blight, or disease-causing bacteria.

[0338] These disease-causing bacteria may include bacterial leaf blight, bacterial leaf streak, bacterial stem rot, bacterial leaf spot, bacterial leaf blight, bacterial blossom end rot, bacterial streak, chocolate blotch, bacterial wilt and goss rot, red spot (holcus) , purple leaf sheath blotch, seed rot, white seedling rot, Stewart's disease (bacterial wilt), corn stunting, fire blight, Pierce's disease, citrus variegated chlorosis, citrus canker, Pseudomonas syringae serovars; or a combination of the above.

[0339] According to said methods, said polypeptide or said composition may further comprise a flagellin or a flagellin-like polypeptide, wherein the amino acid sequence of said flagellin or flagellin-like polypeptide comprises any or any of SEQ ID NOs: 226-525 and 571-573 combination.

[0340] According to said methods, said polypeptide, said composition, or said recombinant microorganism can be applied exogenously to a plant, to a part of a plant, or to a plant growth medium.

[0341] According to said methods, said polypeptide, said composition, or said recombinant microorganism can be applied endogenously to a plant or plant part.

[0342] Said plant part may include plant cell, leaf, branch, stem, flower, foliage, flower organ, fruit, pollen, vegetable, tuber, rhizome, corm, bulb, pseudobulb, pod, root, root ball, rootstock, graft or seed.

[0343] According to said methods, said polypeptide, said composition, or said recombinant microorganism can be applied to a plant surface, plant foliage, or plant seed surface.

[0344] According to said methods, said polypeptide, said composition, or said recombinant microorganism can be applied to the surface of a seed, and said plant or said plant part is grown from said seed.

[0345] According to said methods, said polypeptide, said composition, or said recombinant microorganism can be used as a foliar application agent.

[0346] The plant may be a fruit plant or vegetable plant, and this method provides an increased yield of fruits or vegetables.

[0347] In methods involving the application of bioactive primer polypeptides two or more times during the growing season, the first application may occur at or before the V2 developmental stage, and subsequent applications before the flowering of the plant. For example, in the first application, seed treatments may be used, at or before VE development, at or before V1, at or before V2, at or before V3, at or before developmental stage V4, at or before developmental stage V5, at or before developmental stage V6, at or before developmental stage V7, at or before developmental stage V8, at or before developmental stage V9, at or before developmental stage V10, at or before development V11, at or before development V12, at or before development V13, at or before development V14, at or before development V15, at or before development of VT, at or before developmental stage R1, at or before developmental stage R2, at or before developmental stage R3, at or before developmental stage R4, at or before developmental stage R5, at or before developmental stage R6, at stage or before R7 developmental stage, or at or before stages of R8 development. For example, the first application may occur at or before the germination stage, at or before the seedling stage, at or before the tillering stage, at or before the booting stage, at or before the stemming stage; or at or before the heading stage. For example, if the Fickes scale is used to identify the growth stage of a crop, the first application may be at or before stage 1, at or before stage 2, at or before stage 3, at or before stage 4, at or before stage 5, at or before step 6, at or before step 7, at or before step 8, at or before step 9, at or before step 10, at or before step 10.1, at or before step 10.2 , at or before step 10.3, at or before step 10.4; or at or before step 10.5.

abiotic stress

[0348] Abiotic stress causes significant yield losses and can lead to a significant reduction in yields and potential yields. Bioactive priming polypeptides and compositions as described herein can be used as chemical priming agents to increase a plant's tolerance for one or more abiotic stresses. Accordingly, flagellin polypeptides, flagellin-associated Flg22 or FlgII-28 polypeptides derived from Bacillus species, Flg15 and Flg22 derived from E. coli and other organisms (Table 5), and RHPP polypeptides derived from Glycine max (Tables 13-15 ), are suitable for increasing the tolerance of abiotic stress by a plant, a group of plants, a field of plants and/or parts of plants. The polypeptides and compositions as described herein provide abiotic stress tolerance in a plant or part of a plant. Abiotic stress tolerance imparted to a plant or part of a plant refers to abiotic stresses that include, but are not limited to: temperature stress, radiation stress, drought stress, cold stress, salinity stress, osmotic stress due to nutrient deficiency or high metal content stress, and water stress, which is the result of water scarcity, flooding or anoxia. Chemical priming using bioactive primer polypeptides and compositions as described herein is applied to a plant or plant part, providing a versatile approach to protecting a plant or plant part from individual abiotic stresses, multiple abiotic stresses, or combined abiotic stresses.

[0349] The polypeptides and compositions as described herein are effective in protecting a plant from abiotic stress factors when used as an aboveground foliar application to a plant, plant part, plant roots, plant seeds, plant growth media, or area surrounding a plant , or the area surrounding the plant seed. For example, in the case of trees, one or more applications may be used at different points in the growth of trees, including points before, during, or after shoot formation; before, during or after fruit set; either before or after harvesting the fruit.

[0350] The methods described herein provide for the chemical priming of a plant for protection against abiotic stress or stresses such that said plant already has prepared and initiated defense mechanisms that can be activated more rapidly and increase the tolerance of abiotic stress or multiple stressors that occur. simultaneously or at different times during the growing season.

[0351] Retro-inverse forms of the Flg22 polypeptides as described herein can be applied topically as a foliar spray (as well as other applications, such as a root zone impregnation) during periods caused by excessive temperatures, water and drought stress, and be used to protect the plant from drought, heat stress, and/or other abiotic stresses that can affect stomatal openings and oscillation that normally occur with transpiration loss through the plant.

[0352] According to these methods, said polypeptide or said composition may comprise: a Flg22 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide contains any of SEQ ID NOs: 226-300 and 571-573, or any combination thereof; a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450 or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0353] According to these methods, said polypeptide or said composition may comprise: a FlgII-28 polypeptide, wherein the amino acid sequence of said FlgII-28 polypeptide contains any of SEQ ID NOs: 301-375 or any combination thereof; retro-inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro-inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525 or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0354] According to these methods, said polypeptide or said composition may comprise: a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450 or any combination thereof; retro-inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro-inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525 or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0355] According to these methods, said polypeptide or said composition may comprise an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide comprises SEQ ID NOs: 600, 603, 604, or any combination thereof; a Kunitz trypsin inhibitor (KTI) polypeptide, wherein the amino acid sequence of said KTI polypeptide comprises SEQ ID NO: 602; a retro inverse RHPP polypeptide, wherein the amino acid sequence of said RHPP RI contains SEQ ID NOs: 601, 605, 606, or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0356] Abiotic stress can include heat stress, temperature stress, radiation stress, drought stress, cold stress, salinity stress, nutrient deficiency stress, high metal stress, water stress, osmotic stress, or any combination of these.

Balancing the immune response with plant growth and development

[0357] Although immune responses can protect plants from attack by pathogens, excessive immune responses can have a negative impact on plant growth. Accordingly, optimizing plant health requires a balanced combination of enhanced immunity or disease prevention and protection in the plant with a growth-enhancing response.

[0358] Bioactive priming polypeptides suitable for enhancing the immune response as described herein can be combined with polypeptides that provide a positive effect on plant growth and productivity. These combinations of polypeptides are specifically selected based on their different mechanisms of action/regulation when applied to a plant or plant part. However, some bioactive priming polypeptides (Flg, HpGa-like, CSFα, thionins) are recognized by receptor-like proteins, after which a process begins that initiates their entry into the plant and transport through the plant, which leads to functional outcomes, while others are absorbed by the plant through active absorption ( e.g. RHPP). For example, CSF-α and Flg-associated polypeptides such as Flg22, Flg25, and FlgII-28 recognize a leucine-rich receptor kinase located on the surface of the plasma membrane and involved in a complex signaling pathway involved in pathogen-driven responses leading to the development of immunity, disease resistance or disease prevention (Kutschmar et al. “PSKα promotes root growth in Arabidopsis,” New Phytologist 181: 820-831, 2009).

[0359] Bioactive priming polypeptides as described herein, such as Flg22, HpaG-like polypeptides, and thionins, can act as elicitors and exhibit antimicrobial activity (eg, anti-pesticide; antibacterial, fungicidal, or antiviral activity). Specific combinations of polypeptides have been proposed, for example, the combination of flagellin-associated and harpin-associated bioactive priming polypeptides is suitable for preventing and protecting against pathogen-caused plant diseases, and serves a dual purpose when used together with said other polypeptides, for example, FSK-α and RHPP, which improve the growth and productivity of the plant, plant part and/or plants in the field.

[0360] Combinations of bioactive primer polypeptides as described herein can be applied to a plant exogenously as a foliar spray, furrow application at planting, seed treatment, soaking, or rinsing, or endogenously to stimulate both immune response and plant growth characteristics , which together lead to higher yields. They may also provide protection and growth benefits to different parts of the plant (eg, leaves, roots, tubers, corms, rhizomes, bulbs, pseudobulbs, flowers, pods, fruits, and growing meristems).

[0361] A combination foliar application or sequential application of CSF(with HpaG-like bioactive priming polypeptides) may be suitable for improving plant growth under standard environmental conditions (non-stressed or optimal growth) or plants subjected to abiotic stress (e.g., heat stress and stress caused by water deficiency).

[0362] Treatment with a foliar application agent with bioactive priming polypeptides, X.spp HpaG-like polypeptide and At.PSKα, works differently when applied to plants under optimal (non-stress) and stressed environmental conditions. These two classes of bioactive primer polypeptides are suitable either for sequential use or for use in combination in a foliar application and can improve plant growth in an environment with or without abiotic stress or stresses.

[0363] The X.spp. HpGa-like polypeptide conferred an advantage for the growth of corn plants in a non-stress environment where temperature, water, nutrients, and other environmental conditions were favorable for optimal plant growth. On the other hand, At.PSKα, when used as a foliar spray, provides an advantage for plant growth under environmental conditions characterized by stress caused by high temperatures and drought, or water deficiency. Accordingly, when used together in combination in a formulation as foliar application agents, they can cover both non-stress and stress environmental conditions and provide additional growth benefits for corn plants grown under a variety of environmental conditions.

[0364] Increased productivity and improved plant growth with At.PSKα has also been observed in soybean plants cultivated under environmental conditions with or without abiotic stress. Soybean plants treated with a foliar application of a formulation containing the bioactive At.PSKα priming polypeptide and cultivated under heat and drought stress conditions showed increased yields relative to control soybean plants treated with water and surfactant without the bioactive priming polypeptide.

[0365] When used together, HpaG-like polypeptides and At.PSKα from X. spp. As a foliar spray, they are suitable for providing synergistic effects in crop production under normal and stressful environmental conditions. When using At.PSKα as a spray, improved overall growth in corn is observed, while the HpaG-like polypeptide from X. spp. leads to the opposite trend. Accordingly, the combined use of these two bioactive priming polypeptides can provide plant growth under "heat stress" conditions, balanced in such a way that the changes in plant growth compared to control plants are greater than the sum of the effects of the bioactive priming polypeptides used separately.

[0366] The synergistic interaction of these two classes of bioactive primer polypeptides enhances plant growth under heat stress conditions (eg, increases growth rate along with an increase in plant biomass).

[0367] Any of the bioactive priming polypeptides as described herein can be applied to a plant one or more times, in combination or individually, to improve the growth and productivity of said plant. Multiple applications can be implemented to promote yield benefits throughout the growing season, with the application adapted to environmental conditions, e.g. if a period of hot and dry weather is expected during the growing season, additional sprays with bioactive priming polypeptides that promote growth under abiotic stress, can mitigate the negative impact on the plant.

Foliar application of phytosulfokin-alpha (FSK-α) to increase yield

[0368] A method is provided for using At.PSKα as a foliar application for actively growing soybean plants to provide a yield advantage under heat and drought stress conditions. For example, methods are provided for using a composition comprising a bioactive At.PSKα priming polypeptide as a foliar spray for soybeans in stages V1-V4 using application methods as described herein. Soybean plants treated with foliar application agents with At.PSKα can be cultivated in fields under non-stress and stress (high temperatures and water deficit) environments. At.PSKα treatment may provide growth and yield advantages in plants cultivated under various environmental conditions, including in the presence of abiotic stress factors.

[0369] Any of the bioactive RHPP priming polypeptides shown in Tables 12-14 can be applied to the plant surface as a foliar foliar application, furrow application at planting, seed treatment, or root zone impregnation.

[0370] Foliar application of RHPP results in a change in plant architecture.

[0371] A method is provided in which an RHPP polypeptide is used as a foliar application agent in plants resulting in distinct foliage architecture (corn) and enhanced root system (soybean). The increase in stem-leaf angle and root biomass with RHPP foliar treatment provides significant benefits for agricultural applications in two important crops (corn and soybeans).

Application of RHPP to change plant architecture

[0372] The use of a bioactive priming polypeptide, RHPP, as a foliar foliar application agent in stage V5-V8 maize results in a distinct foliage architecture phenotype with upright foliage and upward directed leaves. This is particularly true at higher planting densities used to maximize yields in the field. RHPP foliar application agents in maize (maize) are suitable for changing the stalk-leaf angle, thereby helping to reduce the stalk-leaf angle, resulting in a vertical leaf orientation. This phenotype may be favorable for increasing leaf area index, reducing shading avoidance syndrome in corn, and improving photosynthetic efficiency. In addition, the use of RHPP as a foliar application formulation to maximize canopy development and overall light penetration plays a key role in improving vegetative plant growth prior to initiating the seed filling stage.

[0373] Maize plants exhibit leaf curling or a change in leaf architecture towards a more vertical orientation to conserve water and improve plant tolerance to drought and heat. Verticalization of the corn leaf phenotype following application of compositions with bioactive RHPP priming polypeptide(s) is useful and provides an alternative, non-breeding way to develop leaf architecture and increase drought and heat tolerance.

[0374] The upright phenotype in corn plants is involved in lowering leaf temperatures, transpiration through the whole plant, and improving water use efficiency, and provides architectural changes to the plant's foliage that can allow higher planting densities, leading to substantial yield increases.

дюйма на одном из четырех верхних узлом на главном стебле. Затем она прогрессирует в стадию полного формирования стручка, когда происходит быстрый рост стручков и начинается развитие семян. Улучшение завязывания стручков количественно определяют по увеличению урожайности (т.е. числу стручков на узел на растении, или общему числу стручков на растение).[0375] The use of a bioactive priming polypeptide, RHPP, in soy may also provide benefits. For example, foliar application of RHPP to flowering soybeans can improve pod set. Pod set is a soybean development stage from mid-R4 to mid-R5 that directly contributes to yield. The beginning of pod tying is marked by the appearance of a pod of size

inches on one of the top four knots on the main stem. It then progresses to the full pod formation stage, where rapid pod growth occurs and seed development begins. The improvement in pod set is quantified by the increase in yield (ie, the number of pods per node per plant, or the total number of pods per plant).

RHPP to increase root biomass and yield

[0376] Soybean plants treated by foliar application of the bioactive priming polypeptide or RHPP polypeptides (SEQ ID NO: 600) can show improved and fuller pod filling compared to untreated plants, which may be the result of increased nitrogen fixation.

[0377] Root architecture, in particular a root system that quickly develops deep soil, can optimize nitrogen uptake and water uptake, which is particularly important when growing on desiccated and nitrogen-poor soils. The RHPP polypeptide(s) as described herein, when used as a foliar treatment in soybean plants, provide a root phenotype suitable for water and mineral (nitrogen) uptake, particularly in nitrogen-poor soils. Increasing the efficiency of nutrient uptake by improving root architecture is a key factor in improving plant productivity when growing soybean in a wide range of soil types.

[0378] Increased root biomass resulting from foliar application of RHPP foliar application in the early vegetative stages of soybean VE-V5 or V2-V3 results in a root system that quickly develops deep soil (deep roots) and a greater overall increase in root biomass. For example, a bioactive root hair priming polypeptide such as RHPP (SEQ ID NO: 600) can be used as a foliar treatment in V2-V3 soybean plants to provide an overall increase in root biomass. Other notable improvements along with root biomass are longer lateral roots, increased root branching, root hairs, and increased root absorptive surface area.

[0379] RHPP can be used as a foliar treatment at key developmental stages (VE-V8 or V2-V8) or in environmental conditions where rapid root growth is needed, such as dry or nutrient deficient soil types. Soil types in particular can influence the development and spread of roots. For example, if it is difficult for plant seedlings to break through clay soil, root formation and root proliferation may be affected. An increase in the root mass can not only have a favorable effect on the germination of plants, but also contribute to the acclimatization of plants. In addition, nodulation and number of nodules are important because the bacteria that inhabit the nodules draw nitrogen from the air, allowing soybean plants to convert it into the nitrogen they need to grow and produce seeds.

[0380] The RHPP polypeptides (Tables 13-15) can be used to improve nodulation and nodule production on soybean roots using any of the above treatments suitable for application directly to the soil, as an impregnation, for furrow application at planting, or in as a foliar foliar application for use on the aerial parts of plants.

[0381] An increase in the number of nodules can lead to increased nitrogen fixation by nitrogen-fixing bacteria inhabiting root nodules, such as Rhizobium leguminosarum or japonicum. Nodulation may be observed shortly after VE and may increase nitrogen fixation. Efficient soybean root nodulation results in higher yields and higher seed quality, more protein and oil per seed or acre. The first trifoliate leaves are fully developed on soybean plants at the V1-V2 developmental stage, which is estimated to be the peak period for nitrogen fixation.

[0382] The combined use of the Gm.RHPP bioactive priming polypeptide with various fertilizers can provide yield stimulation and is recommended, in particular, for use in crop management in nitrogen-depleted soils.

bacterial disease

[0383] Methods of using bioactive primer polypeptides, such as flagellin-associated polypeptides or thionin-like polypeptides as described herein, are suitable for the prevention, treatment, and control of bacterial diseases in corn, and are particularly suitable for the treatment of bacterial leaf streak in corn caused by Xanthomonas vasicola, patovar vasculorum, also known as Xanthomnas campestris, patovar vasculorum.

[0384] Research indicates that bacterial leaf streak is common and can occur over wide areas throughout the US Corn Belt (Western Indiana, Illinois, Iowa, Missouri, Eastern Nebraska, and Eastern Kansas). The disease is most prevalent where crop rotation practices involve planting corn after corn. Bacterial leaf streak can cause infection in dent corn (field) seed corn, pop corn and sweet corn. Symptoms in corn include narrow brown-yellow streaks and brown-yellow stripes between leaf veins. Lesions usually develop on lower or older leaves of the plant, and initially spread to higher or younger leaves on the plant. Yellow discoloration may also be present around the lesions.

[0385] Corn bacterial leaf streak is presumed to survive in the remains of previously infected host plants. Bacterial exudates found on the surfaces of infected leaf tissues can serve as a secondary inoculum. The bacterium is dispersed by wind, heavy rain, and possibly irrigation water. The pathogen enters maize leaves through natural openings such as stomata, which can lead to lesions in streak patterns across the leaves. Colonization of leaf tissues appears to be limited to the main veins.

[0386] Because the disease is caused by a bacterial pathogen, it is difficult to control it with current bactericide applications. Thus, most bactericides work as contact products and are not systemic; thus, they will not be absorbed or absorbed into the plant through other mechanisms. The bactericide treatment may require multiple repetitions as the bactericide can be washed away by rain or carried away by the wind, making such a treatment uneconomical or impractical for use on some corn crops.

[0387] Current disease management practices recommend the use of crop rotation practices (eg, cultivating corn, soybeans, and then corn again) and the implementation of sanitation practices such as cleaning equipment between uses.

[0388] Foliar application of Flg polypeptides (Tables 4-5) and thionine polypeptides (Table 19), or combinations of the two classes, provides an alternative approach to treating the disease. Foliar applications with these bioactive priming polypeptides, which are sprayed onto the surface of the leaves of asymptomatic or symptomatic plants, are a way to prevent, treat and control bacterial leaf streak in corn.

[0389] Alternatively, flagellin and thionin bioactive primer polypeptides, or combinations thereof, may be suitable for the prevention, treatment, and control of other bacterial diseases that infect corn (Table 21).

Table 21 Disease-causing bacteria in corn

Corn disease disease-causing bacteria Bacterial leaf damage and stem rot Pseudomonas avenae, subspecies avenae Bacterial leaf spot Xanthomonas campestris, patovar holcicola Bacterial leaf streak Xanthomonas vasicola Bacterial stem rot Enterobacter dissolvens; Erwinia dissolvens Bacterial stem and top rot Erwinia carotovora, subsp. carotovora
Erwinia chrysanthemi, patovar zeae bacterial streak Pseudomonas andropogonis chocolate spotting Pseudomonas syringae, coronafaciens patovar Bacterial wilt and goss rot (leaf mottle and wilt) Clavibacter michiganensis, subsp. nebraskensis; Corynebacterium michiganense, patovar nebraskense Red spotting (holcus) Pseudomonas syringae, patovar syringae van Hall Purple spotting of the leaf sheath Semi-parasitic bacteria Seed rot - white seedling rot Bacillus subtilis Stewart's disease (bacterial wilt) Erwinia stewartii Maize stunting ("achapparramiento", maize stunting, maize stunting of the Central Plateau or Rio Grande Valley) Spiroplasma kunkelii

Cercosporiosis leaves in soybeans

[0390] Cercospora is a fungal pathogen that causes soybean leaf blight. Cercosporiosis leaf spot, also called purple seed spot, infects both leaves and seeds of soybeans. Cercospora infection in soybean seed reduces seed appearance and quality. The causative organism of leaf cercosporiosis is Cercospora kikuchii, which overwinters on soybean residues and in seed coats. The spread of the disease occurs when spores of the fungus enter soybean plants from infected residues, weeds or other infected soybean plants. The spread of the disease and the development of symptoms are exacerbated during periods of warm and humid weather. Symptoms usually begin after flowering and appear as round soybean leaf lesions that appear as reddish-brown to purple spots that may coalesce to form lesions. Symptoms are prominent in the upper leaf layer, usually on the top three or four trifoliate leaves. As the crop matures, infected soybean plants experience worsening symptoms, and the affected leaves may drop prematurely when the pod fills up. The development of symptoms caused by Cercospora may also appear as lesions on stems, leaf petioles and pods. Infection of seeds occurs through the place of attachment to the pod. Cercospora-infected seeds show a purple-tinged discoloration that may appear as speckles or spots completely covering the seed coat.

[0391] Foliar application of flagellin or flagellin-associated polypeptides (tables 4-5) is an alternative approach to the treatment of this disease. Foliar applications with these bioactive priming polypeptides, which are sprayed on the surface of the leaves of asymptomatic or symptomatic plants, are a way to prevent, treat and control leaf blight in soybeans. Foliar application of Flg22 derived from Bacillus thuringiensis, particularly at high operating rates (e.g., 4.0 fl oz per acre), may provide a way to manage early symptom development and produce healthier and more viable soybean plants cultivated in field locations, infected with Cercospora.

[0392] Specific combinations of bioactive primer polypeptides that may be suitable for the treatment or reduction of symptoms caused by Cercospora include: flagellin or flagellin-associated polypeptide with an amino acid sequence containing SEQ ID NO: 226, 751 or 752; an RHPP polypeptide with a sequence containing SEQ ID NO: 600; or a combination of a flagellin-associated polypeptide with an amino acid sequence comprising any of SEQ ID NOs: 226, 751, and 572 and an RHPP polypeptide having an amino acid sequence comprising SEQ ID NO: 600.

[0393] For example, a suitable combination of bioactive primer polypeptides for treating or reducing symptoms caused by Cercospora in a plant or plant part is a flagellin polypeptide having an amino acid sequence comprising SEQ ID NO: 226, alone or in combination with an RHPP polypeptide having the sequence amino acids containing SEQ ID NO: 600. Additional treatments may additionally contain a fungicide in combination with these bioactive primer polypeptides.

Asian soybean rust

[0394] Asian soybean rust is a fungal disease caused by Phakopsora pachyrhizi. Its etiology and symptoms are similar to the disease caused by Cercospora, and combinations of bioactive priming polypeptides suitable for its treatment are also similar. In particular, combinations of bioactive primer polypeptides that may be suitable for treating or reducing the symptoms of Asian soybean rust include: flagellin or a flagellin-associated polypeptide having an amino acid sequence comprising SEQ ID NOs: 226, 751, or 752; an RHPP polypeptide having a sequence containing SEQ ID NO: 600; or a combination of a flagellin-associated polypeptide having an amino acid sequence comprising any of SEQ ID NOs: 226, 751, and 572 and an RHPP polypeptide having an amino acid sequence comprising SEQ ID NO: 600.

[0395] For example, a suitable combination of bioactive primer polypeptides for treating or reducing symptoms of Asian soybean rust in a plant or plant part is a flagellin polypeptide having an amino acid sequence comprising SEQ ID NO: 226, alone or in combination with an RHPP polypeptide having an amino acid sequence comprising SEQ ID NO: 600. Additional treatments may further comprise a fungicide in combination with said bioactive primer polypeptides.

Red spotting (holcus)

[0396] Red spotting is a bacterial disease caused by Pseudomanas syringae, a patovar actinidae. This document describes methods of using flagellin or flagellin-associated polypeptides to limit the growth of P. syringae and, accordingly, prevent or treat red spot in a plant or plant part. Flagellin or flagellin-associated polypeptides suitable for the treatment of P. syringae include any polypeptide having amino acid sequences comprising any of SEQ ID NOs: 226, 540, 751 and 572, or any combination thereof.

Stem rot caused by Sclerotinia (white mold)

[0397] Sclerotinia sclerotiorum is a phytopathogenic fungus that causes a disease called white mold. It is also known as soft rot, wet rot, stem rot, carrion, crown rot and sclerotinia. Diagnostic symptoms of white rot include dormant black-colored structures known as sclerotia and a white, fluffy growth of mycelium on the infected plant. The sclerotia in turn produce a fruiting body that produces spores in the pouch. Sclerotinia can infect succulent herbaceous plants, particularly fruits and vegetables, or the young tissue of woody ornamental plants. It can also infect legumes or tubers such as potatoes. White mold can infect the host at any stage of growth, including seedlings, mature plants and harvested products. It is usually found in tissues with a high water content and in close proximity to the soil. If left untreated, lesions on the soil line, which are pale to dark brown in color, become covered with a white lush mycelial coating. It infects the xylem, which leads to chlorosis, wilting, leaf fall and death. White mold can also occur on fruit in the field or during storage, and is characterized by white fungal mycelium that coats the fruit, followed by rotting of the fruit. Flagellin or flagellin-associated polypeptides suitable for the treatment of S. sclerotiorum infection include any polypeptide having an amino acid sequence comprising any of SEQ ID NOS: 226, 540, 571, 751 and 752.

leaf spot caused by Pseudomonas

[0398] Pseudomonas syringae, patovar actinidiae (PSA) is a devastating plant pathogen that causes bacterial cancer of both green (Actinidiae deliciosa) and yellow (Actinidiae chinesis) kiwifruit in all kiwifruit production areas, resulting in severe crop losses in New Zealand, China and Italy. In New Zealand alone, the cumulative loss of revenue from the most damaging biovar PSA-V is projected to approach $740 million New Zealand dollars (NZD) by 2025 (Lincoln University Agricultural Business and Economics Research Institute, “The Cost of Psa-V to the New Zealand Kiwifruit and wider community"; May 2012). PSA-V colonizes the outer and inner surfaces of kiwi fruit and can spread through xylem and phloem tissues. Symptoms of PSA-V disease in kiwi fruit include bacterial leaf spot, bacterial stem cancer, red exudates, flower rot, branch discoloration, and eventually dieback of kiwi vines. The current standard of care for PSA-V involves frequent foliar treatment of kiwifruit vines with metallic copper, which is predicted to select for the copper-resistant form of the pathogen and cause the disease to be out of control. There is an urgent need for new methods of control.

[0399] Flagellin or flagellin-associated peptides suitable for the treatment of Pseudomanas syringase infection, particularly in kiwi, include any polypeptide having an amino acid sequence comprising SEQ ID NOS: 226, 540, 752 and/or 571.

Asian citrus greening (Huanglong disease)

[0400] The methods described herein include a different approach to controlling the disease while also providing the benefits of increasing the overall productivity of the plant. This approach specifically aims to provide exogenous or endogenous use of bioactive primer polypeptides that include thionins to counter disease in plants.

[0401] The thionin and thionin-like polypeptides (Table 19) and compositions thereof are suitable for the prevention, treatment and control of Asian citrus greening, also referred to as Huanglong disease (HLB), a devastating citrus disease. HLB disease is widespread and has been found in most commercial and residential areas, in all counties that have commercial citrus orchards.

[0402] This document describes methods of using thionine polypeptides (SEQ ID NO: 650-749) to prevent the spread and treatment of HLB disease.

[0403] Asian citrus greening is carried by the Asian citrus psyllid, Diaphorina citri, or the African citrus psyllid, Trioza erytreae Del Guercio, both species characterized as sap-sucking hemipteran insects of the Psyllidae family, which have been determined to be involved in the spread of citrus greening, a disease caused by highly specialized phloem-inhabiting bacteria Candidatus Liberibacter asiaticus (Halbert, S.E. and Manjunath, K.L, “Asian citrus psyllids Sternorrhyncha: Psyllidae and greening disease of citrus: A literature review and assessment of risk in Florida,” Florida Entomologist 87: 330-353, 2004) . Asian citrus greening or Huanglong disease is considered fatal to a citrus tree after it has been infected.

[0404] Early symptoms of the disease on the leaves are yellowing of the veins and asymmetric chlorosis, called marble spot, which is the main diagnostic symptom of the disease. Infected trees are stunted, have scant foliage with visible marbled blotches. Early symptoms of yellowing may appear on a single shoot or branch, and as the disease progresses, yellowing may spread throughout the tree. Affected trees may experience branch death and fruit drop. The fruits are often few, small, deformed or asymmetrical, and not properly colored, remaining green at the end, with a yellow spot just below the stalk (stem) on the cut fruit.

[0405] Asian citrus greening can also be transmitted by grafting, when citrus rootstocks are selected and grafted onto a varietal scion.

[0406] Management of citrus greening has proven to be complex and, accordingly, current methods for controlling HLB use a multi-level, integrated approach to disease and pest management involving 1) the introduction of disease-free nurseries and rootstocks for use in grafting, 2) the use of pesticides and systemic insecticides for control of psyllid vectors, 3) the use of biological control agents such as antibiotics, 4) the use of beneficial insects such as parasitic wasps that attack psyllids, and 5) breeding for new citrus genetic material with increased resistance to citrus greening-causing bacteria ( Candidatus Liberibacter spp.). The adoption of cultural and regulatory measures to prevent the spread of the disease is also part of a comprehensive management approach. Many aspects of citrus greening management are costly both in monetary terms and in terms of losses in citrus production.

[0407] In interveinal application, the thionin polypeptide or mixture of thionin polypeptides can be delivered directly to the phloem (e.g., phloem cells, including phloem sap, phloem companion cells, and phloem sieve tube elements) where Candidatus Liberibacter can live.

[0408] These thionins can be produced using an expression system in which they can be fused to the phloem targeting sequence(s) (Table 18) and then uniquely delivered to the exact region where bacteria can inhabit the citrus plant.

[0409] These phloem-targeted thionin bioactive primer polypeptides are suitable for treating citrus plants to prevent, reduce, or eliminate the spread of citrus Asian greening or Huanglong disease (HLB) by directly targeting the bacterium Candidatus Liberibacter asiaticus

[0410] These phloem-targeted thionins can be delivered by injection into the phloem of a shrub or tree. In addition, they can be delivered by spraying, rinsing, or adding as a soak or soak to the soil or the area around the plant.

[0411] Any of the phloem targeting sequences (Table 18; SEQ ID NOs: 641-649) can be used in combination with thionin and thionin-like polypeptides (Table 19; SEQ ID NOs: 650-749).

[0412] The HLB-causing bacterium, Candidatus Liberibacter asiaticus, is difficult to isolate and culture. To test individual thionins and thionins with phloem-targeting sequences to determine if they are suitable for the treatment of HLB disease, Agrobacterium tumefaciens can be used as a model organism to test efficacy in reducing cell titers or growth of Agrobacterium prior to the use of thionin or combinations with thionin in orchard conditions.

[0415] The methods of "peptide priming" with thionins and/or thionin-like polypeptides of the present invention (Table 19) can also be used in combination with flagellin and flagellin-associated polypeptides (Tables 1-5). Combinations of thionin and flagellin-associated bioactive priming polypeptides can be used for prophylactic pretreatment of a citrus plant by applying said bioactive priming polypeptide or a composition containing said polypeptide prior to the onset or manifestation of any infection-related symptoms in citrus shrubs or trees. Said pre-treatment increases resistance to the citrus greening pathogen (Candidatus Liberibacter spp.).

[0414] Thionins presented in combination with flagellin-associated bioactive priming polypeptides provide a more comprehensive approach to disease prevention and management. Thionin and flagellin-associated bioactive priming polypeptides employ two distinct mechanisms of action to prevent disease and spread disease.

[0415] Thionin-flagellin combinations of bioactive primer polypeptides can also be used in conjunction with any other integrated management approach for disease control envisaged in HLB, including, but not limited to, (1) the use of disease-free seedlings and/or root shoots for grafting, (2) application of pesticides and/or systemic insecticides to control disease-causing psyllids, (3) application of biological control agents, such as antibiotic injections, or parasitic insects that control psyllids, (4) breeding new variants of citrus genetic material with increased resistance to bacteria causing Asian greening of citrus fruits, (5) control of parasitic plants (eg, dodder) that can spread the disease; or (6) any combination of the above.

[0416] A synthetic variant of a phloem-targeting polypeptide (SEQ ID NO: 641) is particularly suitable for use in targeting antimicrobial polypeptides to phloem sieve tubes and companion cells, and may be suitable for the treatment of various bacterial plant diseases such as bacterial striation leaves, Asian citrus greening or Huanglong disease, and citrus cancer.

[0417] In addition, flagellin or flagellin-associated polypeptides are suitable for the treatment of Asian citrus greening, particularly when used in combination with a bactericide. For example, flagellin or flagellin-associated polypeptides with amino acid sequences comprising any of SEQ ID NOs: 226, 571, and 752 can be used. Preferably, said bacteriocide contains oxytetracycline.

Cancer of citrus

[0418] "Peptide priming" methods have been developed for use with bioactive priming thionin and flagellin-associated polypeptides as described in Table 19 (thionins) and Tables 1-5 (flagellin and flagellin-associated polypeptides) to prophylactically treat citrus plants before any - either visible symptoms of citrus cancer, or as a treatment after the onset of visible symptoms of the disease.

[0419] Citrus canker is found mainly in tropical and subtropical climates; its occurrence has been described in more than 30 countries, including reports of the spread of infection in Asia, Africa, the islands of the Pacific and Indian Oceans, South America, Australia, Argentina, Uruguay, Paraguay, Brazil and the United States. Citrus canker is a disease caused by the bacterium Xanthomonas axonopodis, patovar citri or, patovar aurantifolii (also called Xanthomonas citri, subsp. citri), which infects foliage, fruits, and young stems. Symptoms of citrus canker infection on leaves and fruit of citrus shrubs/trees can result in leaf spot, leaf damage, leaf drop, tip dieback, fruit distortion, fruit peel spots, premature fruit drop, and canker sores on leaves and fruits. Diagnostic symptoms of citrus canker include a characteristic yellow halo surrounding leaf lesions and a watery streak that develops around necrotic tissue on citrus leaves. The citrus canker pathogen can be spread through the transport of infected fruits, plants and equipment. Wind and rain can also contribute to spread. Overhead irrigation systems can also help move the cancer-causing citrus pathogen. Infected stems can carry citrus canker bacteria (Xanthomonas axonopodis, patovar citri) in stem lesions for transmission to other citrus plants. Insects such as the Asian miner fly (Phyllocnistis citrella) also spread the disease.

[0420] In general, citrus plants susceptible to citrus canker disease include orange, sweet orange, grapefruit, pummelo, tangerine tangerine, lemon, lime, Swingle sour lime, Palestinian sweet lime, tangerine, tangelo, sour orange, wild lemon, citron, calamondin, trifoliate poncirus, and kumquat. Millions of dollars are spent annually worldwide on prevention, sanitation, containment, quarantine, and eradication programs to control citrus cancer (Gottwald T.R. “Citrus Canker,” The American Phytopathological Society, The Plant Health Instructor 2000/ updated 2005). Treatment for this disease included the use of antibiotics or disinfectants, the use of copper-based germicidal sprays, and the use of pesticides to control the Asiatic leaf miner.

[0421] A combination with bioactive primer polypeptides containing thionin and flagellin-associated polypeptides can be used in a citrus plant or part of a citrus plant (e.g., rootstock, scion, leaves, roots, stems, fruits, and foliage) using methods that can include: spraying, inoculation, squirting, soaking, soaking, rinsing, dressing and/or application to the surrounding soil, for example as a furrow application at planting.

[0422] Methods are provided for using bioactive primer polypeptides containing thionin and/or flagellin-associated polypeptides to pretreat citrus plants or parts of citrus plants (e.g., rootstock, scion, leaves, roots, stems, fruits, and foliage) before any or visible symptoms. They are also suitable for providing increased resistance to the citrus cancer pathogen, resulting in a reduction in the symptoms of the disease.

[0423] In addition, methods of using bioactive primer polypeptides, such as flagellin and flagellin-associated polypeptides, are suitable for the treatment of citrus plants or parts of citrus plants (for example, rootstock, scion, leaves, roots, stems, fruits and foliage) for early symptoms citrus cancer or after the symptoms of the disease become apparent.

[0424] The use of Flg polypeptides in the treatment of citrus plants to prevent, reduce or eliminate the spread of citrus cancer can be implemented by injection into the phloem of a shrub or tree, spraying, washing, adding as a soak or impregnation to the soil or soil area around the plant, or by incorporating into the furrow at planting.

[0425] The thionin bioactive primer polypeptides as described herein (Table 17) can be used alone or in combination with any of the flagellin-associated Flg polypeptides (Tables 1-5) as a foliar treatment or spray or spray and are suitable to prevent infestation of citrus plants by insects such as the Asian miner fly (Phyllocnistis citrella), which have been identified as carriers of bacteria (Xanthomonas axonopodis, patovar citri) that cause citrus cancer.

citrus plants

[0426] Any of the methods described herein for providing improved plant health, disease tolerance, or use to treat disease, to treat or prevent Asian citrus greening (HLB) or citrus canker, are suitable for use in any citrus plant and shrub/tree .

[0427] The thionin or flagellin-associated polypeptides or compositions comprising the thionin or flagellin-associated polypeptides as described herein can be used for any citrus shrub and/or tree, and for any agronomically important citrus hybrid or non-hybrid citrus plant, and are suitable for prophylactically treating said citrus plant to prevent the onset of an infection or to provide treatment after an infection has occurred.

[0428] Suitable citrus plant species for the methods described herein include, but are not limited to: sweet orange (Citrus sinensis, Citrus maxima × Citrus reticulata), bergamot orange (Citrus bergamia, Citrus limetta × Citrus aurantium), bitter orange, orange or Seville orange (Citrus aurantium, Citrus maxima × Citrus reticulata), king orange (Citrus sinensis), orangelo or chironha (Citrus paradisi × Citrus sinensis), mandarin orange (Citrus reticulate), three-leaf lemon (Citrus trifoliata), tachibana orange (Citrus tachibana), clementine (Citrus clementina), quishu mikan (Citrus kinokuni), lemon (Citrus limon, Citrus maxima × Citrus medica), Indian wild orange (Citrus indica), Imperial lemon (Citrus limon, Citrus medica × Citrus paradisi), lime (Citrus latifoli, Citrus aurantifolia), Meyer lemon (Citrus meyeri); Citrus ×meyeri hybrids with Citrus maxima, Citrus medica, Citrus paradisi and/or Citrus sinensis), wild lemon (Citrus jambhiri), volkameriana lemon (Citrus volkameriana), Ponderosa lemon (Citrus limon × Citrus medica), kaffir lime ( Citrus hystrix or Mauritius papeda), sweet lemon, sweet lime or musambi (Citrus limetta), Persian lime or Tahiti lime (Citrus latifolia), Palestinian sweet lime (Citrus limettioides), talamisan (Citrus longispina), Australian finger lime (Citrus australasica), Australian round lime (Citrus australis), Australian desert or wild lime (Citrus glauca), Mount White lime (Citrus garrawayae), cockatoo lime or 'Humpty-Doo' (Citrus gracilis), Inodoru (Citrus inodora), New Guinea Wild Lemon (Citrus warburgiana), Papuan (Citrus wintersii), Limandarin (Citrus limonia; (hybrids with Citrus reticulata × Citrus maxima × Citrus medica), gainimu ( Citrus pennivesiculata), Australian blood lime (Citrus australasica × Citrus limonia) Chinese lime (Triphasia brassii, Triphasia grandifolia, Triphasia trifolia), grapefruit (Citrus paradisi; Citrus maxima × Citrus × sinensis), tangerine (Citrus tangerina), tangelo (Citrus tangelo) ; Citrus reticulata × Citrus maxima or Citrus paradisi), minneola tangelo (Citrus reticulata × Citrus paradisi), orangelo (Citrus paradisi × Citrus sinensis), tangor (Citrus nobilis; Citrus reticulata × Citrus sinensis), pomelo or pomelo (Citrus maxima), citron (Citrus medica), mountain citron (Citrus halimii), kumquat (Citrus japonica or Fortunella species), kumquat hybrids (calamondin, Fortunella japonica; citranquat, Citrus icchangensis; limequat, Citrofortunella floridana; orangequat, hybrid between Satsuma mandarin×Citrus japonica or Fortunella species; prosaimquat, Fortunella hirdsiie; sanquat, a hybrid between Citrus meyeri and Citrus japonica or Fortunella species; Yuzuquat, a hybrid between Citrus ichangensis and Fortunella margarita), papeda (Citrus halimii, Citrus indica, Citrus macroptera, Citrus micrantha), Ichan papeda (Citrus ichangensis), Sulawesi papeda (Citrus celebica), Khazi papeda (Citrus latipes), Melanesian papeda ( Citrus macroptera), Ichansky lemon (Citrus ichangensis × Citrus maxima), yuzu (Citrus ichangensis × Citrus reticulata), green orange (Citrus reticulata × Citrus maxima), cabosu (Citrus sphaerocarpa), sudachi (Citrus sudachi), alemo (Citrus macrophylla) , mikranthu (Citrus micrantha), small-fruited micrantha (Citrus micrantha), kalpi (Citrus webberi), mikan (Citrus unshiu), hyuganatsu (Citrus tamurana), mangshanyogan (Citrus mangshanensis), kaulu (Citrus crenatifolia), amanatsu or natsumikam (Citrus natsudaidai ), kinnow (Citrus nobilis × Citrus deliciosa), kiyomi (Citrus sinensis × Citrus unshiu), oroblanco (Citrus maxima × Citrus paradisi), agley (Citrus reticulata × Citrus maxima and/or Citrus × paradisi), calamondin (Citrus re ticulata × Citrus japonica), chinotto (Citrus myrtifolia, Citrus aurantium or Citrus pumila), cleopatra tangerine (Citrus reshni), daidai (Citrus aurantium or Citrus daidai), laraja (Citrus aurantium), satsuma tangerine (Citrus unshiu), tangerine 'naartye' (Citrus reticulata × Citrus nobilis), rangpur (Citrus limonia; or hybrid with Citrus sinensis × Citrus maxima × Citrus reticulata), nasnaran (Citrus amblycarpa), yecan, anadomican (Citrus iyo), wild lime (Citrus odichukuthi), golden orange (Citrus flaviculpus), pompi (Citrus monstruosa), Taiwanese tangerine ( Citrus depressa), Shonan Gold (Citrus flaviculpus or Citrus unshiu), Sunki (Citrus sunki), Mangshan Mandarin (Citrus mangshanensis, Citrus nobilis), Clymenia (Clymenia platypoda, Clymenia polyandra), Jabara (Citrus jabara), Mandora (Mandora cyprus), melogold (Citrus grandis × Citrus paradisii/Citrus maxima/Citrus grandis), Icha lemon (Citrus ichangensis × Citrus maxima), honey tangerine (Citrus reticulata) and shikvasa tangerine (Citrus depressa).

[0429] The thionin and/or flagellin-associated primer polypeptides can be used in any citrus plant, shrub/tree used for medical or cosmetic/health/cosmetic purposes, such as bergamot orange (Citrus bergamia), sour or bitter orange (Citrus aurantium), sweet orange (Citrus macrophylla), key lime (Citrus aurantiifolia), grapefruit (Citrus paradisi), citron (Citrus medica), tangerine (Citrus reticulate), lemon (Citrus limon, or hybrids with Citrus medica × Citrus maxima, Citrus limonia, Citrus medica × Citrus maxima × Citrus medica), sweet lime (Citrus limetta), kaffir lime (Citrus hystrix or Mauritius papeda), lemon hybrid or lumia (Citrus medica × Citrus limon), (Citrus medica × Citrus maxima × Citrus medica), Omani lime (Citrus aurantiifolia, Citrus medica × Citrus micrantha), sheddock (Citrus grandis), cockatoo or Humpty-Doo lime (Citrus gracilis), pomelo (Citrus retkulata), tangor (Citrus nobilis); and sour lime or nimbuca (Citrus acida).

[0430] Examples of important citrus fruit hybrids: sweet orange (Citrus sinensis), bitter orange (Citrus aurantium), grapefruit (Citrus paradisi), lemon (Citrus limon), Persian lime (Citrus latifolia), kee lime (Citrus aurantiifolia) ), tangerine (Citrus tangerine) and rangpur (Citrus limonia).

[0431] In addition, any of the bioactive primer polypeptides, any of the compositions, and any of the methods as described herein can be applied to any citrus plant, shrub/tree used as rootstock and/or scion genetic material. These methods are particularly suitable for rootstocks often used for grafting citrus fruits to enhance the merits of a varietal graft, which may include tolerance to drought, frost, disease or soil organisms (eg nematodes). Such citrus plants that provide suitable rootstocks include: sour or bitter orange (Citrus aurantium), sweet orange (Citrus macrophylla), three-leafed lemon (Poncirus trifoliata), wild lemon (Citrus jambhiri), volkameriana lemon (Citrus volkameriana), alemo ( Citrus macrophylla), Cleopatra mandarin orange (Citrus reshini), citrumelo (hybrids with × Citroncirus species), grapefruit (Citrus paradisi), rangpur lime (Citrus limonia), Palestinian sweet lime (Citrus limettioides) and Troyer citrange (Citrus sinensis × Poncirus trifoliata, or Citrus sinensis × Citrus trifoliata) and citrange (Citrus sinensis × Poncirus trifoliata or C. sinensis × C. trifoliata).

Use of Retro-Inverse Bioactive Flg Priming Polypeptides to Treat and Reduce Greening of Citrus Fruits

[0432] Combinations of flagellin-associated polypeptides paired with their retro-inverse equivalents can be used to treat and reduce the greening effect in citrus fruits caused by Asian citrus greening or Huanglong disease.

[0433] An early symptom of HLB in citrus fruits is yellowing of leaves on a single branch or in one sector of the tree's canopy. Leaves yellowing as a result of HLB show an asymmetrical pattern with uneven yellowing or marbling of the leaf, with green spots on one side of the leaf and yellow on the other. As the HLB disease progresses, fruit size decreases and the juice becomes bitter. The fruit may remain partially green and tends to drop prematurely.

[0434] Treatment combinations with Flg polypeptides and their retro-inverse (RI) forms can be used to minimize the greening effect of citrus fruits. Such treatment combinations can be used on HLB-infected trees. The retro inverse forms will compete with natural forms of the Flg polypeptides for binding to the FLS-associated receptor(s) on the plant surface and thus inhibit/delay the formation of greening symptoms associated with HLB disease. Combinations of natural Flg22 and Flg22 RI help to fine-tune the immune response to reduce and even eliminate the disease-causing bacteria, Candidatus Liberibacter asiaticus, while preventing the development of acute symptoms such as leaf yellowing and greening of citrus fruit.

EXAMPLES

[0435] The following non-limiting examples are intended to further illustrate the present invention.

Example 1: Application of Bt.4Q7Flg22 and Retro-Inverse Bt.4Q7Flg22, Ec.Flg22 and Ec.RI Flg22 in Maize

[0436] Effect of bioactive Bt.4Q7Flg22 (SEQ ID NO: 226) and retro-inverse Bt.4Q7Flg22 (SEQ ID NO: 376) priming polypeptides, as well as Ec.Flg22 (SEQ ID NO: 526) and Ec.RI Flg22 ( SEQ ID 527) for corn yield (BECK'S 5828 YH, 6175YE) were determined at 10 separate locations in the US Midwest (FIG. 2 and FIG. 3).

[0437] The seed beds in the field at each location were formed using standard or anti-erosion corn planting methods. Fertilizer was applied according to standard farming guidelines, in the same manner for all locations in the US Midwest. Herbicides were used to control weeds with additional loosening of the soil if necessary. All locations were planted in four-row plots 17.5 feet (5.3 meters) long. Corn seeds were planted 1.5-2 inches (3.8-5.1 cm) deep to allow for normal root development, at a density of 28,000-36,000 plants per acre in rows 30 inches (76.2 cm) wide and seed spacing to accommodate approximately 1.6-1.8 seeds per foot. Each hybrid was grown in at least three separate plots (replicates) at each location to compensate for variability in field conditions.

[0438] The natural bioactive Bt.4Q7Flg22 priming polypeptide (SEQ ID NO: 226) and the corresponding retro inverse polypeptide (SEQ ID NO: 376) were chemically synthesized using solid phase peptide synthesis and formulated for an operating flow rate of 0.33 fl oz per acre (24.1 ml/hectare, ha). The final concentration in the spray tank was 25 nM after dilution in vehicle at 10 gallons of water per acre (37.85 L/ha). Natural bioactive Bt.4Q7Flg22 priming polypeptides were used during the first and second years of field trials to measure effects over a multi-year growing season. Retro inverse polypeptides were used during the first year of field testing for comparison with natural Bt.4Q7Flg22. Bioactive primer polypeptides were used as foliar sprays at an operating rate of 0.33 fl oz per acre (24.1 ml/ha) in developmental stages V5-V8. Each polypeptide was applied together with a nonionic surfactant in an amount of 0.5%. The effect of bioactive priming polypeptides was measured as absolute yield changes in bushels per acre. In addition, the probability of success was calculated: the percentage of locations tested where a treatment yielded a yield advantage over other treatments (in this case, compared to untreated control plants).

[0439] Panel A of FIG. Figure 2 shows that in a first year field trial, a foliar spray with Bt.4Q7Flg22 (SEQ ID NO: 226) experienced an average yield increase of 11.60 bushels per acre (728.1 kg/ha) with a success rate of 90 % at all 10 locations compared to untreated control corn plants. In panel B of Fig. 2 shows that the use of a foliar spray with a retro-inverse bioactive Bt.4Q7Flg22 priming polypeptide (SEQ ID NO: 376) resulted in an average yield increase of +11.90 bushels per acre (746.9 kg/ha) with a success rate of 70 % at all 10 locations in the US Midwest compared to untreated control corn plants. In both figures, locations (1-12) are labeled on the x-axis, and absolute yield change in bushels per acre is labeled on the y-axis and is indicated above or below the bars on the graph for each location. The Ec.Flg22 polypeptide when applied to corn produced an 8.2 bushel/acre (514.7 kg/ha) advantage with an 80% success rate in all 10 plots. The retro-inverted Ec.RI Flg22 did not provide the same results, producing 1.9 bu/acre in all 10 plots with a 50% success rate.

[0440] A second year field trial was conducted over large areas in the field at 10-11 locations in the US Midwest (Illinois, Indiana, Iowa) and used a foliar spray with a bioactive Bt.4Q7Flg22 priming polypeptide (SEQ ID NO: 226) in maize plants at the V8 stage (Dekalb 5064). A foliar spray with Bt.4Q7Flg22 was applied at an operating rate of 0.33 fl oz per acre. As shown in FIG. 3, foliar application using the bioactive Bt.4Q7Flg22 priming polypeptide resulted in an average yield increase of +4.8 bushels per acre relative to control at all 11 locations with an 83% success rate. Locations 1-6 are plotted on the x-axis, and absolute yield change in bushels per acre is plotted on the y-axis, above or below the bars on the graph for each location.

[0441] A first year field trial with a foliar treatment using the bioactive Bt.4Q7Flg22 priming polypeptide (SEQ ID NO: 226) in a corn hybrid (Beck's 5828 YH) shown in FIG. 2 (panel A) resulted in a yield increase of more than +11 bushels per acre (690.4 kg/ha) relative to untreated control plants. A second year field trial with V8 stage corn plants (Dekalb 5064) shown in FIG. 3 resulted in an increase of nearly +5 bushels per acre (313.8 kg/ha) over the yield of untreated control plants. The combined average of the two corn hybrids yielded a 2-year average yield increase of +8.0 bushels per acre (50.2 kg/ha) at different locations with an 86% success rate reflecting a multi-year growing season.

[0442] A third study was performed testing the bioactive Bt.4Q7 Flg22 priming polypeptide as an agent for use in stage V5-V8 maize at 3 flow rates applied along with a nonionic surfactant. The resulting operating costs were 0.33 fl oz/acre, 4 fl oz/acre, 8 fl oz/acre (24.1 ml/ha, 292.3 ml/ha, 584.6 ml/ha), giving approximate final concentrations of 25 nM, 300 nM, 600 nM, respectively. Each study was conducted on 10-11 plots. The final results of the study in stages V5-V8 at a rate of 0.33 fl oz per acre (24.1 ml/ha) amounted to an advantage of 5.75 bushels per acre, or 360.9 kg/ha, at a rate of 4 fl oz per acre - 3.77 bushels / acre, or 236.6 kg / ha, and at a rate of 8 fl oz per acre - 5.05 bushels per acre, or 317 kg / ha.

Example 2 Application of Bt.4Q7Flg22 on V8 Stage Maize with Fungicide

[0443] A foliar treatment of Bt.4Q7Flg22, with or without the addition of a commercially available fungicide, STRATEGO YLD, was performed to determine if there are synergistic effects when combining a bioactive Bt.4Q7Flg22 priming polypeptide with a fungicide. The use of a foliar spray with Bt.4Q7Flg22 (SEQ ID NO: 226) alone or in combination with STRATEGO YLD was evaluated in maize plants (hybrid Dekalb 5064) at the V8 developmental stage.

[0444] Tests in repetitions were carried out in 6-8 locations in the US Midwest (Iowa, Illinois, Indiana). Corn plants were cultivated as described in Example 1. The sites were maintained in accordance with the cultivation practices of individual growers; each site was presented in 3-4 replicas. When applying the fungicide STRATEGO YLD (a combination of prothioconazole and trifloxystrobin), the recommended rate (4.0 fl oz/acre, or 292.3 ml/ha)) in each location was used. Foliar treatment applications included the following treatments: (a) untreated control, (b) STRATEGO YLD fungicide alone and Bt.4Q7Flg22 (SEQ ID NO: 226) free peptide form with (c) and without (d) added fungicide. Bt.4Q7Flg22 was applied at a working rate of 0.33 or 4.0 fl oz/acre or (24.1 or 292.3 ml/ha).

[0445] Corn yields in bushels per acre were recorded at all locations as the average yield for replicate trials at each location. Yield change in bushels per acre for corn plants treated with foliar application with STRATEGOYLD fungicide was normalized to the average yield for control corn plants at 6 locations (Table 22).

[0446] Foliar treatments with Bt.4Q7Flg22 at 0.33 fl oz per acre (24.1 ml/ha) provided yield advantages over untreated corn controls with an increase of +4.84 bushels per acre (303.8 kg/ha) which was observed in all 6 locations. Foliar treatment with STRATEGO YLD fungicide alone also provided a yield advantage in corn with an increase of +4.88 bushels per acre (306.3 kg/ha) over control plants. Application of the free peptide, Bt.4Q7Flg22, at 0.33 fl oz per acre (24.1 ml/ha) in combination with STRATEGO YLD fungicide at 4.0 fl oz per acre showed a synergistic effect, resulting in an average increase of +10 .72 bushels per acre (672.9 kg/ha) relative to untreated control plants. Accordingly, the combination of treatment with Bt.4Q7 Flg22 polypeptide and fungicide resulted in a synergistic effect at an operating rate of 0.33 fl oz per acre (24.1 ml/ha) for polypeptides and an operating rate of 4.0 fl oz per acre /ha) fungicide.

Table 22: Treatment of corn foliage with bioactive Bt.4Q7Flg22 priming polypeptide with fungicide to increase corn yield

Processing - corn Operating Consumption in Fluid Ounces per Acre Average total yield in bushels per acre
(6 locations) Average increase in bushels per acre compared to control Control - 187.37 - Bt.4Q7Flg22 0.33 192.21 +4.84 STRATEGO YLD 4.0 193.80 +4.88 Bt.4Q7Flg22+
STRATEGO YLD 0.33
4.0 207.86 +10.72

[0447] A second study to consider the combination of Ec.Flg22 with STRATEGO was also performed at 8 sites in the form of tests in repetitions, in the same way as described above. Ec.Flg22 at 4 fl oz per acre (292.3 ml/ha) added 1.3 (busels per acre) (81.6 kg/ha) to the STRATEGO YLD result with a 63% success rate in 8 plots. This result demonstrates that both Flg22 polypeptides were able to increase the benefit provided by the commercial fungicide STRATEGO YLD.

Example 3: Application of Bt.4Q7 Flg22, retro-inverse Bt.4Q7Flg22, Ec.Flg22, retro-inverse Ec.Flg22 or RHPP in soybean at stage R2 - increased yield.

[0448] Foliar applications with bioactive Bt.4Q7 Flg22 priming polypeptide (SEQ ID NO: 226; FIG. 4, panel A), retro-inverse (RI) Bt.4Q7Flg22 (SEQ ID NO: 376; FIG. 4, panel B) from Bacillus thuringiensis strain 4Q7 and a root hair stimulator polypeptide (RHPP, SEQ ID NO: 600) derived from Glycine max were applied individually to soybean plants (commercial hybrid Beck's 294 NR) at R2 developmental stage at operating rate 0.33 fl oz/acre, or 24.1 ml/ha (Flg22 polypeptides); or 4.0 fl oz/acre, or 292.3 ml/ha (RHPP). The cultivation methods involved in example 1 were used for soybean seeds. Soybean seeds (commercial hybrid Beck's 294 NR) were planted at a depth of 1.5-2 inches (3.8-5.1 cm) to ensure normal root development. Soybean seeds were planted at an approximate density of 150,000 plants per acre on average, with rows 30 inches (76.2 cm) wide and seed spacing to accommodate approximately 7-8 seeds per foot (0.3 m).

[0449] The final yield in bushels per acre is recorded for soybeans cultivated at 11 separate locations in the US Midwest harvested in October (FIG. 4). Soybean yield (in bushels per acre) is also recorded as the average for all locations change in yield (in bushels per acre) normalized to control soybean plants. Soybean yields after foliar applications of Bt.4Q7Flg22 (SEQ ID NO: 226) and Bt.4Q7Flg22 RI (SEQ ID NO: 376) were compared with that of untreated soybean plants and plotted in FIG. 4. Locations 1-11 are plotted on the x-axis. The absolute change in yield (in bushels per acre) from untreated soybean controls is plotted on the y-axis and is indicated above or below the bars on the graph for each location. Record the average yield in all 11 locations, it is indicated by the black column. Yields of soybeans foliarly treated with Bt4Q7Flg22 and RI Bt.4Q7Flg22 showed similar trends at 11 different locations. Spraying with RI Bt.4Q7Flg22 in soybeans resulted in an average yield increase of 0.90 bushels per acre (60.5 kg/ha) for 2 soybean hybrids at all 11 locations compared to untreated soybean controls. Yield results using natural (all-L) Bt.4Q7Flg22 in soybeans were null (-0.1 bushels per acre, or -6.7 kg/ha)) when compared at all locations. Yield data reported for all 11 individual locations in the US Midwest give a success rate of 64% for both spray treatments with RI Bt.4Q7Flg22 and Bt.4Q7Flg22 compared to control or untreated soybean plants. The addition of 4 fl oz per acre (292.3 ml/ha) of RHPP polypeptide in the same study increased yield by 1.2 bushels per acre (80.7 kg/ha) compared to control.

[0450] A second study was performed to test Ec.Flg22 and Ec.RI Flg22 polypeptides as R2 stage foliar treatments in soybeans using a carrier, water with a nonionic surfactant (NIS), 10 gallons per acre (93, 5 l/ha). For each tank treatment, a concentration of 100 nM was obtained. Application of Ec.Flg22 results in an increase of 0.9 bushels per acre (60.5 kg/ha) with an 82% success rate in 11 plots, and Ec.RI Flg22 results in an increase of 0.6 bushels per acre (40.3 kg/ha) ha) with 80% success rate in 10 sites. The RHPP polypeptide was also included as a seed treatment providing 1.2 bushels/acre (80.7 kg/ha) in 11 plots with a 73% success rate.

[0451] A third study on the same 11 plots was performed with the addition of foliar fertilizer alone or with RHPP at a rate of 8 fl oz/acre (584.6 ml/ha). The addition of RHPP to the foliar fertilizer provided a 1 bushel/acre (67.2 kg/ha) advantage at all 11 plots.

Example 4: Use of Flg22 polypeptides for foliar spraying in soybean.

[0452] Foliar treatments with Bt.4Q7Flg22, Ec.Flg22, and RHPP at 4.0 and 8.0 fl oz per acre (292.3 and 584.6 ml/ha) were tested in R2 on soybeans in 11 plots in 10 gallons of water per acre (93.5 L/ha) with 0.5% non-ionic surfactant (NIS). At the higher dose, 8 fl oz/ac (584.6 ml/ha), the Ec.Flg22 polypeptide gave a benefit of 0.74 bushels per acre (49.8 kg/ha) and Bt.4Q7 Flg22 gave a benefit of 0 .88 bushels per acre (59.2 kg/ha). A lower flow rate of 4 fl oz/acre (292.3 ml/ha) for RHPP resulted in a yield advantage of 0.31 bushels/acre (20.9 kg/ha).

Example 5 Use of Escherichia coli Flagellin Polypeptides to Increase Yield - Maize

[0453] The effect of Escherichia coli-derived flagellin polypeptides on corn yield was then tested. First, maize plants (Beck's 5828 YH) at developmental stages V5-V8 were sprayed with formulations containing the bioactive priming polypeptide Ec.Flg22 (SEQ ID NO: 526) and retro-inverse RI Ec.Flg22 (SEQ ID NO: 527) from Escherichia coli, at an operating rate of 0.33 fl. oz. per acre (24.1 ml/ha). The final yield in bushels per acre was determined for corn grown in 12 separate locations and harvested in October.

[0454] FIG. 5 shows the yield at these 12 locations normalized to untreated control plants and presented as an increase or decrease in bushels per acre compared to the control. Yield data reported for 12 individual locations in Illinois corresponded to a 50% success rate. Corn plants treated with a foliar spray with the bioactive Ec.Flg22 priming polypeptide (Figure 5, panel A) experienced a mean yield increase of +8.2 bushels per acre (514.7 kg/ha) relative to untreated plants in all 12 locations. Maize plants treated with a foliar spray with a retro-inverse bioactive priming RI Ec.Flg22 polypeptide (Figure 5, panel B) experienced a mean yield increase of +1.9 bushels per acre (119.3 kg/ha) in all 12 locations compared to untreated control corn plants. Accordingly, the use of foliar sprays containing bioactive primer polypeptides Ec.Flg22 (SEQ ID NO: 526) provided a favorable growth response and yield advantage in maize plants when applied at the V5-V8 developmental stage.

Example 6 Foliar Application of Escherichia coli Flagellin Polypeptides in V2-V3 Stage Maize to Increase Plant Height

[0455] Foliar application of Ec.Flg22 (SEQ ID NO: 526) and retro-inverse RI Ec.Flg22 (SEQ ID NO: 527) was performed in corn (Beck's 297NR). Plants were cultivated in a growing room with controlled environmental conditions. Seeds were planted directly into 39.7 ^cc containers containing Timberline plant soil at a depth of 2.54 cm, 2 seeds per container. After planting, 50 ml room temperature water was added to each container to ensure germination. The containers were placed in a grow room with artificial lighting, with an input of approximately 300 µmol m ^-2 s ^-1 (light photons) on a daily light/dark cycle of 13/11 and with temperatures ranging from 21°C during the day to 15°C at night. For plants used the same modes of watering and fertilization.

[0456] Foliar treatments containing both natural and retro-inverse forms of Ec.Flg22 were applied to 3-week-old V2 to V3 soybean plants at an operating rate of 0.33 fl oz per acre (24.1 ml/ha). Plant height (cm) was measured immediately prior to foliar delivery 3 weeks later and then again 2 weeks later when the plants were 5 weeks old. Tests in 2 replications were performed using 18 plants per test.

[0457] As described in Table 23, foliar application of the Ec.Flg22 polypeptide in V2-V3 soybeans increased plant height compared to control plants (treatment with water only) (Table 23). Foliar application using bioactive priming polypeptides Ec.Flg22 (SEQ ID NO: 526) and retro-inverse Ec.Flg22 (SEQ ID NO: 527) resulted in a +13% and +16% increase in plant height when normalized to control untreated soybean plants (normalization by 100%).

Table 23. Foliar Application of Flagellin Polypeptide Increases Plant Height in Soybean

Foliage Treatment Height (cm) after 3 weeks Height (cm) after 5 weeks Height in percent relative to control Soya Ec.Flg22 (1 µM) 40.17 (5.83) 64.79 (8.40) 113.2% Retro-inverse Ec.Flg22 (1 µM) 36.57 (6.00) 66.46 (5.77) 116.1%

Example 7 Application of Flg22 and Retro-Inverse Flg22 in Maize - Plant Height

[0458] Corn plants (hybrid Beck's 5828 YH) were grown in a controlled growing room as described in Example 6. Plants were measured three weeks after emergence and then treated with natural (L) and retro-inverse ( D) Flg22 polypeptide forms from Bacillus thuringiensis (Bt.4Q7Flg22, SEQ ID NOs: 226 and 376) and Escherichia coli (Ec.Flg22, SEQ ID NOs: 526-527). Bioactive primer polypeptides were used as free polypeptides at a concentration of 1 μM. Control plants were treated separately with water. After an additional 2 weeks of growth, plant height was measured (after 5 weeks).

[0459] The change in plant height (Δ height, cm) between time points after 2-week and 5-week intervals was measured and normalized to the growth of water-treated control plants. Trials were performed in 3 replicates with 9 plants per trial, for a total of 27 measurements per treatment (Table 24). When measured at the time point 3 weeks later, there was no difference in measured plant height between EcFlg22, Bt.4Q7Flg22 treated or water treated control plants. The maximum change in plant height after 3-5 weeks was recorded in maize plants that were treated with foliar application with Ec.Flg22 ((=17.60 cm). These plants also achieved a height increase of +8.3% compared to control plants when measured at point 5 weeks Two retro-inverse polypeptides (RI Ec.Flg22 and RI Bt.4Q7Flg2) and natural Bt.4Q7Flg22 similarly increased plant height compared to the control treatment, with an increase of approximately +2% to + four%.

Table 24. Foliar application of Ec.Flg22 and Bt polypeptides. Flg22 in corn provided an increase in plant height

Corn Foliage Treatment Height (cm) at 3 weeks (standard deviation, STDEV) Height (cm) at 5 weeks (STDEV) (Height (cm) ΔAltitude as a percentage of reference altitude Ec.Flg22, 1 µM 47.00 (8.30) 64.60 (6.93) 17.60 +8.3% Ec.Flg22, Retro-inverse, 1 µM 48.62 (6.62) 62.00 (4.07) 13.38 +3.9% Bt4Q7Flg, 22
1 µM 50.10 (6.79) 61.89 (7.03) 5.40 +3.7% Bt 4Q7Flg22, Retro-inverse, 1 µM 49.05 (4.28) 61.03 (7.13) 11.98 +2.3%

Example 8: Use of Retro-Inverse Bioactive Flg22 Primer Polypeptides to Promote Growth Under Stress - Maize

[0460] Abiotic stress causes significant yield losses and can lead to a significant reduction in yields and potential yields. Flagellin compositions and flagellin-associated bioactive priming polypeptides can be used as chemical priming agents to increase a plant's tolerance to one or more abiotic stresses. A foliar treatment was performed using Ec.Flg22 and Bt.4Q7Flg22 and retro inverse forms (RI) of both of these bioactive priming polypeptides to determine if these polypeptides were capable of conferring a protective advantage against heat and drought stress when applied foliarly.

[0461] Corn seeds (hybrid Beck's 5828 YH) were planted and cultivated as described in Example 6, except that a 16 hour day/8 hour light cycle was used. The temperature was cycled from 21°C during the day to 15°C at night, with a humidity of 75%. The light cycle was sufficient to provide a uniform, approximately 300 µmol m ^-2 s ^-1 adequate illumination for plant growth. Plants were measured 3 weeks post-emergence and then treated with natural or retro-inverse (RI) foliar formulations of Ec.Flg22 (SEQ ID NOS: 526-527) or Bt.4Q7Flg22 (SEQ ID NOS: 226 and 376) at a concentration of 1 μM. Control plants were treated with water only. One week after the spray treatment, the plants were divided into 2 groups, with one group left under the same standard environmental conditions for growth as described, and the other group was transferred to environmental conditions providing heat and water stress. Under environmental conditions characterized by heat stress, the temperature was raised using heat mats from 21°C to 27°C for 18 hours a day over a period of 5 days. Plants were left without water during heat stress to further mimic water stress. Plant height change (cm) was measured after another 2 weeks at the 5 week point and recorded as a percentage of control (water treated) plant height. Measurements were recorded as the combined average of two trials with 9 plant replicates per trial (Table 25).

[0462] As shown in Table 25, both natural forms of the bioactive primer polypeptides (Ec.Flg22 and Bt.4Q7Flg22) increased plant growth relative to control plant height when applied under non-stress conditions. These two treatments provided plants with heights of 103% and 108% of the respective controls. However, only maize plants treated with Flg22 retro-inverse polypeptides (both retro-inverse polypeptides, Ec.Flg22 and Bt.4Q7Flg22) showed enhanced plant growth compared to control plants under both normal and heat/water conditions. stress. Plants treated with retro-inverse Ec.Flg22 reached 103% of the height of the respective control under both conditions. Plants treated with Bt.4Q7Flg22 reached 102% and almost 108% of the height of the corresponding control under non-stress and stress conditions, respectively.

[0463] Accordingly, corn plants that were treated with retro-inverse Flg22 polypeptides (RI-Ec.Flg22 and RI-Bt.4Q7Flg22) showed improved growth, as indicated by a percentage increase in plant height relative to control plants. This result suggests that retro-inverse forms are more stable and able to survive without proteolytic degradation under more severe environmental conditions or situations that create conditions for abiotic stress. Accordingly, they may provide a protective advantage in plants exposed to abiotic stress.

Table 25. Foliar Application of Ec.Flg22 and Bt.Flg22 in Maize Cultivated in Nonstressed and Stressed Environmental Conditions

Corn Foliar Treatment (no heat stress) Without stress
(Heights (cm) in % normalized to control height Under stress
(Height as a percentage of control height Ec.Flg22, 1 µM 108.3% 95.8% Retro-inverse Ec.Flg22, 1 μM 103.9% 103.5% Bt. 4Q7Flg 22, 1 µM 103.7% 100.1% Retro-inverse Bt.4Q7Flg22, 1 µM 102.3% 107.8%

Example 9 Heat and Water Stress after Flg22 Polypeptide Foliar Treatment in V2-V3 Stage Maize

[0464] In a separate experiment, corn plants cultured as described in Example 8 were treated with Bt.4Q7Flg22 along with a surfactant prior to exposure to heat and water stress. Triple trials with 18 replicate corn plants per trial were grown in a controlled growing room to V2-V3 developmental stage. Each plant was treated with a foliar spray containing 0.1% surfactant, with or without Bt.4Q7Flg22 (1 μM final concentration). One week after spraying, the plants were transferred to an environment providing heat and water stress. Heat stress was created using heat mats to raise the ambient temperature from 21°C to 27°C. During the period of heat stress, the plants were left without watering. The corn plants were kept under simulated abiotic stress for one week and then plant height (cm) was measured again (Table 26).

[0465] As shown in Table 26, in two of the three trials, the use of the Bt.4Q7Flg22 polypeptide as a foliar spray (trials 1 and 3) resulted in a significant improvement in growth (height measured in centimeters) in corn plants compared to controls. plants treated separately with a surfactant. Foliage treatment with the bioactive Bt.4Q7Flg22 priming polypeptide resulted in an almost 13% increase in plant height in Trial 1 and more than a 33% increase in Trial 3 compared to control (surfactant treated alone) plants.

Table 26. Change in corn plant height with Bt.4Q7Flg22

Corn processing Height (cm) before stress,
2 weeks (STDEV) Height (cm)
after the stress
4 weeks (STDEV) (Height (cm) (Height as a percentage of reference height Trial 1 Surfactant (0.1%) 17.62 (2.32) 27.96 (3.02) +10.34 100.0% Bt.4Q7Flg22 (1 µM) 17.72 (2.08) 29.39 (3.04) +11.68 112.9% Trial 2 Surfactant (0.1%) 15.93 (1.22) 25.26 (1.99) +9.32 100.0% Bt.4Q7Flg22 (1 µM) 16.03 (1.97) 25.31 (6.29) +9.28 99.5% Trial 3 Surfactant (0.1%) 13.16 (2.28) 21.43 (2.89) +8.28 100.0% Bt.4Q7Flg22 (1 µM) 14.99 (1.97) 26.02 (3.21) +11.03 133.2%

Example 10 Flg22 Polypeptide Seed Treatment - Corn and Soy

[0466] Maize seeds of two separate hybrids (Beck's 5828 AM and 4606 P2 hybrids) were treated with bioactive Bt.4Q7Flg22 priming polypeptides (SEQ ID NO: 226) applied to the surface of each seed at final concentrations in suspension of 0.25 μM or 1. 0 μM (table 27). Seed agents were prepared using a stock solution of a 40 μM polypeptide diluted to the appropriate concentration in a slurry containing a fungicide, an insecticide, beneficial bacteria, a coloring agent and a seed finisher (EverGol Energy (0.031 mg ai/seed), PONCHO /VOTiVO (0.6 mg ai/seed), Peridium 1006 (5 fl oz/cwt, or 147.9 ml/cwt), and Pro-Ized Red Colorant (regular) (0.5 fl oz/cwt). for seed treatment was applied using Wintersteiger HEGE II (Wintersteiger AG, Austria, Germany).

[0467] Seeds were planted at 12 locations in the US Midwest (Iowa, Illinois, Indiana). Harvested on 16 randomized blocks of replicates for each of the treatments with the Flg22 polypeptide, including the introduction of Bt.4Q7Flg22 at concentrations in suspension 0.25 μm and 1.0 μm.

[0468] Table 27 shows that a seed treatment with a bioactive Bt.4Q7Flg22 priming polypeptide, applied in an amount equivalent to a 40 μM polypeptide solution, at a flow rate of 0.035 or 0.14 fl oz (2.6 or 10.2 ml / ha) of polypeptide solution per unit of corn seed resulted in an increase in yield with an average increase of +2.1 bushels per acre (131.8 kg/ha) when treated at a low rate, and an average increase of +5.3 bushels per acre when treated at a high rate compared to untreated control seeds (no seed treatment).

Table 27 Treatment of maize seeds with Flg22 polypeptides

Treatment
corn Peptide Concentration in Suspension for Seed Coating Equivalent consumption when applied to corn seeds, in fluid ounces per unit Average total yield in bushels per acre,
hybrid 1 Average total yield in bushels per acre,
Hybrid 2 Average total yield in bushels per acre,
Hybrid 1 and 2 Yield Change in Bushels per Acre Compared to Control Seeds Control - - 206.65 184.27 197.32 - Bt.4Q7Flg22 0.25 µM 0.035 fl oz 40 µM peptide solution/unit 218.36 182.88 200.62 +2.1 Bt.4Q7Flg22 1.0 µM 0.14 fl oz 40 µM peptide solution/unit 213.44 187.48 202.62 +5.3

[0469] A second study was set up to test the ability of Ec.Flg22, Ec.RI Flg22, Bt.4Q7Flg22, and Bt.4Q7RI Flg22 to promote corn yield. Trials in replicates at 12 locations were set up as described above. Bt.4Q7 Flg22 provided 2.8 bushels or 71.1 kg with a 50% success rate, Bt.4Q7 RI Flg22 polypeptide provided 0.5 bushels per acre. Ec polypeptide. Flg22 provided a 2.8 bushel per acre (175.8 kg/ha) advantage with a 70% success rate, while Ec.RI Flg22 provided no advantage.

[0470] A third study was designed to examine the benefits of soybean seed treatment with Bt.4Q7 Flg22, Bt.4Q7Flg22 RI, Ec.RI Flg22, and RHPP polypeptides as soybean seed treatments. In a 12-location study, the RHPP polypeptide provided 0.4 bushels/acre (26.9 kg/ha) with a 64% success rate, the Bt.4Q7 Flg22 polypeptide provided 1.3 bushels/acre (87.4 kg/ha) with 64 % success rate, Bt.4Q7 Bt.4Q7Flg22 RI polypeptide delivered 0.3 bushels per acre (20.2 kg/ha) with a 55% success rate, and Ec.RI Flg22 delivered 1.8 bushels per acre (121.1 kg/ha) with a 73% success rate.

Example 11 Application of Flagellin Bioactive Primer Polypeptides in Tomato - Increased Yield

[0471] A foliar application with Bt.4Q7 Flg22 (SEQ ID NO: 226) and Ec. Flg22 (SEQ ID NO: 526) was applied as an exogenous spray at the pre-flowering stage and used to increase yield in tomato.

[0472] Small areas were set up to mimic commercial tomato growing conditions. Cultivation of two hybrids of tomato, "Jetsetter" (Trial 1) and "Better Big Boy" (Trial 2) was started from seedlings in the greenhouse for 42-56 days before planting in raised beds. Tomato plants were planted when the soil temperature at a depth of three inches below the surface (7.6 cm) reached 60°F (15.5°C). Tomato plants were grown in raised beds covered with black plastic mulch. Plants were cultivated using drip irrigation and fertilizers applied according to grower recommendations throughout the growing season to ensure optimum plant growth and yield. Small raised areas were arranged to mimic the planting density used by commercial growers, who typically plant 2600-5800 plants per acre in a single row with 18-30 inches (46-76 cm) between plants in a row, in beds with spacing between centers 5-6.5 feet (1.5-2 m).

[0473] Foliar treatment with Bt.4Q7 Flg22 and Ec.Flg22 low and high operating rates, 1 fl oz per acre (73.1 ml/ha) and 20 fl oz per acre (1461.5 ml/ha) , respectively, was applied to two hybrids at an early stage of flowering (first flowers). Tests in repetitions were carried out at the University of Missouri (Columbia, Missouri) in July. Control plants were treated with equal (working flow) volumes of water. The effects of foliar treatments on yield increase in tomato were determined and the values normalized to the control water treatment were recorded. The average percentage yield change relative to the average control yield is recorded in Table 28.

[0474] Foliar application of bioactive priming polypeptides, both Bt.4Q7Flg22 and Ec.Flg22, increased tomato fruit yield for each hybrid at both low and high operating rates. After averaging the results for two hybrids, it was found that at low and high working consumption of Bt.4Q7 Flg22 increased tomato yield by +25% and +17%, respectively, relative to control plants. Similarly, low and high operating rate treatments with Ec.Flg22 resulted in an average increase in tomato yield of +43% and +46% relative to control plants for the two hybrids.

Table 28: Foliar treatment to increase yield in different tomato hybrids

Foliage Treatment Trial 1:
Yield percentage change relative to
mean value for control;
Hybrid: "Jetsetter" Trial 2:
Yield change as a percentage relative to the mean value for control; Hybrid: "Better Big Boy" Test average
1 and 2 yield change in percent relative to the average value for control Bt.4Q7 Flg22
(1 fluid ounce per acre) +49% +1% +25% Bt.4Q7 Flg22
(20 fl oz per acre) +22% +12% +17% Ec.Flg22
(1 fluid ounce per acre) +61% +25% +43% Ec.Flg22
(20 fl oz per acre) +72% +21% +46%

Example 12 Foliage treatment of tomato plants with Bt.4Q7 Flg22 formulation

[0475] In another experiment, tomato plants (hybrid: "Better Boy") cultivated as described in the previous example were treated with a Bt.4Q7 Flg22 formulation in the first flowering stage. The formulation used consisted of the Bt.4Q7 Flg22 retro-inverse D-RI polypeptide, which was used together with 0.01% (v/v) of a non-ionic surfactant. This formulation was applied to the foliage of tomato plants at a working rate of 1 fl oz per acre (73.1 ml/ha) in a double replicate tomato winter trial in Florida. At harvest, yield was measured as number of fruits per plant, weight (in grams) per fruit, and total yield (in pounds per acre). Table 29 shows yield as percentage comparison or change relative to untreated control (treated with water only) plants.

[0476] Foliar treatment with Bt.4Q7 Flg22 applied at a rate of 1 fl oz per acre (73.1 ml/ha) increased tomato 'Better Boy' yield by an average of 21% compared to untreated (treated with water only) control plants. The reported increase for 'Better Boy' tomato plants was consistent with both an increase in the number of fruits per plant and an increase in fruit weight (Table 29).

Table 29: Foliage treatment with bioactive Flg22 priming polypeptide to increase yield in tomato

Treatment Percent change in number of fruits per plant compared to control Percentage change in weight per fetus
compared to control Percent Yield Change (lbs per acre) vs. Control Bt.4Q7 Flg22
1 fluid ounce per acre +12% +9% +21%

Example 13 Application of Flagellin Bioactive Primer Polypeptides in Peppers - Increased Yield

[0477] Foliar treatments with Bt.4Q7 Flg22 (SEQ ID NO: 226) and Ec. Flg22 (SEQ ID NO: 526) were applied as an exogenous spray at the first flower stage and used to increase yield in two varieties of pepper .

[0478] Foliar treatments with bioactive Bt.4Q7 Flg22 and Ec.Flg22 priming polypeptides were used in small areas designed to mimic commercial pepper (Capsicum) growing conditions. Two pepper cultivars, 'Red Knight' (RK) and 'Hungarian Hot Wax' (HHW) were grown from 6-week-old seedlings in raised beds covered with high water-holding black plastic mulch, pH 5.8-6.6. Plants were cultivated using drip irrigation and fertilizer applied according to grower recommendations throughout the growing season to ensure optimum plant growth and yield. Small raised areas were arranged to mimic the planting density used by commercial growers, who typically plant approximately 10,000-14,000 plants per acre in double rows 14-18 inches (35.6-46 cm) apart on beds with plastic mulch , with 16-24 inches (40.6-61 cm) spacing between plants in a row and 5.0-6.5 feet (40.6-70 cm) spacing between row centers. Pepper plants can also be planted in one row on each bed (5000-6500 plants per acre, or 12,355-16,062 plants per hectare).

[0479] Foliar applications with compositions containing Bt.4Q7 Flg22 and Ec.Flg22 were applied to pepper plants of both varieties at the first flower stage with a working flow rate of 1 fl oz per acre (low level), or 73.1 ml / ha, and 20 fl oz per acre (high level), or 1461.5 ml/ha, and compared with control (treatment with water at the same operating rate). The effects of these foliar treatments on pepper yields were determined from two separately harvested single-harvest crops and normalized to the yield of control plants. The average percent yield change for each treatment relative to the yield of control plants is shown in pounds per acre in Table 29.

[0480] Foliar treatment of pepper plants with bioactive primer polypeptides, either Bt.4Q7 Flg22 or Ec.Flg22, resulted in an overall average increase in pepper yield (in pounds per acre) at both low and high operating rates in both pepper varieties, RK and HHW. The combined average yield for RK and HHW varieties was +53% (low: 1 fl. oz./acre, or 73.1 ml/ha) and +25% (high: 20 fl. oz./acre) for those treated with foliar application with Bt.4Q7 Flg22 pepper plants compared to control pepper plants. Alternatively, the increase in combined average yield for RK and HHW was higher by +30% (low: 1 fl oz per acre) and +47% (high: 20 fl oz per acre, or 1461.5 ml/ha ) in Ec.Flg22 foliar-treated pepper plants compared to control pepper plants.

[0481] The two pepper cultivars showed different foliar treatment responses and different net yield advantages for both pepper cultivars (Table 30). Significant yield increases were observed with the HHW variety compared to the RK pepper variety and control or untreated plants, with yield increases of +77% (low consumption: 1 fl oz per acre, or 73.1 ml/ha) and +42% (high consumption: 20 fl oz per acre, or 1461.5 ml/ha) relative to control or untreated pepper plants for Bt.4Q7Flg22. In addition, Bt.4Q7Flg22 polypeptides at low application rate (1 fl oz/acre) and Ec.Flg22 polypeptides at high application rate (20 fl oz/acre) most effectively increased yield in HHW variety (both variants provided +72% increase over control plants).

Table 30: Flg22 Foliar Treatment to Increase Yield in Different Pepper Varieties

Foliage Treatment Average percent change in total crop weight (pounds per acre)
Red Knight,
tests in 2 repetitions Average percent change in total crop weight (pounds per acre)
("Hungarian Hot Wax"),
tests in 2 repetitions Cumulative average percent yield change
General value
(pounds per acre) for RK and HHW Bt.4Q7Flg22:
1 fluid ounce per acre +29% +77% +53% Ec.Flg22:
1 fluid ounce per acre +30% +29% +30% Bt.4Q7Flg22:
20 fl oz per acre +8% +42% +25% Ec.Flg22:
20 fl oz per acre +22% +72% +47%

Example 14 Application of Flagellin Bioactive Primer Polypeptides in Pumpkin - Increased Yield

[0482] Bt.4Q7Flg22 foliar treatments were applied exogenously to Ambassador squash in the first flowering stage using two separate formulations (formulation 1=F1 and formulation 2=F2). Formulation 1 (F1) consists of the naturally occurring bioactive Bt.4Q7 Flg22 primer L-polypeptide applied together with 0.01% (v/v) non-ionic surfactant. Formulation 2 (F2) consists of Bt.4Q7 Flg22 RI D polypeptide applied together with 0.01% (w/v) nonionic surfactant. Both formulations, F1 and F2, were applied to pumpkin leaves at a working rate of 1 fl oz per acre (73.1 ml/ha). The yield of plants treated with Bt.4Q7Flg22 F1 and F2 foliar sprays was compared with control (water) or untreated pumpkin plants. Pumpkin plants were cultivated in sandy loam soil as follows. In plastic-covered beds 2.5 feet (0.76 m) wide, 2.5 cm holes were made, placed in two rows in each bed at a distance of 1.5 feet (0.46 m) in each row. The rows in the garden were arranged in a checkerboard pattern. The beds were spaced 4 feet (1.2 m) apart. 3 pumpkin seeds were sown in each hole and thinned out 14 days after planting to leave 1 plant per hole. Drip irrigation pipes were laid in the center of each bed and the plants were watered as needed.

[0483] Pumpkin plants were cultivated from seed in raised beds prior to flowering, and leaf treated at the same location in Florida (FL), with 2 replication trials or 2 separate harvests. Yields of plants treated with Bt.4Q7Flg22 F1 and F2 foliar treatment are presented as number of squash fruits per plant, weight (in grams) per squash, and total squash yield (pounds per acre), and are expressed as percentage change from untreated control plants ( table 31).

[0484] Bt.4Q7Flg22 foliar treatments containing two formulations, F1 and F2, provided an increased yield advantage when applied to pumpkin (Ambassador) leaves at the pre-flowering stage compared to untreated control plants. Both the number of squash fruits per plant, weight per squash, and overall average percent yield change (pounds per acre) were increased in Bt.4Q7Flg22 F1 and F2 treated plants compared to control or untreated plants. Pumpkin plants treated with both formulations with Bt.4Q7Flg22, F1 and F2 showed a similar trend for increased number of pumpkin fruits per plant, weight per pumpkin, and overall average yield change in percent (pounds per acre), however, pumpkin plants treated with foliar application of F1, showed an increase in the number of pumpkin fruits per plant and overall yield of pumpkin relative to plants treated with the F2 formulation.

Table 31: Foliar Treatment with Flg22 Polypeptide Composition to Increase Yield in Pumpkin

Treatment Percent change in pumpkin fruits per plant compared to control Percentage change in weight of one pumpkin compared to control Yield Percentage Change (pounds per acre) vs. Control Bt.4Q7Flg22
1 fluid ounce per acre
Composition 1 +7% +2% +9% Bt.4Q7Flg22
1 fluid ounce per acre
Composition 2 +4% +2% +6%

Example 15 Screening of Flg Polypeptides for Reactive Oxygen Species (ROS) Production in Maize and Soybean

[0485] Taking into account the frequency of codon usage, mutations were obtained in Bt.4Q7Flg22 for better matching with the host organism and binding of the Flg22 polypeptide to the FLS receptor on the surface of plant cells. A probabilistic approach was used to generate three variants of native Bt.4Q7Flg22 designed to contain preferred amino acid signatures for corn and soybean and perform at the same or higher potency than native Bt.4Q7Flg22 (SEQ ID NO: 226) in potency assays. AFK. These variants contained mutations in the internal segment (SEQ ID NO: 571), or at the C-terminus (SEQ ID NO: 572), or at the N-terminus (SEQ ID NO: 573), and were named: Bt.4Q7Flg22-Syn01 , Bt.4Q7Flg22-Syn02 and Bt.4Q7Flg22-Syn03, respectively. Then measurements were made for Bt.4Q7Flg22-Syn01 and Bt.4Q7Flg22-Syn03, comparing them with natural forms at various concentrations.

[0486] Fresh leaf tissues of corn (hybrid 5828 YX) and soybean (hybrid 297 R4) plants were cut into identical samples and placed on the surface of 150 μl of sterile water in the wells of a 96-well white low-luminescence plate. The plate was placed under culture lamps with 16/8 light/dark cycles at a constant temperature of 22°C.

[0487] To obtain maize samples, aboveground tissue of V1-V4 maize plants was cut from the plant above the soil line using a clean razor blade. Cotyledons and first leaves were removed. The stems were cut into 1 mm pieces, from the base of the plant to about 1.3 cm below the first leaf node. Each section of corn was placed in an individual well of a 96-well plate.

[0488] To obtain samples of soybean, fully expanded trifoliate leaves were cut from plants at the stage V1-V3. Leaf discs (12.6 mm ² ) were cut from the leaf blades using a clean, sharp 4 mm diameter cork drill. The discs were cut in half using a clean razor blade and each disc half was placed in an individual well of a 96-well plate.

[0489] Stock solutions of natural Flg22 polypeptide (SEQ ID NO: 226) or Flg22 polypeptides containing the described mutations (SEQ ID NO: 571 or 573) were prepared either in sterile deionized water or in 100 mM sodium phosphate buffer (pH 7.8 -8.0) with 0.1% Tween-20. After 18-24 hours, water was removed from all wells of the 96-well plate. Plant tissue samples were treated with 100 µl of an elicitor solution containing a 1:100 dilution of a stock solution of the Flg22 polypeptide (concentration range from picomolar (250 pM) to micromolar (10 µM)), 34 µg/ml luminol, and 20 µg/ml horseradish peroxidase. Recognition of the Flg22 polypeptide by plant tissue led to the activation of immune signaling and the production of apoplastic reactive oxygen species (ROS). In the presence of ROS (H ₂ O ₂ ), horseradish peroxidase catalyzed the oxidation of luminol and the generation of visible light. Relative light units (RLU) were recorded using a GLOMAX 96 microplate luminometer (Promega Corporation) with 0.5 s integration; at intervals of 2.6 minutes over a period of 40 minutes.

[0490] For data analysis, the total number of RLUs generated for each sample over the entire 40-minute time period was calculated. Significantly outliers outside the interquartile range were excluded from the analysis. The total number of RLUs in all conditions (n=6-16) was normalized to the average RLU value for Bt.4Q7Flg22 at a concentration of 25 nm and recorded as a percentage (%) of the Bt.4Q7Flg22 control (table 32).

[0491] Synthetic mutagenesis variant Bt.4Q7Flg22-Syn01 increased ROS activity in the concentration range (0.25-100 nM), while Bt.4Q7Flg22-Syn03 was more diverse and showed increased ROS activity at concentrations of 0.25 nM, 1 nM, 10 nM, 25 nM and 100 nM compared to natural Flg22 or Bt.4Q7Flg22 variant. The synthetic version of the agent with Bt.4Q7Flg22-Syn01, when using 5 nM, provided the maximum change in ROS activity relative to the natural variant or Bt.4Q7Flg22. The activity of ROS in response to the application of Bt.4Q7Flg22-Syn03 in the range of added concentrations was more diverse.

Table 32. The obtained synthetic Flg mutants (Syn-01 and Syn-03) have a higher activity in the analysis of ROS compared to natural Bt.4Q7Flg22 in a wide range of concentrations.

Concentration (nM) Bt.4Q7Flg22
(SEQ ID NO:226) Bt.4Q7Flg22-Syn01
(SEQ ID NO: 571) Bt.4Q7Flg22-Syn03
(SEQ ID NO: 573) 0.25 8.12 23.56 14.86 0.5 14.86 55.00 14.86 one 23.85 57.04 41.47 5 57.00 113.00 57.00 ten 76.85 116.34 85.70 25 100.00 118.05 111.40 100 113.74 120.83 162.29 1000 127.76 121.20 97.67

Example 16 ROS Screening Assays for Identification of Functionally Active Flg Polypeptides for Maize and Soybean

[0492] Based on the results of preliminary studies in Example 15, the following concentrations were selected to screen a wide range of Flg22 polypeptides for ROS activity in corn and soy: 5 nM for corn (hybrid 5828 YX) and 100 nM for soy (hybrid 297 R4). Thereafter, ROS activity assays were used to identify the best candidate bioactive Flg22 priming polypeptides for individual application in corn and soybeans, and to identify candidates active in both corn and soybeans.

[0493] Maize and soybean leaf tissues were harvested and ROS assays were performed as previously described in Example 15 for the mutant polypeptides shown in Table 33. The total amount of RLU produced was calculated for each sample over the entire 40 minute time period. Significantly outliers outside the interquartile range were excluded from the analysis. ROS activity was compared between corn (hybrid 5828 YX) and soybean (hybrid 297 R4) and reported as a percentage (%) of relative light units (RLU) compared to mean RLU values when treated with Bt.4Q7Flg22 at 25 nM (Table 33 ).

[0494] Table 33 summarizes the relative activity for various Flg22 mutant polypeptides compared to natural Bt.4Q7Flg22, plus standard deviation for each condition (STDEV).

Table 33 Comparison of ROS activity for different Flg22 polypeptides in corn and soy

SEQID NO: Amino acid sequence Corn (5828 YX),
5 nM polypeptide Soya (297 R4),
100 nM polypeptide Average activity (%) STDEV Average activity (%) STDEV Bt.4Q7Flg22
Bacillus thuringiensis
SEQ ID NO: 226 DRLSSGKRINSASDDAAGLAIA 100 _ 100 _ Bt.Flg22-Syn01
Mutant S13K
Bacillus thuringiensis
SEQ ID NO: 571 DRLSSGKRINSAKDDAAGLAIA 142.9 39.3 112 3.0 Bt.Flg22-Syn02
Mutant A20Q
Bacillus thuringiensis
SEQ ID NO: 572 DRLSSGKRINSASDDAAGLQIA 78.3 26 68.7 14.0 Bt.Flg22-Syn03
Mutant D1Q
Bacillus thuringiensis
SEQ ID NO: 573 QRLSSGKRINSASDDAAGLAIA 122.1 29.5 113.5 42.6 Bm.Flg22-B1
Bacillus manliponensis
SEQ ID NO: 290 NRLSSGKQINSASDDAAGLAIA 106.0 25.2 74.6 4.9 Ba.Flg22-B2
Bacillus anthracis
SEQ ID NO: 295 NRLSSGKRINSAADDAAGLAIA 134.7 56.8 83.0 26.6 Bc.Flg22-B3
Bacillus cereus
SEQ ID NO: 294 DRLSSGKRINNASDDAAGLAIA 80.3 18.4 90.0 35.5 A spp.Flg22-B4
Aneurini-bacillus spp.XH2
SEQ ID NO: 300 ERLSSGYRINRASDDAAGLAIS 78.1 20.1 133.1 23.9 Ba.Flg22-B5
Bacillus aryabhattai
SEQ ID NO: 289 EKLSSGQRINSASDDAAGLAIS 27.1 2.3 42.2 7.4 P spp.Flg22-B6
Paenibacillus spp. strain HW567
SEQ ID NO: 293 GKLSSGLRINGASDDAAGLAIS 135.3 31.6 112.5 22.8 L spp.Flg22-L1
Lysinibacillus spp.
SEQ ID NO: 291 LRLSSGYRINSAADDAAGLAIS 26.6 3.6 64.1 14.1 L spp.Flg22-L2
Lysinibacillus spp.
SEQ ID NO: 580 EKLSSGLRINRAGDDAAGLAIS 104.5 1.2 128.6 29.5 L spp.Flg22-L3
Lysinibacillus spp.
SEQ ID NO: 581 EKLSSGYKINRASDDAAGLAIS 36.4 7.9 96.9 20.6 L spp.Flg22-L4
Lysinibacillus spp.SG9
SEQ ID NO: 582 LRISSGYRINSAADDPAGLAIS 60.1 5.9 117.9 25.7 Lf.Flg22-L5
Lysinibacillus fusiformis
SEQ ID NO: 583 LRISTGYRINSAADDPAGLAIS 59.3 5.8 111.6 27.5 Lm.Flg22-L6
Lysinibacillus macroides
SEQ ID NO: 584 EKLSSGFRINRAGDDAAGLAIS 58.7 19.4 112.3 42.3 Lm.Flg22-L6
Lysinibacillus
xylanilyticus
SEQ ID NO: 585 EKLSSGYKINRAGDDAAGLAIS 33.7 1.4 77.0 19.2 Pa.Flg22
Pseudomonas aeruginosa
SEQ ID NO: 530 QRLSTGSRINSAKDDAAGLQIA 116.0 32.5 88.6 22.2 Ec.Flg22
Escherichia coli
SEQ ID NO: 586 ERLSSGLRINSAKDDAAGQAIA 95.0 46.7 116.8 13.3 Xcc.Flg22
Xanthomonas campestris, patovar campestris, strain 305 or
(Xanthomonas citri, patovar citri)
SEQ ID NO: 532 QRLSSGLRINSAKDDAAGLAIS 143.3 5.2 96.4 17.6 Ea.Flg22
Erwinia amylovora
SEQ ID NO: 534 QRLSSGLRINSAKDDAAGQAIS 125.2 9.2 91.9 10.1 Bp.Flg22
Burkholderia phytofirmans strain PsJN
SEQ ID NO: 536 TRLSSGKRINSAADDAAGLAIS 111.2 14.0 67.2 3.0 Bu.Flg22
Burkholderia ubonensis
SEQ ID NO: 538 NRLSSGKRINTAADDAAGLAIS 92.9 12.7 91.1 12.9 Ps.Flg22
Pseudomonas syringae, patovar actinidiae ICMP 19096
SEQ ID NO: 540 TRLSSGLKINSAKDDAAGLQIA 154.4 20.7 113.1 19.6

[0495] Based on the results from Table 33, a number of predictions can be made based on the effect of various Flg22 polypeptide mutations on ROS activity in corn and soybeans. Table 34 describes ROS activity observed or predicted for various targeted mutations. Briefly, substitutions of the first amino acid (D1N, D1Q, or D1T) result or are expected to result in the Flg22 receptor being recognized and/or activated in maize. Mutations in the internal segment, K7Y, K7F and A16P, are expected to produce similar positive results in soybeans. Of all the polypeptides tested, Bt.4Q7Flg22-Syn01 (S13K) and Bt.4Q7Flg22-Syn03 (D1Q) had the most pronounced ROS-inducing activity in corn and soybeans.

Table 34. Summary of results for mutant variants of native Bt.4Q7Flg22

SEQID NO Amino acid sequence Description of the results of the action on ROS activity SEQ ID NO: 226 DRLSSGKRINSASDDAAGLAIA Bt.4Q7Flg22
Bacillus thuringiensis
(natural variant used as standard for comparison) SEQ ID NO: 571 DRLSSGKRINSAKDDAAGLAIA S13K mutation: pronounced activation of ROS in both corn and soybeans SEQ ID NO: 572 DRLSSGKRINSASDDAAGLQIA A20Q mutation: negative effect on ROS activation in both corn and soybeans SEQ ID NO: 573 QRLSSGKRINSASDDAAGLAIA Mutation D1Q: Pronounced ROS activation in both corn and soybeans SEQ ID NO: 574 NRLSSGKRINSASDDAAGLAIA Mutation D1N: Pronounced ROS activation in both corn and soy* (predictable) SEQ ID NO: 575 TRLSSGKRINSASDDAAGLAIA Mutation D1T: Pronounced ROS activation in both corn and soy* (predictable) SEQ ID NO: 576 DRLSSGYRINSASDDAAGLAIA Mutation K7Y: Pronounced ROS activation only in soy* (predictable) SEQ ID NO: 577 DRLSSGFRINSASDDAAGLAIA Mutation K7F: Pronounced ROS activation only in soy* (predictable) SEQ ID NO: 578 DRLSSGKRINSASDDPAGLAIA Mutation A16P: Pronounced ROS activation only in soy* (predictable) SEQ ID NO: 579 DRLSSGKRINSASDDAAGLAIA K7Q mutation: pronounced decrease in ROS activation in both corn and soy* (predictable)

Example 17: ROS Activity Assays to Identify Flg Polypeptide Combinations for Maize and Soybean

[0496] Leaf tissues of corn and soybean plants were harvested and ROS analyzes were performed as previously described in Example 15. Relative ROS activity using different Flg22 variants, alone or in combination, was evaluated to identify preferred combinations of Flg22 polypeptides that provide the maximum response from ROS activity when used together in both corn and soybeans. The results are summarized in table 35.

Table 35. Flg22 combinations providing increased ROS activity in corn and soybeans

Flagellin composition Amino acid sequence Corn (5828 YX),
5 nM polypeptide Soya (297 R4),
100 nM polypeptide Average activity (%) STDEV Average activity (%) STDEV Bt.4Q7Flg22
Bacillus thuringiensis
SEQ ID NO: 226 DRLSSGKRINSASDDAAGLAIA 100 _ 100 _ Bt.Flg22-Syn01
Bacillus thuringiensis
SEQ ID NO: 571 DRLSSGKRINSAKDDAAGLAIA 122.48 31.69 83.54 36.21 Ba.Flg22-B2
Bacillus anthracis
SEQ ID NO: 295 NRLSSGKRINSAADDAAGLAIA 142.53 7.45 97.59 68.59 A spp.Flg22-B4
Aneurinbacillus spp.XH2
SEQ ID NO: 300 ERLSSGYRINRASDDAAGLAIS 53.64 1.45 106.37 16.48 P spp.Flg22-B6
Paenibacillus spp. strain HW567
SEQ ID NO: 293 GKLSSGLRINGASDDAAGLAIS 103.61 37.59 132.95 54.72 L spp.Flg22-L2
Lysinibacillus spp.
SEQ ID NO: 574 EKLSSGLRINRAGDDAAGLAIS 113.04 28.89 138.86 53.66 FLG22-Syn01
+B2+B4
+B6+L2 Combinations of polypeptides as described above 148.52 6.30 132.35 53.99 FLG22B2
+B4
+B6+L2 Combinations of polypeptides as described above 128.31 0.65 139.74 55.00 FLG22-Syn01
+B2
+B6+L2 Combinations of polypeptides as described above 122.81 29.81 124.51 67.31 FLG22-Syn01
+B4
+B6+L2 Combinations of polypeptides as described above 119.17 8.02 100.97 25.95 FLG22-Syn01
+B6+L2 Combinations of polypeptides as described above 124.67 8.69 103.45 34.03 FLG22-Syn01
+B2+B4 Combinations of polypeptides as described above 143.02 7.08 120.67 24.76

Example 18 Cellobiose Supplemented ROS Activity Assay - Corn and Soy

[0497] Cellobiose is a disaccharide consisting of glucose and is a building block for the cellulose polymer. Chemically, it is glucose-beta-1-4-glucose, a reducing sugar that consists of two β-glucose molecules linked by a β(1-4) bond. Cellobiose is obtained by the decomposition of cellulose or lichenin, and when hydrolyzed, it gives glucose. Bt.4Q7Flg22 treatment with and without cellobiose was compared in ROS activity assays to determine if cellobiose could act as an elicitor to increase ROS production in reactions involving the Flg22 polypeptide. The following specific treatment was carried out using ROS assays on corn (FIG. 6, panel A) and soybean (FIG. 6, panel B) leaves: Bt.4Q7Flg22 at 25 nM; Bt.4Q7Flg22 at a concentration of 25 nM + cellobiose at a concentration of 100 μM; Bt.4Q7Flg22 at 25 nM + cellobiose at 1 mM; 100 mm sodium phosphate buffer - control; and cellobiose separately (100 µM).

[0498] Leaf tissues of corn and soybean plants were harvested as previously described in Example 15. Stock solutions of the bioactive Flg22 priming polypeptide were prepared either in sterile deionized water or in 100 mM sodium phosphate (pH 7.8-8.0) buffer with 0.1% Tween-20. After 18-24 hours, water was removed from each well of a 96-well plate. Samples were treated with 100 μl of a solution containing Bt.4Q7Flg22 (SEQ ID NO: 226, 25 nM), cellobiose (100 μM or 1 mM), 34 μg/ml luminol and 20 μg/ml horseradish peroxidase. Recognition of the Flg22 polypeptide by plant tissue led to the activation of immune signaling and the production of apoplastic reactive oxygen species (ROS). In the presence of ROS (H ₂ O ₂ ), horseradish peroxidase catalyzed the oxidation of luminol and the generation of visible light. Relative light units (RLU) were recorded using a GLOMAX 96 microplate luminometer (Promega Corporation) with 0.5 s integration; at intervals of 2.6 minutes over a period of 40 minutes.

[0499] For data analysis, mean RLUs per treatment (n=6-16 samples, +/- standard error of the mean) were plotted over time (FIG. 6). Significantly outliers outside the interquartile range were excluded from the analysis.

[0500] The mean RLU in the experiment for each treatment is plotted in FIG. 6, panel A (corn) and panel B (soy). Although ROS production was observed in the tissues of both plants when using products containing only the Flg22 polypeptide (white circles), the addition of cellobiose at a concentration of 1 mM resulted in significant ROS activity in the tissues of both plants (black circles). The addition of cellobiose at lower concentrations (100 μM) did not alter ROS activity compared to Bt.4Q7Flg22 alone (cf. white and gray circles in Fig. 6, panel A) and did not result in any ROS production in soybean ( gray circles in Fig. 6, panel B). Note that the combination of Bt.4Q7Flg22 at 25 nM and cellobiose at 1 mM resulted in greater ROS production in soybean (ROS peak at approximately 25,000 RLU) compared to maize leaves (ROS peak at approximately 75,000 RLU).

Example 20 Use of Phytosulfokine (FSK-α) to Increase Yield - Maize and Soybeans

[0501] The effect of phytosulfokin-alpha (FSK-α), a sulfonated bioactive priming polypeptide derived from Arabidopsis thaliana, on corn and soybean yield was tested. Corn and soybeans were cultivated in the field as described in Example 1 and 3. CSF (Arabidopsis thaliana (SEQ ID NO: 598) was applied at a final concentration of 1 μM as a foliar spray with a surfactant, and evenly applied to the aerial parts of the plants corn (hybrid 5140RR) and soybean (hybrid 375 NR) At.PSKα formulations were applied at V5-V8 developmental stage in corn and V1-V4 developmental stage in soybean At.PSKα-treated corn and soybean plants were compared with untreated controls plants (water) Treated plants were randomized at one location into four replicate blocks for comparison with control plants Yields were recorded in bushels per acre.

[0502] Table 36 shows how foliar application of At.PSKα resulted in yield increases in both corn and soybean trials. In both corn and soybean, a positive increase in field yield was observed with foliar formulations containing At.PSKα at V5-V8 developmental stage in corn and V1-V4 developmental stage in soybeans. On average, corn saw an overall yield increase of +3 bushels per acre (188.3 kg/ha) in the field and soybeans saw a yield increase of +0.8 bushels per acre (53.8 kg/ha).

Table 36. Foliar application of At.PSKα in corn and soybeans results in higher yields (busels per acre)

Bushels per acre of leafy corn Bushels per acre of leafy soybeans 3.0 0.8

Example 21 Foliar Application of Phytosulfokin-alpha (FSK-α) to Increase Yield - Soybean

[0503] A method is provided in which the use of At.PSKα as a foliar application in actively growing soybean plants provides a yield advantage under environmental conditions characterized by heat and drought stress.

[0504] Soybean plants were cultivated as described in Example 6. The At.PSKα polypeptide (SEQ ID NO: 598) was used as a foliar spray for V1-V4 plants. Then, soybean plants treated with foliar applications with At.PSKα and control plants treated separately with water and surfactant were cultivated under the conditions described in examples 7-9, providing a non-stress and stress (high temperature and water deficiency) environment. Wednesday. Table 37 describes the percentage change or increase in height recorded in soybean plants treated with At.PSKα as a foliar spray in the V1-V4 growth stage. Application of At.PSKα resulted in a +3.5% height increase in non-stressed environments and a +4.3% height increase in stressed environments, reported in bushels per acre, compared to untreated soybean controls.

Table 37 Yield increase in soybeans treated with At.PSKα foliar and grown in non-stress and stress environments

Percent (%) Height Change in Soybean Relative to Control in a Non-Stressed Environment with At.PSKα Soybean Height Change in Percent (%) Relative to Control in a Stressful Environment with At.PSKα 3.5% 4.3%

Example 22 Application of RHPP to Modify Plant Architecture - Maize

[0505] A root spikelet stimulator polypeptide (RHPP, SEQ ID NO: 600) originally developed for soybean (Glycine max) has been proposed as a foliar application agent to provide favorable phenotypes in corn.

[0506] Natural and retro-inverse RHPP (SEQ ID NO: 600-601) is used in V5-V8 stage corn plants. Retro-inverse RHPP can be modified by C-terminal amidation prior to use. Treatment of RHPP in this way is expected to result in a distinct foliage architecture phenotype with vertical leaf orientation and higher directed leaves. Increasing the stem-leaf angle provides significant benefits for agricultural applications in this area. This is particularly true at higher planting densities used to maximize yields in the field. Maize (corn) RHPP polypeptide foliar formulations are suitable for changing the stem-leaf angle, thereby helping to reduce the stem-leaf angle resulting in a vertical leaf orientation. This phenotype may be favorable for increasing leaf area index, reducing shading avoidance syndrome in corn, and improving photosynthetic efficiency. In addition, the use of RHPP as a foliar formulation to maximize canopy development and overall light penetration plays a key role in improving vegetative plant growth prior to initiating the seed filling stage.

Example 23: Application of RHPP to Increase Root Biomass and Yields - Soybean

[0507] Efficient soybean root nodulation results in higher yields and higher seed quality, more protein and oil per seed or acre. This may be due to increased nitrogen fixation, as nodule formation increases nitrogen fixation. To determine whether the bioactive root hair stimulator polypeptide RHPP (SEQ ID NO: 600) was able to modulate root biomass and nodule formation and thus improve nitrogen fixation, soybean plants (Morsoy 38X52 hybrid and Beck's 297R4 hybrid) were treated with a foliar application. with RHPP (300 nM) at the developmental stage R1-R2.

Increased plant biomass and nodule formation

[0508] A bioactive RHPP priming polypeptide (SEQ ID NO: 600, originally derived from Glycine max) was applied as a foliar treatment to a 4 week old hybrid soybean (cv. Morsoy) with 0.1% (v/v) nonionic surfactant substances (ALLIGARE SURFACE™) with a spray bottle, applying approximately 1.25 ml/plant. This experiment was performed on a total of 8 plants per trial per treatment group. The containers were kept in a grow room with artificial lighting, at a light input level of approximately 300 µmol m ^-2 s ^-1 with a 16/8 light cycle and with temperatures ranging from 21°C during the day to 15°C at night. Growth measures: number of nodules, root biomass and total biomass per plant were measured 15 days after foliar application and compared with foliar treatments containing ALLIGARE SURFACE surfactant (0.1% v/v) as control and RHPP polypeptide (300 nM) containing ALLIGARE SURFACE surfactant (0.1% by volume). Average growth rates as described were normalized to control plants treated with surfactant alone (Table 38).

[0509] The counted number of nodules formed on the roots of each plant treated with RHPP foliar application was compared to the number of nodules on control plants treated with 0.1% (v/v) surfactant alone. The RHPP treatment resulted in an approximate doubling in the number of root nodules per soybean plant compared to the control (surfactant) treatment. Soybean plants treated with foliar application with RHPP polypeptide also showed an increase in root biomass and total plant biomass, when normalized to the control gave an increase in root biomass of more than 20% and an increase in total biomass of 8%.

Table 38. Increase in plant biomass and nodulation in soybean (cv. Morsoy) following application of foliar application with bioactive priming polypeptide RHPP (n=8 plant replicate)

Growth rates Control (0.1% v/v ALLIGARE SURFACE surfactant) RHPP (300 nM +
0.1% by volume
ALLIGARE SURFACE) Percent RHPP treatment result, normalized to surfactant-treated control Average number of nodules per plant 8.88 15.13 170.42% Root biomass (g) 1.76 2.13 120.57% Total biomass (g) 42.64 46.24 108.44%

Improved plant growth

[0510] A bioactive RHPP priming polypeptide (SEQ ID NO: 600) was also used as a foliar treatment in R1 hybrid soybean (Beck's 297R4) with 0.1% (v/v) non-ionic surfactant (ALLIGARE SURFACE) using a spray bottle, applying approximately 1.2 ml/plant. This experiment was performed to examine the effects of RHPP on plant growth and was performed using a total of 18 plants per treatment group. The containers were kept in a grow room with artificial lighting, with a light input level of approximately 300 µmol m ^-2 s ^-1 with a light daily cycle of 18/6, and with temperatures ranging from 21°C during the day to 15°C at night. Soybean plants at stage R1 were untreated (untreated control), treated with ALLIGARE SURFACE surfactant at a concentration of 0.1% (v/v) or RHPP polypeptide (300 nM) in combination with ALLIGARE SURFACE surfactant (0.1 % by volume). The height of each plant was recorded at the time of spraying and again 16 days after foliar treatment; compared mean growth rates for different foliar treatments (Table 39).

[0511] Soybean plants treated with foliar application of RHPP polypeptide (300 nM + 0.1% ALLIGARE SURFACE) showed improved plant growth (increased plant height) and increased plant height change compared to plants treated with surfactant alone , and compared with the untreated control (table 39).

Table 39. Growth improvement in soybean (Beck's 297R4) plants following foliar application of bioactive priming polypeptide RHPP (n=18 plant replicates)

Growth rates Raw control Control (surfactant 0.1% ALLIGARE SURFACE) RHPP
(300nM + 0.1%
ALLIGARE SURFACE) Height (cm) 19.3 19.4 19.9 Height measurement (cm) 4.0 3.7 4.6

Example 24: Application of RHPP in combination with fertilizer - Soya

[0512] The bioactive Gm.RHPP priming polypeptide (SEQ ID NO: 600) was applied as a foliar application with liquid foliar fertilizer, N-RAGE MAX (21-1-3 NPK), in two soybean varieties (AG3536 and AG3832). Foliar application with RHPP was applied at a rate of 1 fl oz per acre, or 73.1 ml/ha (300 nM concentration) and soybean fertilizer at the recommended operating rate (1-2 gal/acre (9.4-18.8 l/ha) or equal to 2.16 lb/gal (0.29 kg/L) nitrogen, 0.10 lb/gal phosphate P ₂ O ₅ and soluble potash (K ₂ O, 0.31 lb/gal, or 0 4 kg/l) Foliar application of a combination of RHPP and fertilizer was carried out in two soybean varieties (AG3536 and AG3832) at the R2 development stage (recommended stages R1-R6) at 5 locations in the US Midwest (Iowa, Illinois, Indiana). foliar application with Gm.RHPP with N-RAGE MAX provided a yield advantage of 1.9 bushels per acre (127.8 kg/ha) over the control treatment and an average increase of 1.4 bushels per acre ( 94.2 kg/ha) compared to plants that were treated separately with fertilizer for grade 1 (AG3536) (Table 40).

Table 40. Application of RHPP plus fertilizer

Soybean processing Operating flow in fluid ounces per acre Average total yield in bushels per acre
Grade 1 Average total yield in bushels per acre
Grade 2 Average total yield in bushels per acre
Grade 1 and 2 Average change in bushels per acre from control
Grade 1 and 2 Control - 62.50 62.16 62.33 - N-rage Max 128 63.04 60.29 61.66 -0.67 RHPP 4.0 65.42 61.04 63.23 +0.9 RHPP+
N-RAGE MAX 4.0
128 64.40 60.96 62.68 +0.35

Example 25 Application of Bioactive RHPP Priming Polypeptides in Tomato - Increased Yield

[0513] A foliar application treatment with Gm.RHPP (SEQ ID NO: 600) was carried out by exogenous spraying at the pre-flowering stage and was used to increase yield in tomato. Two tomato hybrids ("Jetsetter" and "Better Big Boy") were planted in small areas as described in Example 12. A foliar treatment with Gm.RHPP was applied at a working rate of 1 fl oz per acre (73.1 ml/ha) and 20 fl oz per acre (1461.5 ml/ha) in two hybrids, 'Jetsetter' (Trial 1) and 'Better Big Boy' (Trial 2), at an early flowering stage (first flowers). Replicate trials were conducted in the US Midwest (Missouri) in July. Foliar treatment with Gm.RHPP in tomato plants was compared with control (treatment with water at the same operating rate). The effects of foliar treatments on yield increase in tomato were determined, normalized to the control water treatment, and recorded as the average yield change in percentage relative to the average yield of the control in Table 41.

[0514] The average yield, presented as a percentage change relative to control plants, was recorded separately for two trials and as an average of two tomato hybrids. Foliar treatment with Gm.RHPP resulted in increased tomato fruit yield in each of the two trials when applied at an operating rate of 1 fl oz per acre (73.1 ml/ha). The application of Gm.RHPP resulted in an average increase in tomato yield of +52% relative to the control plants in the two hybrids, with an individual average increase of +93% for the Jetsetter hybrid and +10% for the Better Big Boy hybrid compared to the control plants.

Table 41: RHPP Foliar Treatment to Increase Yield in Different Tomato Hybrids

Foliage Treatment Trial 1:
Yield percentage change relative to
mean value for control;
Hybrid: "Jetsetter" Trial 2:
Yield change as a percentage relative to the mean value for control; Hybrid: "Better Big Boy" Test average
1 and 2 yield change in percent relative to the average value for control Gm.RHPP
(1 fluid ounce per acre) +93% +10% +52%

Example 26 Application of RHPP in Peppers - Increased Yield

[0515] A foliar treatment with Gm.RHPP (SEQ ID NO: 600) was applied by exogenous spraying in the first flowering stage to increase yield in two varieties of pepper. A foliar treatment with Gm.RHPP was applied in a small area set up to mimic commercial growing conditions for pepper (Capsicum) as described in Example 13. two varieties of pepper, 'Red Knight' (RK) and 'Hungarian Hot Wax' (HHW). A foliar treatment of Gm.RHPP was carried out at an operating rate of 1 fl oz per acre (73.1 ml/ha) on RK and HHW pepper plants and compared with a control (treatment with water at the same operating rate). The effects of foliar treatments on pepper yield were determined from two separately harvested single harvest crops and normalized to the yield of control plants. The average percent change in yield relative to that of the control plants is recorded in Table 42 as the percent change in total weight (in pounds per acre) of pepper harvested. The average percentage change in yield is recorded for 2 replicate crops (tests) for pepper varieties RK and HHW, and then as a combined average for both varieties.

Table 42: RHPP Foliar Treatment to Increase Yields in Different Pepper Varieties

Foliage Treatment Average percent change in total crop weight (pounds per acre) for Red Knight Average percent change in total crop weight (pounds per acre) for
Hungarian Hot Wax Cumulative average percent change in total yield
(in pounds per acre) for RK and HHW Gm.RHPP
1 fluid ounce per acre +87% +46% +67%

[0516] The average percentage yield of RK and HHW pepper plants treated with Gm.RHPP at 1 fl oz. per acre (73.1 ml/ha) was increased by 87% for RK pepper and 46% for HHW pepper compared to control plants. The combined mean for both pepper varieties was recorded as a mean 67% increase in percent yield change in Gm.RHPP foliar treated pepper plants relative to untreated (water) pepper control plants (Table 42).

Example 27: Use of harpin-like polypeptides and At.PSK (in maize

[0517] Harpins can provide functional benefits when applied both exogenously, e.g., on the surface of a plant as a foliar spray, and apoplasticly (in the space on the outside of the plant cell membrane) or endogenously (inside the plant cell/on the inside of the plant cell membrane). cells). A synthetic harpin bioactive priming HpaG-like polypeptide (Xanthomonas spp., SEQ ID NO: 587) was applied exogenously to the surface of V2-V3 developmental maize plants. In addition, the effect of exogenous application of phytosulfokin-alpha (FSK-α), a sulfonated bioactive priming polypeptide derived from Arabidopsis thaliana, on maize growth was tested.

[0518] Corn plants (hybrid Beck's 5828 YH) were grown in a controlled growing room. Corn seeds were planted directly into 39.7 cm ³ containers containing Timberline vegetable soil to a depth of 2.54 cm, 2 seeds per container. After planting, 50 ml room temperature water was added to each container to ensure germination. The containers were placed in a grow room with artificial lighting, with an input of approximately 300 µmol m ^-2 s ^-1 (light photons) on a 16/8 light cycle, with temperatures ranging from 21°C during the day to 15°C at night. For plants used the same modes of watering and fertilization.

[0519] Plant height (cm) was measured 3 weeks after emergence. Bioactive priming HpaG-like polypeptides (SEQ ID NO: 587) presented as a 23 amino acid synthetic polypeptide and At.PSKα (SEQ ID NO: 598) were then applied to maize plants as a foliar spray at final concentrations of 1 μM for bioactive primer HpaG-like polypeptides and 100 mM for bioactive primer FSKα polypeptides. Control plants were treated with surfactant (0.01% by volume) separately. One week after the spray treatment, the plants were divided into 2 groups, with one group remaining in the same standard growth environment described above, and the other group transferred to an environment providing heat and water stress. in the growing room (except for temperature and irrigation/fertilization cycles) remained similar to the standard growth environment). Heat stress was provided using heat mats by raising the ambient temperature from 21°C to 27°C. Plants were left without water during the heat stress period to mimic water stress. Plant height change (cm) was measured after 5 weeks and reported as normalized to control plant height or as a percentage of control plant height (treated with water). Measurements were recorded as the combined mean of two trials with 9 plant replicates per trial (Table 43) and presented as percent growth relative to control corn plants that were treated with surfactant water (0.01% v/v), values for which were taken as a standard of 100% (table 43).

Table 43 Height changes in maize plants treated with X. spp. HpaG-like polypeptide and At. FSK-α

Corn processing Height (cm) and (STDEV) after 3 weeks Height (cm)
after non-stress conditions after 5 weeks Height (cm)
after stress
after 5 weeks Plant height normalized as a percentage of reference height under non-stress conditions Plant height normalized as a percentage of control height under stress conditions X. spp. HpaG-like
(1 µM) 47.23 (6.11) 64.10 (5.53) 45.50 (4.37) 107.4% 89.4% At.PSKα (100 nM) 49.36 (8.00) 58.62 (4.84) 54.88 (2.79) 98.2% 107.8%

[0520] Foliar application of the HpaG-like polypeptide showed an improved growth phenotype under normal but not stressful environmental conditions compared to control plants, while foliar application of CSF showed an improved growth phenotype when growing under conditions of heat and water deficiency. stressful, but not in a non-stressful environment.

[0521] In a separate set of replicate tests, similar changes in growth performance were due to foliar application with HpaG-like polypeptide (SEQ ID NO: 587) and CSF((SEQ ID NO: 598). Table 44 shows the change in percent growth maize plants treated with X. spp.HpaG-like polypeptide (final concentration 1 μM) and At.PSKα (final concentration 100 nM) as foliar treatments, as measured by changes in plant height compared to controls (water plus 0.01 % by volume of surfactant) by plants cultivated under optimal (non-stress) and stress environmental conditions.This result suggests that a combined foliar application or sequential application of CSF (with HpaG-like bioactive priming polypeptides) may be suitable for improving plant growth. under standard (non-stressful or optimal for growth) environmental or growth conditions of plants exposed to abiotic stress (e.g. heat stress and water stress).

Table 44 Foliar treatment with Xspp HpaG-like polypeptide and At.PSKα in non-stressed and stressed corn

Treatment Plant height (cm)
Percent change from control (0.01% surfactant)
Non-stress conditions Plant height (cm)
Percent change from control (0.01% surfactant)
stressful conditions Xspp.HpaG-like (1 µM) +5.0% -6.1% At.PSK-α (100 nM) -11.8% +6.1%

Example: 28 Combination of Bt.4Q7Flg22 or Ec.Flg22 with RHPP

[0522] The bioactive priming polypeptides, Bt.4Q7Flg22 and Ec.Flg22, were combined with RHPP and evaluated for yield benefits in soybeans. The combination of either Bt.4Q7Flg22 (SEQ ID NO: 226) or Ec.Flg22 (SEQ ID NO: 526) and RHPP (SEQ ID NO: 600) was used foliarly in two soybean varieties (AG2836, Variety 1; AG3536, Variety 2) at 7 locations in the US Midwest (Iowa, Illinois, and Iowa).

[0523] Foliar application using bioactive Bt.4Q7 Flg22 priming polypeptide (SEQ ID NO: 226; FIG. 4, panel A), Ec. Flg22 (SEQ ID NO: 526; FIG. 4, panel B), and RHPP (SEQ ID NO: 600) was performed individually in soybeans (commercial hybrid Beck's 294 NR) at the R2 developmental stage using varying operating rates of 0.33, 4.0, 8.0, and 16.0 fl oz per acre, or (24, 1 ml/ha, 292.3 ml/ha, 584.6 ml/ha, 1169.2 ml/ha). Average yield (September harvest) in bushels per acre is recorded for soybeans grown at 7 separate locations, both individually for both soybean varieties and as a combined average yield (Table 45). Soybean yield (busels per acre) is also recorded as yield change (in bushels per acre) normalized to soybean control plants for both varieties.

Table 45. Flg polypeptides and RHPP polypeptides increase yield in soybeans

Soybean processing Operating expense of funds in
fluid ounces per acre Average total yield in bushels per acre,
grade 1 Average overall yield in bushels per acre, Grade 2 Average total yield in bushels per acre,
grade 1 and 2 Average increase in bushels per acre compared to control grade 1 and 2 Control - 59.53 61.61 60.57 - Bt.4Q7Flg22 0.33 60.33 61.61 61.02 +0.45 Bt.4Q7Flg22 4.0 57.61 64.19 60.90 +0.33 Bt.4Q7Flg22 8.0 59.05 63.86 61.45 +0.88 Ec.Flg22 0.33 58.62 63.58 61.10 +0.53 Ec.Flg22 4.0 58.02 63.91 60.74 +0.17 Ec.Flg22 8.0 58.27 64.35 61.31 +0.74 Gm.RHPP 0.33 59.15 62.44 60.92 +0.35 Gm RHPP 4.0 58.61 66.35 61.83 +1.26 Gm RHPP 8.0 59.47 62.46 61.08 +0.51 Bt.4Q7Flg22 + Gm.RHPP 4.0
4.0 61.14 64.88 63.18 +2.61 Ec.Flg22+
Gm.RHPP 4.0
16 59.56 62.46 61.08 +0.51

[0524] Soybean variety AG3536 (Variety 2) consistently outperformed AG3536 (Variety 1) in bushels per acre at all 7 locations in the US Midwest. All foliar applications with Bt.4Q7Flg22, Ec.Flg22 and RHPP applied individually at 3 different application rates (0.33, 4.0 and 8.0 fl oz/acre) or (24.1 ml/ha, 292 .3 ml/ha, 584.6 ml/ha) resulted in a yield advantage over untreated control plants. RHPP applied to the leaves at a working rate of 4.0 fl oz per acre (292.3 ml/ha) resulted in a maximum increase in yield of +1.26 bushels per acre (84.7 kg/ha) relative to control plants, according to compared to other bioactive priming polypeptides when used alone. However, the combination of Bt.4Q7Flg22 with RHPP provided an additional yield advantage resulting in an increase of +2.61 bushels per acre (175.5 kg/ha) over untreated soybean controls. This increase in yield observed in soybean plants treated with Bt.4Q7Flg22 foliar application in combination with RHPP illustrates the synergistic effect achieved when bioactive primer polypeptides are combined when the increase in combination yield is greater than the sum of the two polypeptides when applied alone.

Example 29: Use of Agrobacterium tumefaciens to test the effectiveness of thionins in the treatment of HLB disease

[0525] The Agrobacterium tumefaciens GV3101 strain was inoculated with Luria medium (LB) and cultured for 20 hours. Initially, the optical density (OD) of the culture was measured at a wavelength of 600 nm using a spectrophotometer and normalized to a low starting density. The cultures were then divided into equal parts and treated with thionins in similar proportions representative of mixtures used to treat citrus trees. Used ratios of thionine Cs. (SEQ ID NO: 651), thionine As. (SEQ ID NO: 652) and thionine Mt. (SEQ ID NO: 653) were 10.0%, 2.0%, 0.40%, 0.08% and 0.02%, and were prepared in such a way as to obtain 20 ml of the total filtrate volume of each of the mixtures thionin, which is used as a single tree treatment. Each mixture of thionins was also compared to control mixtures containing only: filtrate, minimal medium (LB) or the antibiotic tetracycline (Tet) (10 μg/ml per culture). Each column corresponds to the combined OD measurement for the 3 replicates. After incubation with mixtures of thionins and antibiotic, the optical density (OD 600) was re-measured to determine whether there was a reduction or inhibition of the growth of Agrobacterium cultures.

[0526] As shown in FIG. 8, in all treatments, thionine Cs., thionine As. and thionin Mt., there was a dose-dependent response and reduced growth of Agrobacterium cultures compared to control filtrate, minimal medium (LB) or antibiotic (Tet).

Example 30 Treatment of Candidatus Liberibacter asiaticus Infection with Thionins

[0527] The use of thionins for the treatment of Candidatus Liberibacter asiaticus infection will be tested on citrus trees from orchards located in central Florida (Okeechobee County). For the treatment of a total of 26 trees, thionin mixture formulations (SEQ ID NOs: 620; 621 and 622) with or without a phloem localization sequence (SEQ ID NO: 611) will be used to target said thionins in a specific manner to the phloem, where Candidatus Liberibacter asiaticus lives. Inoculation of 'Valencia' orange (Citrus sinensis) trees with the indicated formulations of thionins and their mixtures will be carried out using a BRANDT ENTREE low pressure injection device. A total of four treatments with thionins, including water as a negative control and oxytetracycline as a positive control, will be given to 5 year old trees. Citrus trees will be randomized into treatment blocks for plots with control (untreated), thionin treated, and positive control antibiotic (oxytetracycline) treated trees. The thionins fused to the phloem targeting sequence will be expressed in the pBC vector and the thionine-containing filtrate will be collected from the expression cells. A total volume of 20 ml containing a mixture of thionines: thionine Cs. (SEQ ID NO: 651), thionine As. (SEQ ID NO: 652) and thionine Ms. (SEQ ID NO: 653) will be presented as 20 ml of the total volume of the filtrate. Thionin-treated citrus trees will be compared with untreated (control) trees and trees treated alone with the positive control, the antibiotic oxytetracycline, at a concentration of 2 grams/tree. Infection levels in Candidatus Liberibacter asiaticus trees will be confirmed by qPCR detection or amplification using 16S rRNA gene-specific primers and nested primers to detect HLB disease [Sequence 5'"3': (forward) HLB as TCGAGCGCGTATGCAATACG; (reverse) HLBr GCGTTATCCCGTAGAAAAAGGTAG; HLBpc (probe) AGACGGFTGAGTAACGCG labeled with fluorescein reporter dye].

[0528] Plants will be treated in March and leaf samples will be collected one month later in April. The average number of Candidatus Liberibacter asiaticus bacteria will be assessed along with scoring of visible symptoms of marbled spotting or signs of leaf and stem yellowing.

[0529] Fruit size, shape, and level of fruit development or maturity will be evaluated for 20 representative fruits per tree. Longitudinal length (main diameter, cm) and width (minor diameter, cm, average between the maximum and minimum width of the fruit if it is not symmetrical). The fruit shape will be measured using the ratio of width to length. The total weight of the fetus will be measured and divided by the total number of fetuses (20) to obtain the average weight of the fetus (in grams). The total fruit weight will be measured and presented in kilograms per tree.

[0530] Brix density, in degrees Brix ( ^o Brix _c ) corrected for acidity, will be calculated in the juice obtained from squeezed grapefruit and orange fruits for each tree, in accordance with the minimum standards of the United States Department of Agriculture (USDA) for laboratory analytical methods for determining ^o Brix _c . The percentage of acid (%, mass/volume) will also be measured. The ^o Brix value on the refractometer for reconstituted juice is equal to the required ^o Brix value corrected for acidity minus the contribution of acid and the effect of temperature. The total titratable acidity (% acid) of the reconstituted juice will also be calculated from the ^o Brix of the reconstituted juice and the ratio of Brix to acidity, and corrected for acidity and temperature correction factors (source: JBT FoodTech Laboratory Manual, “Procedures for Analysis of Citrus Products, Sixth Edition).

[0531] The number of bacterial cells will be calculated using real-time fluorescent PCR, quantitative polymerase chain reaction (qPCR) techniques to detect live bacteria only, and subtract background DNA including deproteinized DNA or DNA from dead cells (Davis and Brlansky, “Quantification of live Candidatus Liberibacter asiasticus” populations using real-time PCR and propidium monoazide”, Plant Disease 97: 1158-1167, 2013). The number of specific colonies with Candidatus Liberibacter asiasticus (CLas) cells will be measured in leaves collected from thionin-treated, untreated (control) and positive control (antibiotic) treated trees. Calculations for live bacterial titers are made based on qPCR DNA yield, fitted with a regression equation to correlate target copy number with total bacteria, and presented as live cells per gram of tissue on a logarithmic scale. Comparative titers from treated and untreated trees will be compared with the severity of disease or disease symptoms such as classic marbled leaf spot, deformed or asymmetric fruit and green fruit, etc., for both red grapefruit and orange trees.” Valencia.

Example 31 Use of Retro-Inverse Bioactive Flg Priming Polypeptides to Treat and Reduce Greening of Citrus Fruits

[0532] Combinations of flagellin-associated polypeptides paired with their retro-inverse equivalents can be used to treat and reduce the greening effect in citrus fruits caused by Asian citrus greening or Huanglong disease (HLB).

[0533] An early symptom of HLB in citrus fruits is yellowing of leaves on a single branch or in one sector of the tree's canopy. Leaves yellowing as a result of HLB show an asymmetrical pattern with uneven yellowing or marbling of the leaf, with green spots on one side of the leaf and yellow on the other. As the HLB disease progresses, fruit size decreases and the juice becomes bitter. The fruit may remain partially green and tends to drop prematurely.

[0534] Retro-inverse forms of Flg22 can compete with natural forms of Flg22 for binding to FLS-associated receptor(s) on the plant surface and thus inhibit/delay the formation of greening symptoms associated with HLB disease. The use of combinations of natural Flg22 and Flg22 RI will help fine-tune the immune response to reduce and even eliminate the disease-causing bacteria, Candidatus Liberibacter asiaticus, and thus prevent the development of acute symptoms such as yellowing of leaves and greening of citrus fruits.

[0535] Treatment with combinations of Flg polypeptides with their retro-inverse (RI) forms will be used to minimize the effect of HLB infection on citrus fruit greening. 34 commercial grapefruit trees, Citrus paradise Macfad., and six sweet orange trees, Citrus sinensis (L.), with or without symptoms of HLB disease, will be treated with the flagellin bioactive primer polypeptide combinations described in Table 46, below, with a low pressure injection device called BRANDT enTREE to distribute Flg polypeptides within a tree.

Table 46. Combinations of natural Flg22 and retro-inverse bioactive Flg22 primer polypeptides

Treatment SEQID NO: nM concentration Bt.4Q7Flg22 226 50 nM Bt.4Q7Flg22 226 100 mM RI Bt.4Q7Flg22 376 50 nM RI Bt.4Q7Flg22 376 100 mM Bt.4Q7Flg22 + RI Bt.4Q7Flg22 226 and 376 50 nM Bt.4Q7Flg22 + RI Bt.4Q7Flg22 226 and 376 100 mM Ec.Flg22 526 50 nM Ec.Flg22 526 100 mM RI Ec.Flg22 527 50 nM RI Ec.Flg22 527 100 mM Ec.Flg22 + RI Ec.Flg22 526 and 527 50 nM Ec.Flg22 + RI Ec.Flg22 526 and 527 100 mM

[0536] Leaf tissue samples from these treated grapefruit and sweet orange trees will be analyzed using the ROS assay as described in Example 15. Samples will be collected from fruit groves from March to August in central Florida. The sample from the citrus orchard is considered representative of the state. Sampling gardens should have a minimum area of 2 hectares (ranging from 2 to 24 hectares, with an average of 5.2 hectares). Citrus trees from the selected orchard will be randomly selected and will include untreated control trees at each randomized site. Leaf tissues from grapefruit and orange trees will be collected from trees of approximately the same age. Leaf samples are taken from similar locations on the trees and only from trees with new growth at the time of sampling. Orchards selected for sampling use similar cultivation practices, including flood irrigation and weed control with herbicides. However, selected orchards will not use any pesticides for at least 30 days prior to taking leaf samples for ROS analysis. Each orchard will be randomly sampled in duplicate in 10 HLB symptomatic grapefruit trees and compared with samples from 14 grapefruit trees (non-infected control) without any symptoms. Similar leaf sampling will be carried out on the sweet orange (four infected samples compared to 2 uninfected controls). Trees that are representative of the entire garden will be selected. A hierarchical analysis of variance (ANOVA) will be performed to determine the statistical significance of any observed differences in ROS activity between control and HLB-infected citrus leaf samples.

Example 32 Foliar Application of Flg22 Polypeptide Reduces Leaf Blight in Soybean

[0537] Foliar application of bioactive Bt.4Q7Flg22 priming polypeptide (SEQ ID NO: 226) derived from Bacillus thuringiensis and Bt.4Q7Flg22 (H1) expressing Bacillus pseudomycoides was used in soybean plants (commercial hybrid Beck's 294 NR) at the developmental stage V3 cultured at 3 separate locations in the US Midwest where Cercospora infection has previously been reported in the field.

[0538] Estimates of cercosporiosis leaves (percentage of affected leaf area) were used to assess the severity of the disease in all field experiments. The percentage of affected leaf area was calculated using a visual cue based on ASSESS image analysis to quantify disease in the plant (source: Chagas Ferreira da Silva, LSU Master's Theses, 2014). Symptom scores as percentages were obtained for the topmost trifoliate leaves.

[0539] The results are shown in Table 47. Externally, soybean plants that were treated with foliar treatments with bioactive Bt.4Q7Flg22 priming polypeptide and Bt.4Q7Flg22 (H1) expressing Bacillus pseudomycoides had increased vitality compared to untreated control plants. Control plants showed an increase in early symptom development when observed at the 4 week time point, 30% compared to 20% with Bt.4Q7Flg22 (0.33 fl oz per acre, or 24.1 ml/ha) and approximately 5% with treated with Bt.4Q7Flg22 (4.0 fl oz/acre, or 292.3 ml/ha). Soybean plants treated with Bt.4Q7Flg22 (H1) expressing Bacillus pseudomycoides also showed less early symptom development from Cercospora infection relative to untreated control plants, 20% after 4 weeks (0.33 fl oz per acre, or 24.1 ml/ ha) and 10% (4.0 fl oz per acre, or 292.3 ml/ha). At 8 weeks post-application, untreated control plants showed visual symptoms of 50% damage to the top tier of the plant's foliage (top 3-4 trifoliate leaves). The symptom score for plants that received the Bt.4Q7Flg22 polypeptide foliar treatment (0.33 fl oz per acre, or 24.1 ml/ha) was comparable to that for untreated control plants 8 weeks after treatment foliage. However, soybean plants that received foliar treatments with Bt.4Q7Flg22 polypeptides (4.0 fl oz per acre) and Bt.4Q7Flg22 (H1) expressing Bacillus pseudomycoides (0.33 fl oz per acre, or 24.1 ml/ ha; and 4.0 fl oz per acre, or 292.3 ml/ha) showed a significant reduction in severe symptoms and damage. Overall, treatment with the Bt.4Q7Flg22 polypeptide (4.0 fl oz per acre, or 292.3 ml/ha) was effective in preventing the development of early symptoms of Cercospora infection relative to untreated plants that showed symptoms of bruising, purple leaves, and shedding. leaves. Accordingly, foliar application of the Bt.4Q7Flg22 polypeptide at a higher application rate (e.g., 4.0 fl oz per acre, or 292.3 ml/ha)) may provide a way to control the development of early symptoms and produce healthier and more viable soybean plants. cultivated in field locations that have been affected by Cercospora.

Table 47: Foliar treatment of soybean plants with Bt.4Q7Flg22 and Bt.4Q7Flg22 expressing Bp. resulted in alleviation of Cercospora disease and symptoms in soybean

Processing - Soy Operating expense of funds in
fluid ounces per acre Percentage of area affected by disease in plants 4 weeks after application Area affected by the disease 8 weeks after application Control - thirty% fifty% Bt.4Q7Flg22 0.33 fl oz per acre twenty% fifty% Bt.4Q7Flg22 4.0 fl oz per acre 5% 35% H1 Bt.4Q7Flg22 0.33 fl oz per acre twenty% 40% H1 Bt.4Q7Flg22 4.0 fl oz per acre ten% thirty%

Example 33 Application in Maize - Enhanced Normalized Difference Vegetation Index (ENDVI) Analysis

[0540] The Enhanced Normalized Difference Vegetation Index (ENDVI) is an indicator of live, photosynthetically active green vegetation and was used to compare the effectiveness of treatments in field trials using remote sensing technology. ENDVI values ranging from -1.0 to 0.1 indicate poor health plants that have reduced photosynthesis, while values close to 1 indicate rich vegetation, high photosynthetic capacity, and increased biomass. Healthy plants actively absorb visible light in the spectral wavelength range of 400-700 nm and reflect light with wavelengths in the near infrared range from 700 to 1100 nm. ENDVI measurements may correspond to certain vegetative properties, such as plant biomass or green color, canopy light absorption, photosynthetic capacity (eg, leaf area index, biomass, and chlorophyll concentration). Images for ENDVI were obtained with a BGNIR camera (Zenmuse X3) attached to a drone (DJI MATRICE 100) designed specifically for image capture and filtering when capturing different wavelengths of light. The camera uses sensors to capture radiation from the electromagnetic spectrum in the visible and near infrared ranges. Healthy plants with a lot of vegetative mass or biomass reflect green (G) and near infrared (NIR) light while absorbing both blue (B) and red light. Plants that are less healthy or have less aboveground biomass reflect more visible light and less NIR light. ENDVI considers two channels, NIR and G, as reflection channels, and B as an absorption channel. In the ENDVI formula below, the values for the NIR and green channels are summed to give the value for the reflection channel. The value for the blue channel is multiplied by two to compensate for the summation of the NIR and G channels. The ENDVI equation uses the following calculations for the NIR, G, and B channel values to obtain the coefficient value as a single output value:

[0541] Corn seeds (hybrid DEKALB DKC 58-89) treated with a seed treatment containing the fungicide EVERGOL (7.18% propiconazole, 3.59% penflufen in combination with 5.74% metalaxyl) and PONCHO/VOTiVO 500 ( a mixture of 40.3% insecticide clothianidin and 51.6% Bacillus firmus I-1582, a microbial agent) was planted in the US Midwest (Illinois). Various foliar treatments containing Bt.4Q7Flg22 and a synthetic variant of Bt.4Q7Flg22 (Syn01Flg22, as described in Table 48) were applied to V5-V7 developmental corn plants. BGNIR images were acquired from drones flying 50 m above the test site three weeks after each foliar treatment was applied and after the corn canopy had closed completely. Individual BGNIR images were processed with drone image analysis software to produce a single orthomosaic image of the test site, which was further analyzed with Fiji imaging software. In the orthomosaic image, the site areas for identifying individual foliar treatments in the field and replicates for each of the treatments were uniquely set using GPS coordinates in each field trial. The treatment replicates identified for rendering were of the same size. Three replicates were collected for each variant of the foliar treatment, and two rows were visualized on each replica site. Within each replicate, the average light intensity for each of the image channels [cyan, green, and near-IR (rendered as red)] was measured on a scale from 0 to 255, where intensity 0=0% reflectance (black pixel) and intensity 255=100 % reflection (white pixel). These mean B, G, and NIR light intensities were used to calculate the ENDVI value using the ENDVI algorithm for plant health assessment (green) for each replica site. The ENDVI values were then averaged over the three replicate sites as described in Tables 49 and 50. The ENDVI values for the treatments were compared to the control treatment at each site. The control treatment included treatment of corn plants cultivated from seeds with the main seed treatment only and did not include the foliar treatment. The foliar treatment formulations were as described and applied at operating rates as shown in Table 48.

Table 48 Flg22 Foliar Treatment Compositions for Corn and Soybean Testing

Composition Composition for foliar application Application rate in fluid ounces per acre or milliliters per hectare (mL/ha) Composition 1 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT) 4 fluid ounces per acre, or 292.3 ml/ha Composition 2 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
11.6 mM sodium phosphate dibasic in combination with 4.2 mM citric acid monohydrate pH 5.6
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 4 fluid ounces per acre, or 292.3 ml/ha Composition 3 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 4 fluid ounces per acre, or 292.3 ml/ha Composition 4 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM + Cellobiose: 320 mM
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 4 fluid ounces per acre (Flg22)
292.3 ml/ha,
8 fl oz per acre (Cellobiose)
584.6 ml/ha Composition 5 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 48 fl oz per acre, or 3507.6 ml/ha Composition 6 Syn01Flg22 (SEQ ID NO: 571) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 4 fluid ounces per acre, or 292.3 ml/ha Composition 7 Syn01Flg22 (SEQ ID NO: 571) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 0.4 fl oz per acre, or 29.23 ml/ha Composition 8 Syn01Flg22 (SEQ ID NO: 571) 16.7 μM + Cellobiose: 320 mM
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 0.4 fl oz per acre (Flg22)
29.23 ml/ha
8 fl oz per acre (Cellobiose)
584.6 ml/ha Composition 9 At.Flg22-B4 (SEQ ID NO: 300)
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 4 fluid ounces per acre, or 292.3 ml/ha

[0542] The leaf treatment compositions contained 0.1% (v/v) PROXEL BC preservative, an aqueous dispersion of a mixture of 330.7 mM 1,2-benzisothiazoline (BIT), 53.5 mM 5-chloro-2-methyl-4- isothiazolin-3-one (CMIT) and 26.1 mM 2-methyl-4-isothiazolin-3-one (MIT). Foliar formulations were applied at a given rate (fluid ounces per acre, or ml/ha) in a vehicle (water) volume of 20 gal per acre with 0.1% (v/v) Alligare Surface™ nonionic surfactant

[0543] As shown in Table 49, foliar formulations containing Bt.4Q7Flg22 and Syn01Flg 22, when applied to V5-V7 corn, resulted in increased ENDVI measurement coefficient values when compared or normalized to plants that did not receive the agents for foliage treatment (control with seed treatment). Bt.4Q7Flg22 foliar formulations in buffered formulations (compositions 2, 3, 4 and 5; sodium phosphate, pH 5.6-5.7) resulted in plants with higher ENDVI values compared to plants who treated Bt.4Q7Flg22 as an unbuffered formulation (composition 1) at a rate of 4 fl oz per acre, or 292.3 ml/ha. However, all ENDVI ratio values in Bt.4Q7Flg22 treated plants (compositions 1-5) were increased compared to untreated control plants. In corn plants, application of composition 4 as a foliar treatment consisting of the Bt4Q7Flg22 polypeptide in combination with cellobiose in a phosphate buffered formulation, when applied at an application rate of 8 fl oz per acre, or 584.6 ml/ha, resulted in +9% an increase in the average value of the ENDVI coefficient relative to the control (only seed treatment) plants. Plants treated with foliar formulations 1 and 5, which differed only in their respective application rates (4 and 48 fl oz per acre, or 292.3 ml/ha and 3.507.6 ml/ha), had similar coefficient values. ENDVI (+3% and +4%) compared to control plants. It is important to note that the higher rate, 48 fl oz/acre, or 3,507.6 ml/ha, did not result in detectable phytotoxicity, which could be seen as a decrease in ENDVI value compared to the control (seed treatment only). Compositions 6, 7 and 8 with synthetically produced Bt.4Q7Flg22 variant (Syn01Flg22) were also used as a foliar spray in V5-V7 developmental maize plants. The Syn01Flg22 polypeptide in the phosphate buffered formulation (Composition 6 and Composition 7) was compared according to operating costs. Syn01Flg22 polypeptide (composition 6) when applied to corn plants with a higher application rate (4 fl oz per acre, or 292.3 ml/ha) resulted in a decrease in the ENDVI ratio or had a lower percentage increase in ENDVI compared to the Syn01Flg22 polypeptide ( composition 7) when applied to plants with an operating rate of 0.4 fl oz per acre, or 29.23 ml/ha; the difference between treatments compositions 6 and 7 was 8%. Cellobiose was added to Syn01Flg22 (Formulation 8) and, similarly to Composition 7, was applied at a working rate of 0.4 fl oz per acre, or 29.23 ml/ha. Foliar application of Syn01Flg22 (composition 7) was compared with Syn01Flg22 in combination with cellobiose (320 mm) (composition 8). Composition 7 and composition 8 with Syn01Flg22 had a similar increase in the ENDVI measurement factor, resulting in a +10% increase over control plants or +8% increase over plants treated with Syn01Flg22 (Formulation 6) at a higher operating rate of 4 fl oz / acre, or 292.3 ml per hectare (ha).

Table 49. Obtained ENDVI scores with Flg22 foliar treatment in DKC 52-61 corn hybrid

Treatment ENDVI (STDEV) Average percent change in ENDVI normalized to control plants* Control seed treatment 0.253 (0.027) _ Bt.4Q7Flg22, composition 1 0.259 (0.019) +3% Bt.4Q7Flg22, composition 2 0.269 (0.021) +6% Bt.4Q7Flg22, composition 3 0.272 (0.003) +7% Bt.4Q7Flg22 + Cellobiose, composition 4 0.276 (0.009) +9% Bt.4Q7Flg22, composition 5 0.263 (0.010) +4% Syn01Flg22 track 6 0.258 (0.016) +2% Syn01Flg22 track 7 0.277 (0.018) +10% Syn01Flg22 + Cellobiose composition 8 0.279 (0.015) +10%

* Rationing for control seed treatment: EVERGOL and PONCHO / VOTiVO 500

[0544] Corn seeds (hybrid DEKALB DKC 52-61) were also treated with Roundup POWERMAX (active ingredient glyphosate, 48.7% as potassium salt) in combination with formulation 3 with Bt.4Q7Flg22. Roundup POWERMAX was used at the recommended application rate of 24 fl oz/acre. Bt.4Q7Flg22 (Formulation 3) was applied at a rate of 4.0 fl oz/acre, or 292.3 ml/ha. The results are shown in table 50.

Table 50. ENDVI foliar application of Flg22 polypeptides in combination with herbicide in corn (hybrid DKC 52-61)

Composition code for processing
Operating expense funds ENDVI (STDEV) Average Percent Change in ENDVI Normalized to Roundup POWERMAX Processing Roundup POWERMAX 0.271 (0.006) _ Roundup POWERMAX + Bt.4Q7Flg22
(track 3) 0.293 (0.005) +8%

*Rated to RoundUp POWERMAX foliar treatment

[0545] As shown in Table 50, Roundup POWERMAX when applied to V5-V7 corn as a foliar herbicide in combination with Bt.4Q7Flg22 (Formulation 3) resulted in a +8% increase in ENDVI measurement ratio compared to Roundup POWERMAX treatment without Bt.4Q7Flg22 polypeptide.

Example 34 Application of Bioactive Priming Polypeptides in V4-V7 Maize - Increased Yield

[0546] Large area test corn was planted from seeds (DEKALB hybrids: DKC 52-61, DKC 58-89 and DKC 65-81) coated with a seed treatment containing EVERGOL fungicide (7.18% propiconazole, 3. 59% penflufen and 5.74% metalaxyl) with PONCHO/VOTiVO 500 (mixture of insecticide clothianidin and microbial agent, Bacillus firmus I-1582). Field trial corn was planted at 8 locations in the US Midwest (Indiana, Illinois, and Iowa). The seed beds in the field at each location were formed using standard or anti-erosion methods for planting corn. Fertilizer was applied according to standard farming recommendations, in the same way for all locations in the US Midwest. Herbicides were used to control weeds with additional loosening of the soil if necessary. In all locations, four-row plots of 5.3 meters were planted. Corn seeds were planted at a depth of 3.8-5.1 cm to ensure the normal development of the roots. Corn was planted at an approximate average density of 42,000 plants per acre, or 103,782 plants per hectare, with an average row width of 0.8 meters and a seed spacing allowing 1.6-1.8 seeds per 30 cm.

[0547] Maize plants at approximately the V5 developmental stage were treated with foliar applications using a foliar treatment composition containing a Bt.4Q7Flg22 polypeptide (SEQ ID NO: 226) and a Bt.4Q7Flg22 synthetic variant, which is described as a Syn01Fflg22 polypeptide (SEQ ID NO: : 571). Leaf treatment compositions containing said Bt.4Q7Flg22 polypeptide and a synthetic variant of Bt.4Q7Flg22 polypeptide were used in 3 corn hybrids (DEKALB hybrids: hybrid 1: DKC 52-61; hybrid 2: DKC 58-89; hybrid 3: DKC 65- 81) planted at 8 locations in the US Midwest (Indiana, Illinois, and Iowa). Corn plants received foliar treatments at concentrations and operating rates as described in Table 51. Corn crops (in bushels per acre) were harvested and recorded in Table 51 as average yields (in bushels per acre) at all locations (8 locations for hybrid 1, 7 locations for hybrid 2, and 6 locations for hybrid 3) and as the average change in bushels per acre compared to the base seed (ST) treated control after surfactant treatment alone.

Table 51. Foliar treatment with Bt.4Q7Flg22 and synthetic mutant Syn01Flg22 - increase in corn yield

Foliage Treatment
(Concentration) Operating expense funds
fluid ounces per acre (ml/hectare) Average yield bushels per acre Average yield change in bushels per acre compared to surfactant-treated control Bt.4Q7Flg22
(16.7 µM)
(track 1) 4.0 fl oz per acre
(292.3 ml/hectare) 201.43 +1.14 Bt.4Q7Flg22
(16.7 µM) + Cellobiose
(320 mm)
(track 4) 4.0 fl oz per acre
(292.3 ml/hectare)
8.0 fl oz per acre
(584.6 ml/hectare) 205.43 +2.55 Syn01Flg22
(16.7 µM)
(track 6) 4.0 fl oz per acre
(292.3 ml/hectare) 203.79 +0.90 Syn01Flg22
(16.7 µM)
(track 7) 0.4 fl oz per acre
(29.2 ml/hectare) 204.36 +1.48 (16.7 µM) + Cellobiose
(320 mm)
(track 8) 0.4 fl oz per acre
(29.2 ml/hectare)
8.0 fl oz per acre
(584.6 ml/hectare) 204.47 +1.59

[0548] Maize plants approximately at the V5 development stage were treated with foliar applications using a foliar treatment composition containing the Bt.4Q7Flg22 polypeptide and a synthetic variant, Syn01Flg22, of the Bt.4Q7Flg22 polypeptide. Bt.4Q7Flg22 polypeptides and the synthetic Bt.4Q7 Flg22 variant were also combined with cellobiose (320 mM), a reducing sugar consisting of two β-glucose molecules linked by a β(1→4) bond, used as an eliciting agent to enhance the effect Flg22 polypeptide. Both Bt.4Q7Flg22 and Syn01Flg22, when used in combination with cellobiose in maize plants, resulted in increased yield stimulation relative to foliar applications of Bt.4Q7Flg22 and Syn01Flg22 polypeptides. A positive yield increase of +2.55 bushels per acre or 160 kg/ha was observed in corn plants treated with Bt.4Q7Flg22 foliar treatment and cellobiose compared to a yield increase of +1.14 bushels per acre or 71 .6 kg/ha for foliar treatment with Bt. 4Q7Flg22 when used alone. There was also a positive yield increase of +1.59 bushels per acre, or 99.8 kg/ha, in corn plants treated with Syn01Flg22 foliar treatment (0.2 fl. oz. per acre, or 14.6 ml/ha) combined with cellobiose, compared to an increase of +1.48 bushels per acre or 92.9 kg/ha yield for Syn01Flg22 foliar treatment at the same application rate. Thus, Bt.4Q7Flg22 and Syn01Flg22 as a foliar treatment for V5 corn plants at 4.0 fl oz or 292.3 ml/ha provided a slightly smaller increase in yield, +1.14 bushels per acre (71.6 kg/ha) and +0.90 bushels per acre (56.5 kg/ha) compared to combinations of these two Flg22 polypeptides with cellobiose.

Example 35 Combination of Synthetically Produced Flg22 (Syn01Flg22) and Fungicide

[0549] In an additional study, trials were conducted to investigate yields over large areas using a foliar application containing compositions with a Bt.4Q7Flg22 polypeptide and a synthetically derived polypeptide from Bt.4Q7Flg22 (Syn01Flg22) with the addition of a broad spectrum fungicide, STRATEGO YLD (10 .8% prothioconazole and 32.3% trifloxystrobin). STRATEGO YLD, which is a commercially available fungicide suitable for use as an early-season foliar application in corn, was applied as a foliar spray following the instructions for use at a working rate of 4.0 fl oz per acre (292.3 ml/hectare). Maize plants approximately V5 developmental stage were treated with foliar application using a foliar treatment composition containing Bt.4Q7Flg22 polypeptide and Syn0Flg22, a synthetic variant of the Syn01Flg22 polypeptide, in combination with STRATEGO YLD fungicide. Foliar treatments were applied to 2 corn hybrids (DEKALB hybrids: hybrid 1: DKC 52-61; hybrid 2: DKC 58-89) planted at 2 locations in Iowa. Corn crops were harvested (in bushels per acre) and recorded as the average yield (in bushels per acre) at both locations for both hybrids, as well as the average change in bushels per acre compared to corn plants cultivated from seed treated with the base agent. for seed treatment (ST) and foliar application of STRATEGOYLD fungicide only (Table 52).

Table 52. Corn yield after foliar application of the synthetic mutant Bt.4Q7Flg22 in combination with a fungicide

Foliage Treatment
(Concentration) Operating flow in fluid ounces per acre
(ml/hectare) Average yield in bushels per acre Average yield change in bushels per acre compared to fungicide control Fungicide STRATEGO YLD 4.0 fl oz per acre
(292.3 ml/hectare) 223.13 _ Fungicide STRATEGO YLD + Bt.4Q7Flg22
(SEQ ID NO: 226) (16.7 μM)
(track 3) 4.0 fl oz per acre
(292.3 ml/hectare)
4.0 fl oz per acre
(292.3 ml/hectare) 228.62 +5.49 Fungicide STRATEGO YLD + Syn01Flg22
(SEQ ID NO: 571) (16.7 μM)
(track 6) 4.0 fl oz per acre
(292.3 ml/hectare)
4.0 fl oz per acre
(292.3 ml/hectare) 228.96 +5.83

The basic seed treatment (ST) consisted of the fungicide EVERGOL + PONCHO/VOTIVO 500. The STRATEGO YLD fungicide was applied at a concentration and with a working consumption of the agent as recommended in the instructions for use of the drug.

[0550] Foliar application in stage V5 maize plants of Bt.4Q7Flg22 and Syn01Flg22 polypeptides in combination with the fungicide, STRATEGO YLD, at concentrations and operating rates as indicated in Table 5 above, resulted in a gain of more than +5 bushels per acre Foliar treatment with the Syn01Flg22 polypeptide resulted in a slightly greater increase in corn yield, +5.84 bushels per acre (366.6 kg/ha), compared to treatment of corn plants with the Bt. acre (345.2 kg/ha) compared to plants treated with STRATEGO YLD fungicide-only foliar treatment.

Example 36 Seed Treatment with Flg22 Polypeptides to Increase Maize Yield

[0551] In other studies, tests to study yields over large areas were carried out using a basic seed treatment consisting of the fungicide ® EVERGOL (7.18% propiconazole, 3.59% penflufen in combination with 5.74% metalaxyl) and PONCHO /VOTiVO 500 (a mixture of 40.3% insecticide clothianidin and 51.6% Bacillus firmus I-1582, a microbial agent) in combination with various Flg22 polypeptides. Seed treatments were applied to 3 corn hybrids (Beck's 4919V2, 5140HR and 5828YX) planted at 8 locations in the US Midwest (Indiana, Illinois and Iowa). Seed treatment compositions with Flg22 polypeptides were applied at a rate as described in Table 53 in fluid ounces per unit of corn or soybean seeds in total slurry containing Bt.4Q7Flg22 seed treatment base from Bacillus thuringinesis (composition 10) and Pa.Flg22 from Paenibacillus alvei (composition 11). The final concentration of the polypeptide in suspension for compositions 10 and 11 was 1 μm.

Table 53. Flg22 seed treatment compositions for testing in corn and soybeans

Composition The composition of the seed treatment Operating flow rate in fl oz/unit of corn or soy, or milliliters per unit (mL/unit) Composition 10 Bt.4Q7Flg22 (SEQ ID NO: 226) 40.0 μM, 11.6 mM sodium phosphate dibasic in combination with 4.2 mM citric acid monohydrate pH 5.6 0.14 fl oz/unit or
4.14 ml/unit Composition 11 Pa.Flg22 (SEQ ID NO: 293) 40.0 μM,
11.6 mM sodium phosphate dibasic in combination with 4.2 mM citric acid monohydrate pH 5.6 0.14 fl oz/unit or
4.14 ml/unit

[0552] Corn was harvested (in bushels per acre) and recorded as yield (in bushels per acre) at all 8 locations, averaging over all 3 hybrids. The average change in bushels per acre was compared to corn plants cultivated from seeds that were treated with a basic seed treatment (ST) only and recorded in Table 54.

Table 54: Treatment of maize seeds with Flg22 polypeptide increases yield

Foliage Treatment Operating expense funds Average yield (busels per acre) Average change in yield (in bushels per acre) compared to control ST Bt.4Q7Flg22
Bacillus thuringinesis
(SEQ ID NO: 226)
(track 10) 0.14 fl oz/unit or
4.14 ml/unit 179.72 +4.73 Pa.Flg22
Paenibacillus alvei
(SEQ ID NO: 293)
(track 11) 0.14 fl oz/unit or
4.14 ml/unit 182.24 +3.57

[0553] Treatment of corn seed with Bt.4Q7Flg22 (SEQ ID NO: 226) and Pa.Flg22 (SEQ ID NO: 293) polypeptides increased yield reported as the average of 3 corn hybrids at 8 locations in the US Midwest. The Bt.4Q7Flg22 polypeptide provided as a seed treatment provided an even greater yield advantage, or +4.73 bushels per acre (296.9 kg/ha) compared to control plants. Pa.Flg22, when applied as a seed treatant, also produced a yield increase of +3.57 bushels per acre (224 kg/ha) relative to corn plants grown from seed treated with the primary seed treater alone. Accordingly, both Flg22 polypeptides derived from bacteria of different species (Bacillus and Paenibacillus) provided a significant increase in yield when used as a seed treatment in corn.

Example 37 Use of Cellobiose Flg22 Polypeptides to Increase Maize Yield

[0554] Corn for large area trials was planted with seeds (DEKALB hybrids: DKC 52-61, DKC 58-89 and DKC 65-81) containing EVERGOL fungicide seed treatment (7.18% propiconazole, 3.59% penflufen in combination with 5.74% metalaxyl) in combination with PONCHO/VOTiVO 500 (mixture of insecticide clothianidin and microbial agent, Bacillus firmus 1582). Maize plants at approximately V5 developmental stage were treated with foliar applications with an agricultural composition containing Bt.4Q7Flg22 and synthetic Syn01Flg22 polypeptides with or without addition of cellobiose (320 mM). These foliar treatments were applied to 2 corn hybrids (DEKALB hybrids: hybrid 1: DKC 58-89; hybrid 2: DKC 65-81) planted at 2 locations in the US Midwest (Illinois) exposed to drought-like conditions after foliar application, at the stage of pollination during the development of corn. Maize plants were treated with foliar treatments with Bt.4Q7Flg22 and Syn01Flg22 at concentrations and operating rates as described in Table 48, with a non-ionic surfactant (Alligare Surface™ at a final concentration of 0.1% by volume of the spray tank volume) . Corn yield (in bushels per acre) was collected and reported as the average yield (in bushels per acre) at both locations for the 2 hybrids, as well as the average change in bushels per acre compared to the yield of corn plants treated with the primary treatment alone. seed (ST) and a non-ionic surfactant (Alligare Surface™ at a final concentration of 0.1% by volume of the spray tank volume) (Table 55).

Table 55 Combinations of Flg22 Polypeptides with Cellobiose - Maize

Foliage Treatment
(Concentration) Operating flow in fluid ounces per acre
(ml/hectare (ha) Average Yield (in bushels per acre) Average change in yield (busels per acre) compared to surfactant-treated control Bt.4Q7Flg22
(SEQ ID NO:226)
(16.7 µM) 4.0
(292.3 ml/ha) 96.46 +3.70 Bt.4Q7Flg22
(SEQ ID NO:226)
(16.7 μM) +
Cellobiose
(320 mm) 4.0
(292.3 ml/ha)
8.0
(584.6 ml/ha) 100.98 +8.22 Bt.4Q7Flg22
(SEQ ID NO:226)
(16.7 µM) 48.0
(3507.6 ml/ha) 119.37 +26.61 Syn01Flg22
(SEQ ID NO: 571)
(16.7 µM) 4.0
(292.3 ml/ha) 98.48 +5.72 Syn01Flg22
(SEQ ID NO: 571)
(16.7 µM) 0.4
(29.2 ml/ha) 102.36 +9.60 Syn01Flg22
(SEQ ID NO: 571)
(16.7 μM) +
Cellobiose
(320 mm) 0.4
(29.2 ml/ha)
8.0
(584.6 ml/ha) 108.24 +15.48

[0555] The use of foliar treatments with Bt.4Q7Flg22 (SEQ ID NO: 226) and synthetic variant Syn01Flg22 (SEQ ID NO: 571) resulted in a significant increase in yield in corn plants when combined in foliar treatments with cellobiose, a disaccharide, which is used as a secondary stabilizing agent for the Flg polypeptide and a base for delivery to the surface of the plant membrane. Bt.4Q7Flg22 polypeptide (16.7 µM) with cellobiose (320 mM) as a combined foliar spray applied at a spray rate of 4.0 fl oz per acre (Flg22) provided more than double yield gain, +8 increase .22 bushels per acre or approximately 516 kg/ha relative to control plants, compared to 4.0 fl oz per acre of the Bt.4Q7Flg22 polypeptide alone. Application of the Bt.4Q7Flg22 polypeptide without cellobiose resulted in an increase of +3.70 bushels per acre, or 232 kg/ha, relative to control plants grown from the surfactant-treated control. A similar increase in yield occurred in corn plants treated with Syn01Flg22 and the combination of Syn01Flg22 (16.7 µM) with cellobiose (320 nM) at an operating rate of 0.2 fl oz per acre, by +9.60 (602.6 kg/ha) and +15.48 (971.6 kg/ha), respectively, compared with the yield of surfactant-treated control plants. In addition, Bt.4Q7Flg22 polypeptide (16.7 μM) was applied as a foliar spray to V5-V7 developmental corn plants at three different application rates, 0.2, 2.0, and 24.0 fl oz per acre (14.6 ml/ha, 146.2 ml/ha and 1753.8 ml/ha). The Bt.4Q7Flg22 polypeptide, when applied at the highest operating rate, provided a substantially greater yield advantage, an increase in yield of nearly +27 bushels per acre (1694.6 kg/ha) relative to control plants. Overall, Bt.4Q7Flg22 and Syn01Flg22 synthetic variant provided protection from drought-like growth conditions at a critical stage of plant development (i.e. pollination), resulting in increased yields for all combinations of Bt.4Q7Flg22, Syn01Flg22 and cellobiose used in as a means for foliar application.

[0556] In another study, seed treatment with Flg22 polypeptides and combinations of Flg22 polypeptides with cellobiose provided an overall increase in yield in field trials recorded as the mean of four replicate trials (Table 56). Seed treatment was performed on a corn hybrid (Beck's 5828YX) planted at 1 location in the US Midwest (Columbia). The Flg22 seed treatment formulations were applied as described in Table 56 at 0.14 fl oz per unit of corn seed in total slurry containing base seed treatment. The final concentration of Flg22 polypeptides in suspension was standardized to 1 μM per seed. The same final concentration of cellobiose was used as in combination products with Flg22 polypeptides of 1.0 mM per seed. Record the average yield in bushels per acre and the average increase in yield in bushels per acre compared to the untreated control (column 1) and with Bt.4Q7Flg22 (SEQ ID NO:226) (column 2) for corn cultivated from seeds that were treated with combined agents with the Flg22 polypeptide as described below in Table 56.

Table 56. Seed Treatment Combinations with Flg22 Polypeptides and Variant Flg22 Polypeptides with Cellobiose - Maize

Foliage Treatment (Concentration) Average bushels per acre yield (Average change in bushels per acre from untreated control) Mean change in bushels per acre compared to untreated control Average change in bushels per acre compared to Bt.4Q7Flg22; SEQ ID NO:226 Basic control seed treatment 28.00 - -1.60 Bt.4Q7Flg22 in concentration
1.0 µM
(SEQ ID NO:226) 29.60 +1.60 - Syn01Flg22 in concentration
1.0 µM
(SEQ ID NO: 571) 39.58 + 11.58 +9.98 Syn03Flg22 in concentration
1.0 µM
(SEQ ID NO: 300) 35.17 +7.17 +5.57 Pa.Flg22
Paenibacillus alvei
at a concentration of 1.0 µM
(SEQ ID NO: 293) 39.04 +11.04 +9.44 La.Flg22
Lysinibacillus in concentration
1.0 µM
(SEQ ID NO: 574) 37.13 +9.13 +7.53 Flg22-B2
Bacillus at a concentration of 1.0 μM
(SEQ ID NO: 295) 36.79 +8.79 +7.19 Combination of Flg22 Syn01Flg22 (SEQ ID NO: 571) + Flg22-B2 (SEQ ID NO: 295) + At.Flg22-B4 (SEQ ID NO: 300), each
at a concentration of 0.33 μM 45.39 +17.39 +15.79 Cellobiose 1 mM 39.66 +11.67 +10.07 Bt.4Q7Flg22
(SEQ ID NO:226) at a concentration of 1.0 μM +
Cellobiose 1 mM 36.22 +8.22 +6.62 Bt.4Q7Flg22
(SEQ ID NO:226) at a concentration of 0.25 μM 47.06 +19.07 +17.47 Bt.4Q7Flg22
(SEQ ID NO:226) at a concentration of 0.25 μM +
Cellobiose 1 mM 40.62 +12.63 +11.02 Syn01Flg22 (SEQ ID NO: 571) at concentration
0.25 µM 32.65 +4.66 +3.06 Bt.4Q7Flg22
(SEQ ID NO: 571) at a concentration of 0.25 μM +
Cellobiose
1 mM 31.03 +3.03 +1.43

Example 38 Application of Flg22 with Cellobiose Supplement to Soybean at Stage V4-V6

Increased Yields - Tests to investigate yields over large areas

[0557] Soybeans for testing in large areas were planted with uncoated soybean seeds. Soybean seeds were planted at a depth of 1.5-2 inches (approximately 5 cm) to ensure normal root development. Soybeans were planted in 12.5' (3.8 m) plots, averaging 150,500 plants per acre, with rows 30 inches (0.8 m) wide and seed spacing to accommodate 7-8 seeds per foot ( 30 cm).

[0558] Soybeans were treated with agricultural compositions containing agriculturally effective amounts of compositions Bt.4Q7Flg22 (SEQ ID NO: 226), Syn01Flg22 (SEQ ID NO: 571) and Flg22 from Aneurinbacillus thermoaerophilus, At.Flg22-B4 (SEQ ID NO: 300) . This treatment with Flg22 polypeptides was performed by foliar spraying at the operating rate (in fluid ounces per acre, or ml/ha) shown in Table 57 on soybeans cultivated at five locations in the US Midwest (participating sites: Iowa and Illinois). Soybean plants were treated with foliar treatments containing Bt.4Q7Flg22 (SEQ ID NO: 226); Syn01Flg22 (SEQ ID NO: 571) and At.Flg22-B4 (SEQ ID NO: 300) approximately V4-V6 with a non-ionic surfactant to aid spreading and absorption of agents (Alligare Surface™ at 0.1 final % by volume of the sprayer tank volume). 3 soybean varieties (Asgrow: AG2733, AG3536 and AG4034) were harvested from plants treated with Flg22 formulations. Soybean yield was also recorded as the change in yield in bushels per acre compared to control soybean plants that were treated with a nonionic surfactant (Alligare Surface™ treatment only at a final concentration of 0.1% (v/v) (Table 57).

[0559] Foliar application of Bt.4Q7Flg22 and Syn01Flg22 polypeptides was also performed in combination with cellobiose as an additive, and the effect of Flg22 polypeptides in combination with cellobiose additive on yield increase was investigated. Cellobiose is a disaccharide of glucose and a building block for the cellulose polymer. Chemically, it is glucose-beta-1-4-glucose, a reducing sugar that consists of two β-glucose molecules linked by a β(1-4) bond. Cellobiose is obtained by the decomposition of cellulose or lichenin, and when hydrolyzed, it gives glucose. The cellobiose additive in combination with Bt.4Q7Flg22 provided an increase in the activity of reactive oxygen species (ROS) in soybeans. 3 soybean varieties (Asgrow: AG2733, AG3536 and AG4034) were harvested from plants treated with Flg22 formulations, with or without added cellobiose additive, and recorded as average yields (in bushels per acre) for all 3 varieties at different locations. Soybean yield was also recorded as change in yield in bushels per acre compared to control soybean plants treated with a non-ionic surfactant (Alligare Surface™ treatment only at a final concentration of 0.1% by volume) (Table 57).

Table 57 Soybean Yields in Foliar Treatment with Diverse Flg22 Polypeptides

Product concentration Application rate in fluid ounces per acre (ml/hectare (ha)) Average number in bushels per acre
(5 locations) Change in bushels per acre from surfactant-treated control Separate nonionic surfactant 0.1% of spray volume 61.36 - Bt.4Q7Flg22 (SEQ ID NO: 226)
16.7 µM,
Composition 1 4.0 fl oz per acre
(292.3 ml/ha) 62.85 +1.49 Bt.4Q7Flg22 (SEQ ID NO: 226)
16.7 µM,
Composition 2 4.0 fl oz per acre
(292.3 ml/ha) 64.72 +1.56 Bt.4Q7Flg22 (SEQ ID NO: 226)
16.7 µM,
Composition 3 4.0 fl oz per acre
(292.3 ml/ha) 63.87 +2.51 Bt.4Q7Flg22 (SEQ ID NO: 226): 16.7 μM,
+ Cellobiose: 320 mM
Composition 4 4.0 fl. oz. per acre (292.3 ml/ha), 8.0 fl. oz. per acre
(584.6 ml/ha) 63.15 +1.79 Bt.4Q7Flg22 (SEQ ID NO: 226)
16.7 µM,
Composition 5 48.0 fl oz per acre
(3507.6 ml/ha) 62.64 +1.28 Syn01Flg22 (SEQ ID NO: 571)
16.7 µM,
Composition 6 4.0 fl oz per acre
(292.3 ml/ha) 63.12 +1.76 Syn01Flg22 (SEQ ID NO: 571)
16.7 µM,
Composition 7 0.4 fl oz per acre
(29.2 ml/ha) 62.88 +1.52 Syn01Flg22 (SEQ ID NO: 571)
16.7 µM,
+ Cellobiose (320 mM)
Composition 8 0.4 fl oz per acre
(29.2 ml/ha),
8.0 (584.6 ml/ha) 63.92 +2.56 At.Flg22-B4 (SEQ ID NO: 300)
16.7 µM,
Composition 9 4.0 fl oz per acre
(292.3 ml/ha) 63.66 +2.30

[0560] Treatment of foliage with various Flg22, Bt.4Q7Flg22 polypeptides; Syn01Flg22 and At.Flg22-B4 (compositions 1-9) in all cases resulted in yield advantages when applied to V4-V6 developmental soybeans compared to soybean controls treated by foliar application of surfactant alone. Bt.4Q7Flg22 Foliar Treatment (Formulation 3) at 4.0 fl oz per acre resulted in +2.51 bushels per acre (168.8 kg/ha) increase over control plants (surfactant only) . Syn01Flg22 polypeptide (Composition 6) applied to soybean plants as a foliar treatment at a rate of 4.0 fl oz per acre resulted in a yield increase of +1.76 bushels per acre (118.4 kg/ha) compared to surfactant-only treated control plants. Syn01Flg22 (Formulation 7) and Syn01Flg22 with Cellobiose (320 nM) (Formulation 8), which were applied to soybean plants at a lower application rate of 0.2 fl oz per acre, resulted in an increase of +1 bushel per acre with the addition of a cellobiose additive or an overall increase in yield of +2.56 bushels per acre (172.2 kg/ha) relative to control plants. The At.Flg22-B4 polypeptide (composition 9) when applied to soybean (V4-V6) also resulted in a yield advantage of +2.3 bushels per acre (154.7 kg/ha) compared to control plants or a yield advantage of more than 3 .5 bushels per acre (235.4 kg/ha) compared to plants treated with non-ionic surfactant alone.

[0561] In yet another study, seed treatments with Flg22 polypeptides and combinations of Flg22 polypeptides with cellobiose were used as seed treatments in soybean, resulting in an overall yield increase in field trials reported as the average of four replicate trials (Table 58). Seed treatments were applied to 1 soybean hybrid (cultivar) planted at 1 location in the US Midwest (Columbia, MO). The Flg22 seed treatment formulations were applied as described in Table 58 at a rate of 0.14 fl oz per unit of soybean seed in total slurry and applied to soybean seeds coated with a base seed treatment consisting of Poncho VOTiVO 600 FS and Evergol Energy . The operating rate for all seed treatments was the same at 0.14 fl oz per acre, or 4.14 ml/unit. The final concentration of Flg22 polypeptides in suspension was standardized to be 1 μM per seed. The same final concentration of 1.0 mM per seed was used for cellobiose used in combination products with Flg22 polypeptides. Four replicate pads for each seed treatment option were placed in a random location. The average yield in bushels per acre and the average change in bushels per acre compared to control plants treated with base seed treatment alone are shown in Table 58. The most significant increase in yield was observed for Bt.4Q7Flg22 (SEQ ID NO: 226) and Syn01Flg22 (SEQ ID NO: 571) when applied as a soybean seed treatment at a final concentration of 1.0 μM Flg22 polypeptides, resulting in corresponding increases in average yield of +5.11 (343.7 kg/ha) and + 9.92 (667.1 kg/ha) relative to the yield of soybeans treated with the main seed treatment.

Table 58. Seed Treatment Combinations with Flg22 Polypeptides and Flg22 Polypeptide Variants with Cellobiose - Soybean

Foliage Treatment
(Concentration) Average yield in bushels per acre (Average change in bushels per acre from untreated control) Mean change in bushels per acre compared to untreated control Control basic means for seed treatment 41.11 - Bt.4Q7Flg22 at a concentration of 1.0 µM
(SEQ ID NO:226) 46.22 +5.11 Syn01Flg22 at a concentration of 1.0 µM
(SEQ ID NO: 571) 51.09 +9.92 Syn03Flg22 at a concentration of 1.0 µM
(SEQ ID NO: 573) 43.61 +2.50 Pa.Flg22
Paenibacillus alvei
at a concentration of 1.0 µM
(SEQ ID NO: 293) 41.39 +0.28 An,.Flg22
Aneurillusbacillus at a concentration of 1.0 µM
(SEQ ID NO: 300) 46.01 +4.90 Bacillus species Flg22 (Combination of Flg22 sequences)
Syn01Flg22 (SEQ ID NO: 571, Flg22-B2 (SEQ ID NO: 295) and Flg22-B4 (SEQ ID NO: 300), each at a concentration of 0.33 μM 44.43 +3.32 Cellobiose
1 mM 43.98 +2.87 Bt.4Q7Flg22
(SEQ ID NO:226) at a concentration of 1.0 μM +
Cellobiose
1 mM 43.40 +2.29 Bt.4Q7Flg22
(SEQ ID NO:226) at a concentration of 0.25 μM 43.80 +2.69 Bt.4Q7Flg22
(SEQ ID NO:226) at a concentration of 0.25 μM +
Cellobiose
1 mM 43.52 +2.41

Example 39 Application of RHPP to Soybean at Stage V5 Increased Yield

[0562] Corn for large area trials was planted with seeds (DEKALB hybrids: DKC 52-61, DKC 58-89 and DKC 65-81) containing EVERGOL fungicide seed treatment (7.18% propiconazole, 3.59% penflufen in combination with 5.74% metalaxyl) in combination with PONCHO/VOTiVO 500 (mixture of insecticide clothianidin and microbial agent, Bacillus firmus 1582). Maize plants, approximately at the V5 developmental stage, were treated by foliar application of an agricultural composition containing the Gm.RHPP polypeptide (SEQ ID NO: 600). The Gm.RHPP polypeptide formulation (Table 59) was applied to corn hybrids at an application rate of 8.0 fl oz per acre (584.6 ml/ha) with 0.1% by volume (of the spray tank volume) of a non-ionic surfactant substances (Alligare Surface™). A total of 6 locations were tested in the US Midwest (Illinois, Indiana, Iowa), with 1-2 hybrids per location and 3 replica sites per hybrid. Corn was harvested (in bushels per acre) and recorded as an average yield (in bushels per acre). The mean change in bushels per acre was compared with the yield of plants cultivated from the surfactant-treated control and reported as the combined average yield (in bushels per acre) for 6 locations (a total of 11 replicate sites) and as the total change in bushels per acre compared to control plants. The results are shown in Table 59.

Table 59: RHPP Foliar Treatment - Increased Maize Yield

Foliar treatment, concentration Application consumption Average yield in bushels per acre (Average change in bushels per acre from surfactant-only control) Surfactant treated control (control) - 206.15 Gm.RHPP (SEQ ID: 600)
100 µM, preservative PROXEL BC: 330.7 µM; 50.1 μM (CMIT); 21.71 µM (MIT) 8.0 fl oz per acre
(584.6 ml/ha) 209.67
(+3.52; 64% success rate)

[0563] Treatment of plant foliage with the Gm.RHPP polypeptide resulted in increased yield in corn compared to plants that were treated with the surfactant alone. The average combined yield at 6 locations for corn plants treated with the Gm.RHPP polypeptide foliar treatment was slightly above 209 bushels per acre, while the control plants had 206 bushels per acre. Yields of Gm.RHPP-treated plants increased by 3.52 bushels per acre, or 220.9 kg/ha, compared to corn control plants (Table 59).

Example 40: RHPP polypeptide increases the number of pods in soybean

[0564] Soybean plants (MorSoy cultivar) were cultivated from seeds by planting 2 seeds per container in a controlled growing room under conditions of approximately 300 µmol ^-2 s ^-1 (photons of light) in a daily light-dark cycle 13/ 11 and a temperature range of 21°C during the day/15°C at night, up to the developmental stage V4. The plants were then placed under long day conditions including a 16/8 light cycle and a temperature of 21-26°C to encourage early flowering and accelerate progression to the reproductive (R) growth stage. When soybean plants reached the R1 developmental stage, they were treated with a foliar application containing the Gm.RHPP polypeptide (SEQ ID NO: 600) at a final concentration of 300 nM with 0.10% non-ionic surfactant (NIS90:10; Precision Laboratories, LLC). Soybean plants were treated with the Gm.RHPP control formulation and the control nonionic surfactant separately. Control treatment with both Gm.RHPP and non-ionic surfactant was performed on 18 plants for each treatment. Each plant was sprayed with six equidistant sprays from above from a distance of approximately 15 cm to completely cover the foliage. After application of the agents, the R1 stage soybean plants were returned to the controlled environment growing room. After 17 days, the plants were treated with another foliar treatment with a formulation including the Gm.RHPP polypeptide and a nonionic surfactant, as well as the nonionic surfactant alone. Soybean pods longer than 1 mm were counted on plants 31 days after the first foliar spray treatment. Record the average number of pods per plant and the standard deviation from the overall average (table 60). A p-value (p<0.05 for significance) was calculated based on comparison using a paired t-test for the number of pods in plants that were treated with Gm.RHPP agents or a control non-ionic surfactant.

Table 60. Number of pods in greenhouse cultivated soybeans 31 days after foliar treatment with RHPP

Product concentration Counted number of pods
(STDEV) p-value Nonionic surfactant (NIS90:10 control)
0.01% (by volume) 1.07
(+0.44) 0.0116 Gm.RHPP (SEQ ID: 591) + Surfactant
300 nM 2.00
(+1.22)

*p-value<0.05 corresponds to statistical significance

[0565] Foliar application of the Gm.RHPP polypeptide at an early reproductive stage (R1) in soybean plants resulted in approximately doubling the number of pods counted compared to plants that were treated with a control nonionic surfactant.

Example 41 Flg22 and RHPP Polypeptides Increase Yield in Tomato and Pepper

[0566] A foliar treatment with Bt.4Q7Flg22 (SEQ ID NO: 226) and Gm.RHPP (SEQ ID NO: 600) was performed as an exogenous spray at the pre-flowering stage and used to increase yield in tomato and jalapeno peppers.

[0567] Small areas were set up to mimic commercial tomato growing conditions. Cultivation of tomato cv. Roma plants began from seedlings in the greenhouse for 45 days prior to field planting in 2 raised beds with 2 feet (0.6 meters) between plants, averaging 30 plants per bed. Tomato seedlings were planted in the soil to a depth of three inches when the soil temperature reached 15.6°C. Tomato plants were grown in raised beds covered with black plastic mulch. Plants were cultivated using drip irrigation and fertilizer (80 lbs or 36.3 kg nitrogen; 100 lbs (45.4 kg) phosphate and 100 lbs (45.4 kg) potash or potassium) applied according to grower recommendations. throughout the growing season to ensure optimum plant growth and yield. Small raised areas were arranged to mimic the planting density used by commercial growers, who typically plant 2600-5800 plants per acre in a single row with 45.7-76.2 cm between plants in the row and centers 1.5- 2 min. [Orzolek et al., “Agricultural Alternatives: Tomato Production.” University Park: Penn State Extension, 2016].

[0568] Foliar treatments with Bt.4Q7Flg22 and Gm.RHPP were applied to tomato plants immediately at the early flowering stage (first flowers). The Bt.4Q7Flg22 polypeptide foliar treatment was applied at a working rate of 4.0 fl oz per acre (292.3 ml/hectare) and the Gm.RHPP polypeptide foliar treatment was applied at a working rate of 3.2 fl oz per acre (234 ml/hectare) tomato plants in 10 gallons of water per acre with 0.1% v/v non-ionic surfactant (Alligare™ Surface). Bt.4Q7Flg22 and Gm.RHPP treated plants were compared to control plants that were not treated with foliar treatment. Plants were treated in replicates (with replicates) of 6 plants, three replicates per treatment. The effect of foliar treatments on tomato yield was determined and the results normalized to the non-sprayed control were recorded. The average fruit weight per tomato plant was recorded in Table 61 as the combined average of 2 separate crops and the average percent change in fruit weight compared to the no-spray control.

Table 61

Foliar Treatment Concentration Average fruit weight (grams) per plant Percentage change in fruit weight compared to non-spray control Control without spraying 1369.9 _ Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 3) 1487.8 +8.61% Gm.RHPP (SEQ ID NO: 591) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 1397.1 +1.99%

[0569] The use of a foliar treatment with the Bt.4Q7 Flg22 polypeptide at a concentration of 16.7 μM and at an operating rate of 4.0 fl oz per acre (292.3 ml/hectare) resulted in an overall increase in average fruit weight per plant, recorded as total weight in grams, and +8.61% fruit weight change compared to control without spraying. The Gm.RHPP polypeptide, when applied at a concentration of 100 μM and at an application rate of 3.2 fl oz per acre (234 ml/hectare), also resulted in an overall increase in yield in terms of average fruit weight (in grams) per plant and a change in fruit weight of almost +2% compared to control without spraying.

[0570] In another study, foliar treatments with Bt.4Q7Flg22 (SEQ ID NO: 226) and Gm.RHPP (SEQ ID NO: 600) polypeptides were applied to jalapeno pepper (Capsicum) plants at an early flowering stage (first flowers). Small areas were set up to mimic commercial jalapeno growing conditions. Pepper plants were cultivated for 12 weeks in a controlled growing room and then planted outdoors in 2 raised beds covered with high water retention black plastic mulch in soil pH 5.8-6.6. Jalapeno pepper plants were planted 14-16 inches (38 cm) apart, with 16-24 inches (50 cm) between plants, approximately 25 plants per bed. Plants were cultivated using drip irrigation and fertilizer applied according to grower recommendations throughout the growing season to provide optimal conditions for plant growth. The raised areas were arranged to mimic the planting density used by commercial growers, who typically plant approximately plants per acre (5,000-6,500 plants per acre, or 12,355-16,062 plants per hectare) in double rows spaced 35.6 -45.7 cm in beds centered 5.0-6.5 feet (1.52-1.98 meters) (Orzolek et al., “Agricultural Alternatives: Pepper Production.” University Park: Penn State Extension, 2010).

[0571] Foliar treatments with Bt.4Q7Flg22 and Gm polypeptides. RHPP was applied to jalapeno peppers at a working rate of 2.0 fl oz per acre (146.2 ml/hectare) and 4.0 fl oz per acre (292.3 ml/hectare) for Bt.Flg22, and oz per acre (234 ml/hectare) for Gm.RHPP polypeptide, in a spray volume of 10 gallons of water per acre with 0.1% v/v non-ionic surfactant (Alligare™ Surface). 6 plant replicates were treated, with three replicates per treatment. Replicates with an average yield per plant, 50% above or 50% below the median yield for the specified trial were excluded as outliers. Foliar treatments with Bt.4Q7Flg22 and Gm.RHPP polypeptide applied to jalapeno pepper plants were compared to plants sprayed with 10 gallons per acre of water with 0.1% v/v non-ionic surfactant (Alligare™ Surface) alone .

[0572] Effects of Bt.4Q7Flg22 and Gm polypeptides. The RHPP used as a foliar spray on pepper yield was determined from two separately harvested using the single harvest method. The number of peppers and above ground biomass per plant were normalized to the yield and biomass of control pepper plants that were treated with surfactant alone (Table 62).

Table 62

Foliar treatment and consumption Average fruit weight (grams) per plant Percent change in fetal weight compared to surfactant-treated control Surfactant treated control (Alligare™ Surface; 0.1% v/v spray) 123.7 _ Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM
1.67 mM sodium phosphate buffer, pH 5.7, preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 3)
2 fl oz/acre 184.1 +49% Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM
1.67 mM sodium phosphate buffer, pH 5.7, preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 3)
4 fl oz/acre 173.7 +40% Gm.RHPP (SEQ ID NO: 591) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
3.2 fl oz/acre 156.6 +27%

[0573] The Bt.4Q7Flg22 polypeptide, when applied as a foliar spray to pre-flowering jalapeno pepper plants, provided a significant increase in average fruit weight per plant, +49% for an application of 2 fl oz per acre (146.2 ml/hectare) and +40% for 4 fl. oz. per acre (292.3 ml/ha) application, compared to surfactant-only treated control plants. Treatment with the Gm.RHPP polypeptide, also as a pre-flower foliar spray, also resulted in an increase in average fruit weight per jalapeno pepper plant, with an increase in pepper weight of +27% per plant compared to pepper fruits harvested from treated only surfactant of control plants.

Example 42 Pumpkin Application - Increased Yield

[0574] A foliar treatment containing a Bt.4Q7Flg22 or Gm.RHPP polypeptide was applied exogenously as a foliar treatment for gourds in the first flowering stage. Foliar treatments with Bt.4Q7Flg22 and Gm.RHPP polypeptides were applied to squash plants at an operating rate of 2.0 fl oz per acre (146.2 ml/hectare) or 3.2 fl oz per acre (234 ml/hectare) , respectively, in a spray volume of 10 gallons of water per acre with 0.1% by volume of a non-ionic surfactant (Alligare™ 90). The yield of polypeptide-treated plants was compared to that of surfactant-only control plants using three replicates per treatment. Yields for foliar treated plants that were treated with Bt.4Q7Flg22 or Gm.RHPP polypeptide are recorded in Table 63 as the average weight (in grams) of gourd fruit per plant for two crops per replicate and expressed as a percentage change from control plants. Replicates with an average yield per plant 50% above or 50% below the median yield for the test were excluded as outliers.

[0575] Pumpkin plants were cultivated in sandy loam soil as follows. In plastic-covered beds 0.76 m wide, holes were made 2.5 cm in size, arranged in two rows in each bed at a distance of 0.46 m in each row. The rows in the garden were arranged in a checkerboard pattern. The beds were located at a distance of 1.2 m from one another. 3 pumpkin seeds were sown in each hole and thinned out 14 days after planting to leave 1 plant per hole. Drip irrigation pipes were laid in the center of each bed, and the plants were watered as needed.

Table 63 Foliar Treatment with a Gm.RHPP Polypeptide Compound to Increase Yield in Pumpkin

Foliar treatment and consumption Average mass of pumpkin fruits (in grams) per plant Percent change in fetal weight compared to surfactant-only treated control Surfactant treated control (Alligare™ 90; 0.1% v/v spray) 716.7 _ Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM, 1.67 mM sodium phosphate buffer, pH 5.7, preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 3)
2 fl oz/acre 748.4 +4.4% Gm.RHPP (SEQ ID NO: 591) 100 μM
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
3.2 fl oz/acre 748.4 +4.4%

[0576] Foliar treatment with both the Bt.4Q7Flg22 polypeptide and Gm.RHPP in pre-flowering pumpkin plants resulted in an increase in harvested pumpkin fruit weight by an average of 31.7 grams per plant, or a +4.4% change in fruit weight by compared to surfactant-only treated control plants (Table 63).

Example 43 Flg22 polypeptide reduces the severity of white leaf spot in kale

[0577] In a fall season replicate test on kale in the Midwest (Columbia, Missouri), very humid and warm growth conditions resulted in the development of kale leaf spot, typically caused by Cercospora brassicicola. Infected kale plants have not previously received foliar treatments to prevent fungal disease. To assess the severity of the disease, scoring criteria were established (on a scale of 1 to 5), where score 1=healthy plant with three or less white spots caused by the fungus, 2=plant with 4 or more spots, part of the leaves of which is affected by the disease, 3=on most of the leaves are symptomatic and up to 1 leaf has fallen off due to the disease, 4=most of the leaves are showing symptoms and 2-3 leaves have fallen off due to the disease; and 5=most of the leaves are symptomatic and four or more leaves have fallen due to the disease. One person evaluated all plants at one test site, after which plants receiving different treatments were evenly distributed by disease score in Table 64 for 6 replication blocks of 6 plants per treatment (total = 36 plants per treatment). To test Bt.4Q7Flg22 (SEQ ID NO: 226) for improvement in disease symptoms in kale, a foliar spray was applied at a flow rate in vehicle volume (water) of 10 gal/acre as shown in Table 64, from 0.1% to volume of nonionic surfactant (Alligare™ Surface). Three weeks after the foliage treatment, the disease severity of the plants was assessed using the same criteria. The disease score change was calculated for each plant and the average disease score change for each treatment was determined. Plants were harvested four days after disease severity was assessed and yield was measured as plant weight (in grams). Outliers for weight, either 50% below or 50% above the median weight per test, were excluded from the data set.

Table 64 Treatment of kale with foliar agents to mitigate white leaf spot.

Foliage Treatment (Concentration) Operating flow in fluid ounces per acre
(ml/hectare) Change in Yield (Average Plant Weight in Grams) Relative to Control (%) Mean change in disease score Control, surfactant alone n/a 14.6
(100%) 0.6 point improvement Bt.4Q7Flg22 (SEQ ID NO: 226) (100 μM), 1.67 mM sodium phosphate buffer, pH 5.7, preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 12.0 fl oz per acre (876.9 ml/hectare) 15.1
(103%) 1.1 point improvement Liquid fungicide with copper Recommended flow rate (54.45 fl oz/acre) 11.5
(79%) 1.1 point improvement Liquid fungicide with copper
+
Bt.4Q7Flg22
(SEQ ID NO: 226)
(100 μM), 1.67 mM sodium phosphate buffer, pH 5.7, PROXEL BC preservative: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) Recommended flow rate (54.45 fl oz/acre)
+
12.0 fl oz per acre (876.9 ml/hectare) 12.4
(85%) 0.8 point improvement

[0578] Treatment of leaves of infected kale plants with Bt.4Q7Flg22 formulation (SEQ ID NO: 226) resulted in improved yield and disease symptoms relative to control (Table 64). With an average plant weight of 14.6 g in the untreated control, plants treated with Bt.4Q7Flg22 foliar application had an average plant weight of 15.1 g and had an average improvement in disease scores of 0.5 points relative to the control. The application of the fungicide with copper improved disease rates in plants to the same extent as Bt.4Q7Flg22, but reduced the yield by 21% (11.5 g) compared to the control. The combined fungicide treatment with copper and Bt.4Q7Flg22 increased yield to 12.4 g per plant, but overall, Bt.4Q7Flg22 alone provided the maximum yield and plant health benefit in this trial. Thus, Flg22 polypeptides can be used to slow the progression of fungal infection in vegetable crops and increase yields under stressful cultivation conditions.

Example 44 ROS Screening Assays to Determine Compatibility of Flg22 Polypeptide with Seed Treatments

[0579] Seed treatments were tested for compatibility with the generation of apoplastic reactive oxygen species (ROS) in corn petiole tissues. Various commercially available seed treatments were tested for compatibility with the Flg22 polypeptide (Bt.4Q7Flg22; SEQ ID NO: 226), which has been shown to increase yield when used alone as a corn seed treatment. ROS activity assays were performed on 5828 YX hybrid corn petiole samples as described in Example 15, except that relative light units (RLU) were recorded using a SpectraMax L luminometer (integration 0.5 s; intervals 2.0 min) over the period time 40 ^{min .} Bacillus pumilis), ILEVO (48.4% fluopyram) and PONCHO/VOTiVO (mixture of 40.3% clothianidin and microbial agent, Bacillus firmus I-1582) and tested for the presence of an ROS response in corn petioles. All three seed treatments, as described, were applied at the operating rate per seed as recommended in the individual instructions for use of each seed treatment. A standard curve was built for varying concentrations of the Bt.4Q7Flg22 polypeptide to obtain a logarithmic correlation between RLU and Flg22 concentration with R2=0.90. RLU values are the average of 4 individual measurements (4 treated wells per plate); the total increase in ROS (RLU) (fold increase relative to the background) is given in parentheses (table 65).

Table 65. Compatibility study of seed treatments with Flg22 polypeptide using ROS assay

Seed treatment agent Background 1 μM Bt.4Q7Flg22
(SEQ ID NO: 226) (concentrated ST)
(Magnification factor (X) relative to background) 1 µM Bt.4Q7Flg22
(SEQ ID NO: 226)
(ST at 1:10 dilution)
(Magnification factor (X) relative to background) PPST 2030 15952.2 109313.7
(6.9X) 96129.9
(6.0X) ILeVO 84716.9 548686.2
(6.5X) 382365.1
(4.5X) PONCHO/VOTiVO 17379.7 120788.9
(6.9X) 267720.2
(15.4X)

[0580] ROS production as assessed based on RLU values increased when 1 μM Bt.4Q7Flg22 was added in combination with each of the seed treatments as described in Table 65. ROS production (RLU values) at a 1:10 dilution of seed treatments ( ST) supplemented with 1 μM Bt.4Q7Flg22 also increased compared to background RLU for seed treatment alone or in the absence of Bt.4Q7Flg22 polypeptide. Diluted PONCHO/VOTiVO seed treatment in combination with 1 µM Bt.4Q7Flg22 provided more than 15X increase over background, or 2.2X increase over treatment with undiluted PONCHO/VOTiVO per seed, as recommended in the leaflet on the use of the drug. Accordingly, the Flg22 polypeptide can be detected using a ROS assay in combination with a standard base seed treatment at the stated rate for said agent. When such Flg22 polypeptides are combined with certain seed treatments, adjustment of either the polypeptide concentration or the seed treatment concentration may be considered to provide an optimal ROS response in the plant. These results demonstrate the activity of Flg22 polypeptides in plants in the presence of other complex seed treatments on the market today.

Example 45 Combinations of Flg22 and FlgII-28 Peptides to Increase ROS Activity in Tomato

[0581] In a separate study, Flg22 and FlgII-28 polypeptides derived from different regions of the flagellin protein were tested individually and in combination for response compatibility in tomato leaves. Although both Flg22 and FlgII-28 are both microbial-associated molecular patterns (MPMPs), they can be separately recognized by flagellin-sensitive receptor 2 (FLS2) and flagellin-sensitive receptor 3 (FLS3), respectively (Hind et al., 2016 ; Nature Plants 2:16128), and interactions may differ between plant species. A number of Flg22 polypeptides (Bt.4Q7Flg22, SEQ ID NO: 226; Bt.4Q7Flg22-Syn01, SEQ ID NO: 571; and Ec.Flg22, SEQ ID NO: 526) were compared using tomato ROS activity assays with multiple FlgII- 28 (Ps.tomatoFlgII-28, SEQ ID NO:751; A.sp.FlgII-28, SEQ ID NO:375).

[0582] 4 week old tomato plants were stripped of leaves and using a cork drill, 4 mm disks were cut from the leaves. Each disk was cut in half with a razor blade, after which each half of the disk was placed on the surface of 150 μl of water in the well of a 96-well plate and left overnight. The next day, just prior to polypeptide treatment, water was removed from all wells. Flg polypeptides as described in Table 66 were added to water to final concentrations of 5 nM (Table 67) and 100 nM (Table 68) in Luminol/HRP solution prior to addition to each treatment well. To maintain activity, the polypeptides were stored in small aliquots to avoid repeated freezing and thawing. All dilutions to obtain working concentrations were carried out in ultrapure water. Polypeptide solutions were stored at -20°C for short term storage or -80°C for long term storage. RLU values and relative ROS activity (Tables 67, 68) were recorded as the average of 4 measurements. ROS activity assays were performed using the methods previously described in Example 15, except that relative light units (RLU) were recorded using a SpectraMax L luminometer (integration 0.5 s; intervals 2.0 min) over a time period of 40 minutes .

Table 66 Flg22 and FlgII-28 polypeptides from various sources

Description of the Flg polypeptide Amino acid sequence length Subsequence Bt.4Q7Flg22
Bacillus thuringiensis
(SEQ ID NO: 226) 22 DRLSSGKRINSASDDAAGLAIA Syn01Flg22,
Synthetic
(SEQ ID NO: 571) 22 DRLSSGKRINSAKDDAAGLAIA Ps.tomato FlgII-28
Pseudomonas syringae, patovar tomato DC3000
(SEQ ID NO: 751) 28 ESTNILQRMRELAVQSRNDSNSATDREA Ec.Flg22
Escherichia coli
(J26)
(SEQ ID NO: 526) 22 ERLSSGLRINSAKDDAAGQAIA A.sp.FlgII-28
Aneurinibacillus sp.XH2
(SEQ ID NO: 300) 28 EIHEMLQRMRELAVQAANGTYSDKDKKA

Table 67. Comparison of ROS activity for Flg22 and FlgII-28 polypeptides in tomato leaf tissue

Means with a polypeptide Mean RLU (5 nM Flg polypeptide)
(Magnification factor (X) relative to processing Bt.4Q7Flg22) Negative control (water) 24423
(0.7X) Bt.4Q7Flg22
Bacillus thuringiensis
(SEQ ID NO: 226) 33118
(-) Bt.4Q7Flg22-Syn01,
Synthetic
(SEQ ID NO: 571) 116751
(3.5X) Ps.tomatoFlgII-28
Pseudomonas syringae, patovar tomato
(SEQ ID NO: 751) 1019995
(30.8X) Ec.Flg22
Escherichia coli
(SEQ ID NO: 526) 426307
(12.9X) Aneurinibacillus.sp.FlgII-28
(SEQ ID NO: 375) 32980
(1.0X)

Table 68. FlgII-28 polypeptides from the gram-negative bacterium Pseudomonas syringae, patovar Tomato DC3000, and the gram-positive bacterium Aneurinibacillus sp.XH2 trigger ROS production in tomato leaf tissue

The concentration of the agent with the polypeptide Average RLU value for 100 nM Flg polypeptide (fold increase (X) relative to Bt.4Q7Flg22 treatment) Negative control (water) 15,824 (0.007X) Bt.4Q7Flg22
Bacillus thuringiensis
(SEQ ID NO: 226)
100 nM 2118932 (-) Ps.tomatoFlgII-28
Pseudomonas syringae, Tomato DC3000 patovar
(SEQ ID NO: 751)
100 nM 3657810 (1.7X) Bt.4Q7Flg22
(SEQ ID NO: 226; 100 nM) +
Ps.tomatoFlgII-28
(SEQ ID NO:751; 100 nM) 4 222 426 (2.0X) Aneurinibacillus.sp.FlgII-28
(SEQ ID NO: 375)
100 nM 2844947 (1.3X)

[0583] Based on the results in Table 67 and Table 68, the second flagellin epitope, termed FlgII-28 and derived from either Gram-negative Pseudomonas syringae, patovar tomato DC3000, or Gram-positive Aneurinibacillus sp.XH2 (SEQ ID NO: 375), was determined to be sufficient to trigger an immune response (eg, ROS production) in tomato (SEQ ID NO: 751) at both 5 nM and 100 nM concentrations. At a concentration of 5 nM, Ps.tomato FlgII-28 was characterized by the highest activity compared to other Flg22 and FlgII-28 polypeptides, and led to an almost 31-fold increase in RLU compared to Bt.4Q7Flg22 at the same concentration, while 5 nM A .spp.FlgII28 provided an equal low ROS response to 5 nM Bt.4Q7Flg22. The Flg22 polypeptide (Ec.Flg22; SEQ ID NO: 526) from Gram-negative Escherichia coli also resulted in increased ROS activity when applied to tomato leaves, with RLU values 12.9X higher than treatment with Bt.4Q7Flg22 alone. The Bt.4Q7Flg22 polypeptide (SEQ ID NO: 226) elicited a very weak ROS response in tomato leaves at 5 nM, but produced a strong response at 100 nM. Ps.tomato FlgII-28, on the other hand, provided a strong ROS response compared to the negative control (water) at both concentrations tested. Thus, tomato leaves showed increased sensitivity to Flg polypeptides derived from the flagellin of Gram-negative bacteria such as Ps.tomato FlgII-28 and Ec.Flg22. In addition, a synthetic variant of Bt.4Q7Flg22, referred to as Syn01Flg22 (SEQ ID NO: 571), had substantially increased activity (3.5X) compared to Bt.4Q7Flg22 treatment when tested at 5 nM.

[0584] As indicated in Table 68, combinations of polypeptides from Gram-positive (Bt.4Q7Flg22; SEQ ID NO: 226) and Gram-negative bacteria Ps.tomato FlgII-28 (Pseudomonas syringae, patovar tomato DC3000; SEQ ID NO: 751) can be used in as a combined foliar application to increase ROS production relative to any of the treatments alone, and enhance plant immunity to certain pathogenic organisms.

Example 46 Synthetic Flg22Syn01 and Flg-15Syn01 Polypeptides to Increase ROS Activity in Maize and Soybean

[0585] A truncated variant of Syn01Flg22 derived from Bt.4Q and Flg22 was prepared that lacked seven N-terminal amino acids, resulting in a 15 amino acid long polypeptide with the sequence nh2-RINSAKDDAAGLAIA-cooh. Said polypeptide, referred to as Bt.4Q7Syn01Flg15 (SEQ ID NO: 752), is a polypeptide naturally occurring in Gram-negative proteobacteria, but not present in the protein sequences of Gram-positive bacteria. The core sequence required for interaction with the receptor, RINSAKDD, is retained in the truncated polypeptide, and thus the 15 amino acid variant is expected to be active in triggering ROS production in plants. To test this assumption, Syn01Flg15 was compared to Bt.4Q7Flg22 and Syn01Flg22 in ROS assays on both corn (Table 69) and soybeans (Table 70). ROS activity assays were performed using the methods previously described in Example 15, except that relative light units (RLU) were recorded using a SpectraMax L luminometer (integration 0.5 s; intervals 2.0 min) over a time period of 40 minutes .

Table 69 Flg22Syn01 and Flg15Syn01 variants have higher activity than Bt.4Q7Flg22 in the ROS activity assay in corn stalk tissue.

Flg polypeptide concentration (nM) Bt.4Q7Flg22
(SEQ ID NO:226) Syn01Flg22
(SEQ ID NO: 571) Syn01Flg15
(SEQ ID NO: 752) 100 33037
(1X*) 54888
(1.6X) BUT. ten 6032
(0.2X) 17660
(0.5X) 14079
(0.4X)

*Relative ROS activity was normalized to mean RLU values for Bt.4Q7Flg22 (SEQ ID NO: 226). N.O.: The value was not tested and, accordingly, the relative value is not determined.

[0586] In the analysis of ROS activity on corn (Table 69), Flg22 Syn01 (SEQ ID NO: 571) had a maximal ROS response in corn stalk tissue at both 100 nM and 10 nM, as indicated by relative corresponding activity of 1, 6X (100 nM) and 0.5X (10 nM) as compared to treatment with Bt.4Q7Flg22 (SEQ ID NO: 226), characterized by an attenuated ROS response, 0.2X at 10 nM. Shortened versions of Syn01Flg22 (SEQ ID NO: 571) or Syn01Flg15 (SEQ ID NO: 752) also showed a larger ROS response, 0.4X at 10 nM, which is twice the relative ROS activity for Bt.4Q7Flg22 (SEQ ID NO: 752). : 226) at the same concentration.

Table 70 Flg22Syn01 and Flg15Syn01 variants are more active than Bt.4Q7Flg22 in the ROS assay on soybean leaf tissue

Flg polypeptide concentration (nM) Relative ROS activity Bt,4Q7Flg22
(SEQ ID NO:226) Relative ROS activity
Flg22Syn01
(SEQ ID NO: 571) Relative ROS activity
Syn01Flg15
(SEQ ID NO: 752) 100 250 432
(1X)* 315 961
(1.25X) But. ten 10.754
(0.04X) 62.020
(0.25X) 42.983
(0.17X)

*Relative ROS activity was normalized to mean RLU values for Bt.4Q7Flg22 (SEQ ID NO: 226). N.O.: indicates that the value has not been tested and therefore the relative value is not determined.

[0587] Similarly, in the soybean ROS activity assay (Table 70), the synthetically produced Bt.4Q7Flg22 mutant described as Bt.4Q7Flg22 Syn01 (SEQ ID NO: 571) also exhibited a maximal ROS response in soybean leaf tissue at a concentration both 100 nM and 10 nM, as indicated by the relative respective potency of 1.25X (100 nM) and 0.25X (10 nM) compared to the treatment with Bt.4Q7Flg22 (SEQ ID NO: 226) characterized by very reduced ROS response, 0.04X, at 10 nM. The truncated versions of Syn01Flg22 or Syn01Flg15 also showed a larger ROS response, 0.17X at 10 nM, which is 4 times the relative ROS activity for Bt.4Q7Flg22 at the same concentration.

[0588] Overall, Syn01Flg22 had higher ROS activity at both concentrations tested in both corn and soy tissues compared to Bt.4Q7Flg22 (SEQ ID NO: 226). The 15 amino acid truncated Syn01Flg15 polypeptide was 2-4 times more potent than Bt.4Q7Flg22 and only slightly less active than the 22 amino acid Syn01Flg22 at 10 nM, indicating that key amino acids are retained in this sequence for stimulating plant immune responses.

Example 47 Chemical Modification of Flg22 Polypeptides to Increase ROS Activity

[0589] Chemical modifications can be made to Flg22 polypeptides to increase the stability of the protein with protection from proteolysis and/or promote longer duration of activity, which can lead to greater accessibility to the FLS2 receptor. In general, modifications to polypeptides can be used to 1) stabilize the polypeptide under adverse conditions or in the presence of proteases, or 2) provide additional functional or molecular characteristics to the peptide. Modifications to improve stability include cyclization of polypeptides and modifications at the N- and C-termini. Head-to-tail cyclization (i.e., formation of an amide bond between the N-terminal amino terminus and the C-terminal carboxyl terminus) results in a rigid polypeptide backbone that resists conformational changes, often stabilizes peptide binding to the receptor, and protects the polypeptide ends from exoproteases. Alternatively, modification of the polypeptide ends can stabilize the polypeptides by neutralization (C-terminal amidation) and prevention of N-terminal degradation (N-terminal acetylation). Increased solubility and stability of the polypeptide can also be conferred by conjugation of a hydrophilic molecule, such as polyethylene glycol (PEG).

[0590] Such modifications used to stabilize Flg22 polypeptides include pegylation, cyclization, and amidation/acetylation, all of which are described in Table 71. Stabilization of polypeptides using pegylation is carried out by linking the polypeptide to polyethylene glycol (PEG). After binding to the polypeptide, each PEG subunit is in close association with 2-3 water molecules, which accordingly increases the solubility of the specified polypeptide, and also increases the overall structure, making it less susceptible to proteolytic degradation and more accessible to the FLS2 membrane receptor on the plant surface. Cyclization can also be used to improve the stability of the Flg polypeptide. Stabilization of the polypeptide can also be achieved by N-terminal acetylation and C-terminal amidation, and these modifications provide more similarity to the natural protein and, accordingly, can increase the biological activity of the specified polypeptide.

Table 71 Modified Flg22 polypeptides

Description of the peptide
(Identification code) Modification MW Subsequence Bt.4Q7Flg22
(modified SEQ ID NO: 226) Derived from a natural sequence from Bacillus thuringiensis 2229.42 nh2 DRLSSGKRINSASDDAAGLAIA conh2 Bt.4Q7Flg22 Mod-1
(modified SEQ ID NO: 226) N-terminal acetylation
C-terminal amidation 229.3 Ac DRLSSGKRINSASDDAAGLAIA nh2 Syn05Flg22
(modified SEQ ID NO: 578) Amino acid substitution (A16P)
N-terminal acetylation
C-terminal amidation 2255.46 Ac DRLSSGKRINSASDDPAGLAIA nh2 Syn05Flg22-PEG4
(modified SEQ ID NO: 578) PEGylation
conjugation with Flg22 before the amide bond 2461 peg4 (where x=4) DRLSSGKRINSASDDPAGLAIA conh2 Syn05Flg22-Cyc
(modified SEQ ID NO: 578) Head-to-tail cycling 2196 Cyc(DRLSSGKRINSASDDPAGLAIA)

[0591] Specialized modified polypeptides as described in Table 71, including Syn05Flg22-Syn05 (J36), Syn05Flg22-PEG (J37), and Syn05Flg22-Cyc, were synthesized at the University of Missouri Molecular Interaction Center (Columbia, Missouri, USA), lyophilized with obtaining a dry powder and confirming the proper MW and the required purity (>70%) using liquid chromatography with mass spectrometry (LC/MS) and high performance liquid chromatography (HPLC), respectively. Standard synthesized polypeptides, including Bt.4Q7Flg22 (SEQ ID NO: 226) and Bt.4Q7Flg22 Mod-1 (SEQ ID NO: 226; J41), were obtained from Genscript (Piscataway, NJ, USA). All lyophilized polypeptides were resuspended in ultrapure water to a concentration of 10 mM and serially diluted in ultrapure water to the desired concentration for testing in soybean and corn ROS assays as described above in Example 15.

[0592] To obtain soybean samples from plants at stages V1-V3 (variety Morsoy), fully opened trifoliate leaves were cut. Leaf disks (4 mm) were cut out using a cork drill and then placed on the surface of 150 μl of water, abaxial side down, overnight prior to the ROS assay described above.

[0593] To obtain maize samples, aerial tissue was obtained from V1-V4 stage maize plants (Beck's 5828 YX hybrid) as previously described. Then cut out pieces of leaves with a size of 1 mm were placed on the surface of 150 µl of water overnight.

[0594] ROS activity assays were performed using the methods previously described in Example 15, except that relative light units (RLU) were recorded using a SpectraMax L luminometer (0.5 s integration; 2.0 min intervals) over the period 40 minutes. First, relative light units (RLU) versus time were plotted using time kinetics for each concentration tested, followed by integration to calculate the area under the curve to calculate total RLU produced. Then, for each polypeptide used in soybeans (Tables 72-73) and corn (Table 74), average total RLUs (n=4 samples per treatment) were plotted against polypeptide concentration.

[0595] The data for each treatment was fitted using logarithmic regression or best fit linear regression (R>0.80). Using best fit regression, for each polypeptide, the concentration required to produce a total RLU of 15,000 (corn) or 50,000 (soy) was calculated and the % activity in each dataset was compared with the control treatment (Tables 72-74) .

Table 72 N- and C-terminally modified Flg22-Bt polypeptides trigger production of reactive oxygen species in soybean

Treatment
(the code) Polypeptide concentration (nM) to produce a total of 5×10 ⁴ RLU % activity (compared to unmodified Bt.4Q7Flg22
(SEQ ID NO: 226) Bt.4Q7Flg22
(SEQ ID NO: 226) 31.4 100.0% Bt.4Q7Flg22 Mod-1
(SEQ ID NO: 226) 29.6 106.14%

[0596] The Flg22 polypeptide concentration required to provide an RLU output of 50,000 RLU for Bt.4Q7Flg22S Mod-1 (SEQ ID NO: 226) was lower than for the existing Bt.4Q7Flg22 (SEQ ID NO: 226), which has been shown to increase yield and protect soybean plants. This indicates that modification of Flg22 by N-terminal acetylation and/or C-terminal amidation does not interfere with polypeptide binding to the FLS2 receptor, and modifications can be used to produce a more active and/or stable Flg22 variant, as indicated by a +6% increase in activity Bt.4Q7Flg22S Mod-1 relative to Bt.4Q7Flg22 (Table 72).

[0597] The Center for Molecular Interactions at the University of Missouri (Columbia, Missouri) generated new polypeptides with a single amino acid substitution (A16P) compared to the unmodified Bt.4Q7Flg22 polypeptide (SEQ ID NO: 226), which resulted in the Syn05Flg22 polypeptide (SEQ ID NO: 578), which was further modified by N-terminal pegylation to give Syn05Flg22-PEG (SEQ ID NO: 578) and head-to-tail cyclization to give Syn05Flg22-Cyc (SEQ ID NO: 578). Soybean ROS were analyzed to evaluate the effect of these two additional modifications, namely, N-terminal pegylation and head-to-tail cyclization of the Flg22 polypeptide; the results are shown in table 73.

Table 73 Modified synthetic Flg22-Bt polypeptides trigger production of reactive oxygen species in soybean

Treatment Polypeptide concentration (nM) to produce a total of 5×10 ⁴ RLU % activity (compared to Syn0Flg22; SEQ ID NO: 578) Syn05Flg22
(SEQ ID NO: 578) 89.8 100.0% Syn05Flg22-PEG
(SEQ ID NO: 578) 64.8 138.6% Syn05Flg22-Cyc
(SEQ ID NO: 578) 146.9 61.1%

[0598] In a soybean ROS assay comparing the relative activity of Syn05Flg22 (SEQ ID NO: 578) and two modified variants of said polypeptide, the pegylated Syn05Flg22-PEG polypeptide (SEQ ID NO: 578) required substantially less of said polypeptide to achieve an overall complexity of 50,000 RLU, resulting in +38% increased activity compared to the non-pegylated variant or Syn05Flg22 (SEQ ID NO: 578). Pegylation of the N-terminus of the peptide increases the hydrophilicity of said polypeptide and may increase affinity for the peptide-binding pocket of the FLS2 receptor. In contrast, the cyclized Syn05Flg22-Cyc variant (SEQ ID NO: 578) required more polypeptide in the ROS activity assay (+57.1 nM) compared to the non-cyclized Syn05Flg22 variant to produce a total of 50,000 RLUs in the soybean ROS assay . This result suggests that cyclization of the Flg22 polypeptide (Syn05Bt.4Q7Flg22-Cyc) may result in a more rigid polypeptide backbone characterized by altered binding to the FLS2 receptor, thus more cyclized peptide is needed to achieve an equivalent ROS response. However, the increased stability of the cyclized polypeptide in the environment may compensate for the slight decrease in activity.

Table 74 Modified synthetic Flg22-Bt polypeptides trigger reactive oxygen species production in corn

Treatment Polypeptide concentration (nM) to produce a total of 5×10 ⁴ RLU % activity (compared to unmodified Syn05Flg22
(SEQ ID NO: 578) Syn05Flg22
(SEQ ID NO: 578) 19.5 100.0% Syn05Flg22-PEG
(SEQ ID NO: 578) 15.0 130.3%

[0599] In the maize ROS assay, the pegylated Syn05Flg22-PEG variant required substantially less (nearly 5 nM) of the indicated polypeptide to achieve a total of 15,000 RLUs, resulting in +30% increased activity compared to the non-pegylated variant or Syn05Flg22 (table 74).

[0600] Modification of Flg22 (Bt) or Syn05Flg22 (Bt) polypeptides by N-terminal acetylation, N-terminal pegylation, C-terminal amidation, and/or head-to-tail cyclization results in a peptide that retains activity, as assessed based on results of analyzes for ROS in tissues of corn and soybeans. These polypeptides can be used to deliver a further stabilized Syn05Flg22-derived (SEQ ID NO: 578) polypeptide variant for agricultural use (foliar application, seed treatment, furrow application at planting, seedling application, or trunk injection). Syn05Flg22-Cyc cyclization can be used to increase the stability of this polypeptide, but it interferes with ROS activity, presumably by affecting the affinity of this synthetic polypeptide for the FLS2 membrane receptor.

Example 48 Adjuvant Compatibility with Flg22 Polypeptides

[0601] Product formulations with Flg22 polypeptides can typically include antimicrobial biostatic preservatives such as Proxel and surfactants. Accordingly, the compatibility of these types of adjuvants was tested using ROS activity assays to determine the effect on response to Flg22 in solution when used in combination with such adjuvants. Proxel preservatives are generally broad spectrum biocides for the preservation of many agricultural products, protecting them from spoilage by bacteria, yeasts and fungi. Surfactants in general are also widely used in agricultural formulations to improve the penetration of many agrochemicals into the plant for increased efficiency. In this study, five different Proxel preservatives and two different non-ionic surfactants were tested in formulations in combination with Bt.4Q7Flg22 (SEQ ID NO: 226) for ROS generation efficiency using soybean leaf ROS activity assay. The various Proxel (Lonza) formulations are described in Table 75 below. These Proxel formulations were mixed with 40 μM Flg22 polypeptide in the manufacturer's recommended flow range in the accompanying leaflet (Lonza) and then diluted in the ROS assay to a final polypeptide concentration of 100 nM and the Proxel concentrations indicated in Table 75. The nonionic surfactants tested were used in the ROS assay at a flow rate within the range recommended by the individual supplier or manufacturer in the accompanying instructions. Four sample averages of RLU measurements after ROS analysis were taken using soy leaf discs as previously described in Example 15, except that relative light units (RLU) were recorded using a SpectraMax L luminometer (integration 0, 5 s; intervals of 2.0 min) over a period of 40 minutes. The average of these 4 RLUs is shown in Table 76.

Table 75 Miscellaneous PROXEL Supplements Used as Adjuvants in Polypeptide Formulations

PROXEL formulations Chemical Description PROXEL BD20 20% aqueous dispersion of 1,2-benzisothiazolin-3-one PROXELBC An aqueous dispersion of a mixture of 1,2-benzisothiazolin-3-one (BIT), 5-chloro-2-methyl-4-isothiazolin-3-one (CIMT) and 2-methyl-4-isothiazolin-3-one (MIT) PROXELGXL 20% dipropylene glycol aqueous solution of 1,2-benzisothiazolin-3-one PROXELBN Aqueous dispersion of 1,2-benzisothiazolin-3-one and 2-bromo-2-nitropropene-1,3-diol PROXEL AQ Solution of 1,2-benzisothiazolin-3-one in water

Table 76. RLU output values in soybean leaf ROS activity assays using Flg22 polypeptide formulated with various Proxel preservatives

Comparison of processing with or without the addition of PROXEL preservative
Concentration Average RLUs
(Magnification factor relative to negative control) Sham-treated (with water) negative control 4823 Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM)
(No added preservative PROXEL) 81887
(17.0X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXEL BD20 (0.0005988%) 89188
(18.5X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELBD20 (0.00011976%) 105527
(21.9X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELBC (0.0005988%) 136575
(28.3X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELBC (0.00011976%) 92808
(19.2X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELGXL (0.0002994%) 128410
(26.6X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELGXL (0.0008982%) 101847
(21.1X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELBN (0.0002994%) 91554
(19.0X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELBN (0.00017964%) 105164
(21.8X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELAQ (0.0005988%) 116634
(24.2X) Bt.4Q7Flg22
(SEQ ID NO: 226 at 100 nM) +
PROXELAQ (0.0035928%) 98394
(20.4X)

[0602] All Proxel preservative products as described in Table 76 were compatible when used in formulations with the Flg22 polypeptide (Bt.4Q7Flg22; SEQ ID NO: 226), as indicated by high RLU values (19.0-28.3X magnification). sham-treatment) compared to the control Bt.4Q7Flg2 polypeptide without Proxel preservative (17.0X magnification relative to sham-treatment).

Table 77. RLU output values in ROS activity assays in soybean leaf tissues using the Flg22 polypeptide formulated with various nonionic surfactants

Comparison of treatment with or without the addition of a surfactant
Concentration Average RLUs
(Magnification factor relative to negative control) Sham-treated (with water) negative control 51288 Bt.4Q7Flg22
(SEQ ID NO: 226)
52.2 nM
Equivalent: 4.0 fl oz per acre in 10 gallons of water/acre 350503
(6.8X) Bt.4Q7Flg22
(SEQ ID NO: 226)
52.2 nM+
Silwet-L77 (0.025%) 142478
(2.8X) Bt.4Q7Flg22
(SEQ ID NO: 226)
52.2 nM+
Silwet-L77 (0.10%) 163517
(3.2X) Bt.4Q7Flg22
(SEQ ID NO: 226)
52.2 nM+
NIS90:10 (0.25%) 329295
(6.4X) Bt.4Q7Flg22
(SEQ ID NO: 226)
52.2 nM+
NIS90:10 (0.5%) 295726
(5.8X)

[0603] All (nonionic) surfactant agents as described in Table 77 were compatible when mixed at the indicated concentrations with the Flg22 polypeptide (Bt.4Q7Flg22; SEQ ID NO: 226) at a concentration of 52.2 nM, equivalent to operating flow 4 0 fl oz/acre of Composition 1 (Bt.4Q7Flg22; SEQ ID NO: 226; 16.7 μM) in water at a spray rate of 10 gallons per acre. The fold increase in ROS production relative to the sham-treated control was comparable for the control Bt.4Q7Flg2 polypeptide without surfactant (6.8X relative to control) and for the Bt.4Q7Flg2 polypeptide with NIS90:10 nonionic surfactant when used at 0.25% or 0.5% v/v of the treatment solution (5.8-6.4X), or was slightly lower for the Bt.4Q7Flg2 polypeptide with Silwet-L77 when used at 0.025% v/v or 0.1% v/v. volume from treatment solution (2.8-3.2X). Silwet-L77 (Helena), a nonionic silicone surfactant, is presented as a copolymer with improved wetting and spreading characteristics when used in aqueous sprays. NIS90:10 (Precision Laboratories) is a low-foaming, non-ionic surfactant that enhances crop protection and performance by increasing spray solution coverage and improving penetration into the target leaf surface. Both nonionic surfactants in combination with Bt.4Q7Flg22 allowed ROS production in response to the Flg22 polypeptide in target leaf tissues (Table 77) and are therefore compatible with the Flg22 polypeptide for foliar application in the field.

Example 49 Preparation of Bt.4Q7Flg22 Using Enterokinase Digestion Fermentation and Activation Methods for Disease Prevention Trials in Potato, Lentil and Citrus Trees

[0604] Bt.4Q7Flg22 (SEQ ID NO: 226) was presented in a conformation that provides stabilization of the specified polypeptide and increased activity for an alternative method of production, namely, bacterial fermentation. The Bt.4Q7Flg22 polypeptide was combined with an amyQ secretion signal from Bacillus amyloliquefaciens alpha-amylase) fused to glutathione S-transferase (GST) and an enterokinase cleavage tag sequence as described below: amyQ secretion signal (Bacillus amyloliquefaciens alpha-amylase) GST ( Schistosoma japonicum)_Linker_Enterokinase cleavage site_Bt.4Q7Flg22_Stop codon (Table 78).

Table 78 Cloning of Bt.4Q7Flg22 with sequences to enhance polypeptide stability and activity

Description Amino acid sequences amyQ secretion signal
(Bacillus amyloliquefaciens)
SEQ ID NO:769 MIQKRKRTVSFRLVLMCTLLFVSLPITKTSA GST
(Schistosoma japonicum)
SEQ ID NO:770 MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKWQIAWK Linker
SEQ ID NO:771 GGGGGGS Label for cleavage by enterokinase
(Consensus target for cleavage by bovine enterokinase, a light chain protease)
SEQ ID NO: 772 DDDDK Bt.4Q7Flg22
(SEQ ID NO: 226)
(Bacillus thuringiensis strain 4Q7) DRLSSGKRINSASDDAAGLAIA

*DNA used for cloning from amy E, GST and Bt.4Q7Flg22 secretion signal sequences (SEQ ID NO: 226) came from proprietary internal libraries; producer strain code=H101 (Chloramphenicol resistant)

Table 79 Cloning of Syn01Flg22 (SEQ ID NO: 571) with sequences to enhance polypeptide stability and activity

Description Amino acid sequence amyQ secretion signal
(Bacillus amyloliquefaciens)
SEQ ID NO: 769 MIQKRKRTVSFRLVLMCTLLFVSLPITKTSA GST
(Schistosoma japonicum)
SEQ ID NO: 770 MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKWQIAWK Linker
SEQ ID NO: 771 GGGGGGS Label for cleavage by enterokinase
(Consensus target for cleavage by bovine enterokinase, a light chain protease)
SEQ ID NO: 772 DDDDK Bt.4Q7Flg22-Syn01
(SEQ ID NO: 226)
(Bacillus thuringiensis strain 4Q7) DRLSSGKRINSAKDDAAGLAIA

*DNA used for cloning from amy E, GST and SynFlg22 secretion signal sequences (SEQ ID NO: 571) came from proprietary internal libraries. Producer strain code=H114 (tetracycline resistant)

Table 80. Cloning of a Thionin-Like Protein with a Sequence for Secretion into Growth Media for Fermentation

Description Amino acid sequence amyQ secretion signal
SEQ ID NO: 769
(Bacillus amyloliquefaciens) MIQKRKRTVSFRLVLMCTLLFVSLPITKTSA Thionin-like protein
(SEQ ID NO: 650)
(Synthetic) RTCESQSHRFKGPCSRDSNCATVCLTEGFSGGDCRGFRRRCRCTRPCVFDEK

[0605] The sequences from Tables 78, 79 and 80 were cloned into a standard cloning vector containing an ampicillin selectable marker and either a chloramphenicol (Cm) or tetracycline (Tet) selectable marker that can be replicated in E. coli and then transferred to a Bacillus strain subtilis K08 for production (producer strain codes: H101=amyQ-GST-EK-BtFlg22, H114=amyQ-GST-EK-BtFlg22-Syn01 and H117=H117=amyQ-Thionin-like). Production by fermentation was carried out starting with an overnight culture in sterile 2XYT medium (16 g bactotrypton, 10 g yeast extract and 5 g NaCl per liter; pH adjusted to 7.0) with 10 μg/ml Cm or Tet, which was then diluted with fresh 2XYT medium with 10 µg/ml Cm or Tet the next day. The production was carried out in a medium volume of 50 ml (shaking flask) or 3 l (glass bioreactor) at a constant temperature of 30°C. Larger scaled volumes can include 5-1000L+, up to 30000L). Bacterial growth was monitored until the culture reached an optical density of 0.6-1.0, after which isopropyl-β-D-1-thiogalactopyranoside (IPTG) was added to a final concentration of 0.1-1.0 mM to induce production of the GST-Bt fusion protein. .4Q7Flg22. The induced production was continued under culture conditions for another 12-24 hours to obtain a fusion protein secreted into the growth media. Upon secretion, the amyQ secretion label is cleaved from the fusion protein. The cultures were then centrifuged at 5000×g for 20 min and filtered through a 0.22 µm bottle vacuum filter to remove bacterial cells. The sterile filtrate was then collected and used as a foliar treatment on lentil and potato plants in a Sclerotinia disease prevention trial (Example 50) or as a stem injection in citrus trees to eradicate and prevent symptoms of HLB disease (Example 51).

[0606] After fermentation, two variants of the Bt.4Q7Flg22 polypeptide product (SEQ ID NO: 226) were used in disease prevention trials in potato and lentils, one without enterokinase treatment (H101 filtrate, non-activated) and the other after activation using enterokinase for cleavage GST tag fused to Flg22 polypeptide (EK activated filtrate H101). To activate Bt.4Q7Flg22, 32 U (units) of enterokinase (EK: light chain enterokinase; New England BioLabs, Inc, item #P8070) per 1 ml H101 filtrate was added with an incubation period of 2-3 hours at 30°C for enzymatic release Bt.4Q7Flg22 upon detachment from the GST-EK cleavage site to provide an activated released product containing 22 amino acid Bt.4Q7Flg22 polypeptides. For citrus tree injection tests, the H101 filtrate and H114 filtrate were EK-activated by adding 0.8 U of enterokinase light chain (New England Biolabs, Inc, item #P8070) per ml of filtrate, incubating for 3 hours at 30°C to enzymatic release of the Flg22 polypeptide. The release of the thionin-like peptide, which was produced without a GST tag, did not require an activating treatment.

Example 50 Foliage Pretreatment with Bt.4Q7Flg22 Polypeptides Protects Lentil and Potato Plants from Sclerotinia Stem Rot (White Mold)

[0607] Bt.4Q7Flg22 treatments (SEQ ID NO: 226) were tested for their ability to provide protection to lentil and potato plants against infection and disease progression caused by Sclerotinia sclerotorium strain MT07 (white mold). Three different Bt.4Q7Flg22 polypeptide variants were studied in disease assessment studies, a formulation with Bt.4Q7Flg22 (100 μM) in sodium phosphate buffer, pH 5.7, and two different Bt.4Q7Flg22 variants produced using fermentation methods as described ( example 49) used with and without Flg22 activation by enterokinase (EK) and referred to as H101 filtrate.

[0608] Prior to the use of these three variants of these polypeptides in disease protection assays in lentil and potato plants, an analysis of ROS activity in corn petiole tissues was performed using the methods described previously in example 15 to confirm that the H101 Bt.4Q7Flg22 filtrate, in in particular, the treated EK was active. Activation of H101 filtrates by Bt.4Q7Flg22 without enterokinase and with enterokinase (EK=8 U/mL filtrate) was compared with activation by synthetic Bt.4Q7Flg22 (SEQ ID NO: 226) which was used to generate a series of concentration comparisons to predict Flg22 concentrations in H101 filtrates, obtained using fermentation procedures.

Table 81. ROS activity assay using fermentation-produced Flg22 with and without enterokinase activation in maize

Flg22 polypeptide concentration Mean RLU value upon treatment with Flg22 polypeptides Change (X) in the number of RLUs for the Flg22 polypeptide Compared to the negative control Bt.4Q7Flg22
(SEQ ID NO: 226)
(1.0 nM) 6851 0.8X Bt.4Q7Flg22
(SEQ ID NO: 226)
(5 nM) 9389 1.1X Bt.4Q7Flg22
(SEQ ID NO: 226)
(25 nM) 12157 1.4X Bt.4Q7Flg22
(enzymatic filtrate H101) with (+) enterokinase, 8 U/ml (0.1% v/v) 25212 3.0X Bt.4Q7Flg22 (H101 Enzymatic Filtrate) Without (-) Enterokinase (0.1% v/v) 16891 2.0X

*RLU values are reported as the average of 4 separate measurements after background RLU levels have been subtracted.

[0609] Both fermentation-produced Bt.4Q7Flg22 H101 filtrate, activated and non-activated EK, provided higher ROS activity (RLU values) than control (0 nM Bt.4Q7Flg22). EK-treated H101 Bt.4Q7Flg22 filtrates (0.1% v/v) applied to corn stalks in the ROS assay provided a 3.0X increase in RLU values compared to control treatment without any Flg22 polypeptide, and the ROS response was higher than Bt.4Q7Flg22 (SEQ ID NO: 226) at 25 nM; accordingly, the calculated activity of Bt.4Q7Flg22 in the undiluted EK-activated filtrate was ≥ 25 μM. Treatment with fermentation-produced H101 Bt.4Q7Flg22 filtrates without EK still resulted in higher ROS activity (2.0X RLU) relative to the negative control treatment, but the increase in RLU values was less than for H101 Bt.4Q7Flg22 filtrates with EK. After confirming the activity of H101 filtrates in ROS assays (Table 81), they were evaluated in disease protection studies in potatoes and lentils.

[0610] Various formulations with Bt.4Q7 Flg22 polypeptides were used in lentil and potato plants by pre-treatment of plant foliage 48 hours prior to inoculation with the fungus Sclerotinia sclerotorium, in combination with a fungicide and without a fungicide (Endura, active ingredient 70% boscalid), effective for the treatment and protection of plants against infection by the fungus Sclerotinia (white mold). Bt.4Q7Flg22 formulations were tested using a crop disease model (Montana State University, Crop Protection Advisory Service) to investigate the effects of each foliar pretreatment on preventing and protecting against disease and its symptoms. All treatments, including control (water), were performed on lentil and potato plants using a spray gun connected to a variable air compressor set to 50 psi spray gun outlet pressure. inch. After pre-treatment, the plants were inoculated with Sclerotinia sclerotorium using a mycelial plug (agar plug coated with mycelium), which was applied with the mycelium side to the stem of the plants, and placed in humid chambers (100%) for a predetermined time.

Lentils

[0611] Lentil plants (cv. Pennel) were cultured on a soilless medium consisting of a 1:1 mixture of peat moss and perlite in 4'4' containers, one plant per container, for 24 days in a controlled growth chamber under the following growth conditions: 300-400 µmol m ^-2 s ^-1 (light photons) with a daily light-dark cycle on 13/11 and a temperature range of 21°C day/15°C night. Disease studies included five lentil plants per each of six different foliar treatments, with 6 plant replicates per treatment, for a total of 30 plants per foliar treatment as described in Table 35. All foliar treatments used for pretreatment treatments were applied with the addition of a non-ionic surfactant (ALLIGARE SURFACE; Alligare, LLC) to a final concentration of 0.1% (v/v), or a concentration of alkyl polyoxyethylene, glycol derivatives. Each treatment with Bt.4Q7Flg22, whether formulated or fermented with Bt.4Q7Flg22, was performed at a working rate of 0.1% (v/v) or 300 µl of product per 300 ml of water; each plant was given an equivalent number of sprays to completely cover the foliage, using 8 ml of each treatment for all 30 plants per treatment. Pre-treatment with Endura fungicide was carried out at a volume equivalent to a working application rate of 11 fl oz per acre (803.8 ml/ha), following the instructions for use in the instructions for use of the drug. Treatments were randomized using block randomization with a completely random distribution. Approximately 48 hours after pre-treatment, plants were inoculated with a strain of Sclerotinia sclerotorium isolated locally in Montana using a mycelial plug (agar plug coated with mycelium) which was applied with the mycelium side to the stem of the plants. The lentil plants were then placed in a humid chamber (100%) for a period of 72 hours. 11 days after inoculation, disease symptoms were evaluated and assigned a score, and the average fresh weight (total weight of each replicate - grams) was determined (Table 82). The plants were allowed to dry for approximately 3 weeks and then the dry weight (total weight per replicate - grams) was determined (Table 82)

[0612] Determination of disease scores (disease scores on a scale of 0-7), wet weight and dry weight (in grams) were collected for each replicate of five plants and then averaged over the total number of plants (n=30). Disease scores were scored on a scale of 0-7, where a score of 0 is equivalent to no disease and a score of 10 means no plants survived (Table 82).

Table 82 Disease assessment in lentils 10 days after infection with Sclerotinia sclerotiorum

Treatment Disease indicators on a 0-7 point scale (STDEV) Average total wet weight per plant (grams)
(STDEV) Average total dry weight per plant (grams)
(STDEV) Control (water) 2.83
(±1.84) 4.52
(±1.18) 0.95
(±0.21) Endura fungicide 0.50
(±0.84) 2.89
(±0.30) 0.68
(±0.05) Ready composition with Bt.4Q7Flg22 1.33
(±0.82) 5.44
(±0.48) 0.99
(±0.07) Fungicide Endura+
Ready composition with Bt.4Q7Flg22 1.0
(±0.89) 4.95
(±0.59) 0.96
(±0.05) Non-activated filtrate H101 2.17
(±1.47) 4.51
(±0.93) 0.85
(±0.06) Activated EK filtrate H101 2.17
(±1.33) 6.11
(±0.69) 1.09
(±0.11)

*p-value<0.1 means there is a statistically significant difference between treatments and control (water).

[0613] Foliar application of Bt.4Q7Flg22 formulation was compared with Endura fungicide, Endura fungicide in combination with Bt.4Q7Flg22 formulation and two Bt.4Q7Flg22 formulations containing Flg22 polypeptides produced by fermentation reactions with and without EK activation as previously described in Table 82. All foliar treatments in the crop disease model were compared with each other and with control (water) treated plants, and the onset of disease symptoms was assessed 11 days after inoculation. Each plant was assigned a disease score from 0 to 7. The total fresh and dry weight (in grams) per plant was also determined. Endura fungicide, a commercially available treatment for Sclerotinia sclerotium, produced the least symptomatic disease in lentils when compared with all foliar treatments, with a disease score of 0.50, with water treatment (control) resulting in a disease score of 2.83. Foliar application of the formulation with Bt.4Q7Flg22 in lentil plants resulted in an increase in resistance to Sclerotinia with a disease score of 1.33 (p-value=0.0972) compared to plants that received the control water treatment. In contrast to Endura fungicide treatment, which resulted in slower growth compared to control (water) treated plants, Bt.4Q7Flg22 pre-formulation treatment resulted in sustained vigorous growth during early symptom development. Lentil plants pre-treated with Bt.4Q7Flg22 formulation had an average wet weight of 5.44 grams per plant, in contrast to plants treated with Endura fungicide alone (2.89 g) or control (water) (4.52 G). Combined treatment with Endura fungicide and formulation with Bt.4Q7Flg22 polypeptide further increased the protection of lentil plants from developing symptoms at a disease score of 1.0 (p-value=0.0524) compared to control (water) treated plants. The weight (fresh and dry) of plants that were pre-treated with the formulation with Bt.4Q7Flg22 polypeptide was higher than the fresh or dry weight of plants that were treated with control (water) or Endura fungicide alone. Bt.4Q7 Flg22 polypeptides derived from fermentation products (non-activated EK and activated EK) had equivalent disease symptom scores of 2.17, which is lower than the disease score of plants treated with water control alone. However, wet weight per plant treated with the activated EK variant of the Bt.4Q7Flg22 polypeptide was significantly higher at 6.11 grams (p-value=0.0266) compared to water-treated plants. The activated EK variant of the Bt.4Q7Flg22 polypeptide also had the highest total fresh and dry weight compared to all other treatments in Table 82. Other important results of this study were the finding that pre-treatment of lentil plants with the Bt.4Q7Flg22 polypeptide formulation protected lentils from fungicide-induced damage. The average wet weight of plants that were treated with Endura fungicide was 2.89 g, while that of the formulation treated with Bt.4Q7Flg22 provided 5.44 g (p-value=2.645×10-05). Bt.4Q7Flg22 produced by fermentation contained the enterokinase (EK) enzyme used to cleave the Bt.4Q7Flg22 polypeptide from GST-EK-Bt.4Q7Flg22 as previously described. Treatment of lentils with this Bt.4Q7Flg22 filtrate provided increased activity of the Flg22 polypeptide, thus leading to a significant improvement in plant growth during infection compared to water-treated control plants (p-value=1.180×10-05). Non-activated EK or GST-EK-Bt.4Q7Flg22 or undigested Bt.4Q7Flg22 filtrate did not enhance plant growth compared to plants treated with control (water) alone (p-value=0.9852).

Potato

[0614] Seed potatoes (variety: Russet Burbank) were planted from 2 cm potato fragments with protruding "eyes" (1 fragment per container) cut down, to a depth of approximately 7-8 cm, in a soilless medium consisting of a mixture of 1:1 peat moss and perlite in containers of 10×10 cm. Cultivated one potato plant per container for 19 days in a controlled growth chamber under standard conditions with approximately 300-400 µmol m ^-2 s ^-1 (light photons) at daily light - dark cycle 13/11 and a temperature range of 21°C day/15°C night. 19 days after planting, potato plants were pre-treated with foliar treatments as described in Table 36. Disease studies included five potato plants for each of six different foliar treatments with 6 replicate plants per treatment, for a total of 30 plants for each foliar treatment as described in Table 83. All foliar treatments used for pretreatment were applied to the foliar with a nonionic surfactant (ALLIGARE SURFACE; Alligare LLC) to a final concentration of 0.1% ( by volume), or the concentration of alkylpolyoxyethylene, glycol derivatives. Each treatment with Bt.4Q7Flg22 using the formulation and fermented product was done at a working rate of 0.1% (v/v) or 300 µl of product in 300 ml of water, and each plant was given an equivalent number of sprays to completely cover the foliage, 15 ml of each treatment for all 30 plants per treatment. A pre-treatment with Endura fungicide was applied at a working rate equivalent to 11 fl oz per acre (803.8 ml/ha) following the instructions for use of the formulation. Treatments were randomized using block randomization with a completely random distribution. Approximately 48 hours after the pre-treatment, the plants were inoculated with Sclerotinia sclerotorium using a mycelial plug (agar plug coated with mycelium) which was applied with the mycelium side to the plant stem and placed in a humid chamber (100%) for 192 hours. 16 days after inoculation, the symptoms of the disease were assessed and assigned a score, and the average fresh weight (total stem weight - grams) was recorded (table 83). The plants were left to dry for 12 days, after which the dry weight (total stem weight - grams) was recorded (Table 83).

[0615] After 48 hours, potato plants were inoculated using mycelial plugs placed on the soil near each plant and placed in a humid irrigated chamber. Treatments were randomized using block randomization. Indicators of the disease (according to the rating scale with points from 0 to 6). The fresh and dry stem weights (in grams) for each plant were also determined and then averaged over the total number of plants (n=30). The dry weight of the stems was determined after the plants had completely dried out approximately 12 days after harvest. Disease scores were assessed 16 days after the initial inoculation. Disease scores were scored on a scale of 0 to 6, where a score of 0 is equivalent to no disease and a score of 6 means no plant survived.

Table 83. Disease assessment in potato plants 15 days after infection with Sclerotinia sclerotiorum

Treatment Indicators of the disease on a point scale of 0-6
(STDEV) Average fresh weight of stems per plant (grams; "g")
(STDEV) Average dry weight of stems per plant (in grams; "g")
(STDEV) Control (water) 2.83
(+1.33) 96.01
(+17.05) 12.08
(+2.75) Endura fungicide 0.50
(+0.84) 110.98
(+18.32) 16.86
(+8.69) Ready composition with Bt.4Q7Flg22
(SEQ ID NO: 226) 1.83
(+0.98) 113.37
(+14.58) 15.01
(+3.72) Non-activated filtrate H101 2.33
(+1.03) 98.08
(+15.34) 12.96
(+2.77) Activated EK filtrate H101 1.83
(+0.75) 117.76
(+15.83) 17.66
(+8.70)

*p-value<0.1 means there is a statistically significant difference between treatments and control (water).

[0616] The effect of leaf pre-treatment with Bt.4Q7Flg22 formulation and fermentation-derived Bt.4Q7Flg22 polypeptides (H101 filtrates) on the development of disease symptoms in Endura fungicide-treated potato plants and control water treatment was compared. . Foliar application of the formulation with Bt.4Q7Flg22 (SEQ ID NO: 226) as a pre-treatment of potato plants resulted in a disease score of 1.83, in contrast to plants that were treated with control (water) (disease score=2.83). Plants that were pre-treated with Endura fungicide showed less disease symptoms with a disease score of 0.50 (p-value=0.0045) compared to control (water) treated plants. Pre-treatment with the Bt.4Q7Flg22 polypeptide formulation resulted in a mean plant disease rate similar to that of enterokinase-activated Bt.4Q7Flg22 (activated EK H101) as a filtrate (fermentation product); both treatments had disease rates of 1.83. Non-activated EK or GST-EK-Bt.4Q7Flg22 or Flg22 filtrate without cleavage treatment (non-activated H101) treated with plants had a score of 2.33, which was not significantly different from the disease score of control (water) treated plants ( p-value=0.4835). However, pre-treatment of potato plants with EK-activated Bt.4Q7Flg22 filtrate resulted in increased average fresh and dry weight of stems per plant relative to all treatments, with an increase in fresh weight of stems by approximately 20 g and an increase in dry weight of stems by nearly 6 g per plant compared to plants that were pre-treated with control (water). All plants treated with the Bt.4Q7Flg22 polypeptide formulation showed increased fresh and dry stem weight per plant compared to plants that received the control treatment with water alone.

Example 51 Treatment of Candidatus Liberibacter asiaticus Flg22 Infection with Antimicrobial Polypeptides

[0617] Bt.4Q7Flg22 formulations were applied by injecting both Valencia orange (Citrus sinensis) and Ruby Red grapefruit (Citrus×paradisi) into the trunk of trees. The study was conducted in a commercial fruit grove located in central Florida (Okeechobee County). Injection treatment using Bt.4Q7Flg22 polypeptide (SEQ ID NO: 226) at 1X low concentration (0.55 µmol peptide; calculated phloem concentration 0.138 µM) and 10X high concentration (5.5 µmol peptide; calculated phloem concentration 1.38 μM) were compared with untreated control trees. Injection treatments were performed using block randomization with complete random distribution, on 10 grapefruit trees (4 years old) per treatment. The injection was carried out in April (2017) at the stage of the first growth, from the appearance of leaves until they reach full size. Injection into grapefruit trees was carried out using a low pressure injection device, BRANDTENTREE (BRANDT). Leaf samples from each of the grapefruit trees were collected at the time of injection (0 day), 21 and 56 days after injection. A total of six leaf samples per tree were selected to represent the leaf population per tree, including leaf age, location, and presence of visible symptoms. Each central vein was separated from the leaf blade and immediately cut into very small pieces with a new sterile razor blade. Then the leaf samples from each tree were placed in an individual test tube, which was then stored in a freezer at -80°C until further processing. DNA extraction and real-time polymerase chain reaction or quantitative PCR analysis (qPCR) on these leaves was performed at Southern Gardens Citrus (Cleviston, FL).

[0618] The presence of titers of CLas bacteria in HLB-infected citrus trees can be determined using quantitative real-time polymerase chain reaction (qPCR) methods with specific primers to confirm the presence of the disease (Li, W.B., Hartung, J.S. and Levy, L. 2008 “ Optimized quantification of unculturable 'Candidatus Liberibacter spp.' In host plants using real-time PCR”, Plant Disease 92: 854-861). DNA extraction and quantitative PCR analysis (qPCR) on these leaves was performed at Southern Gardens Citrus (Cleviston, FL) using an HLB primer kit targeting C. Liberibacter 16S DNA, 5'→3' (forward): HLB TCGAGCGCGTATGCAATACG (SEQ ID NO: 773); (reverse) HLBr: GCGTTATCCCGTAGAAAAAGGTAG (SEQ ID NO: 774); HLBpc (probe): AGACGGFTGAGTAACGCG (SEQ ID NO: 775) labeled with an intercalating fluorescent reporter dye]. Spent 40 qPCR cycles and measured the fluorescent signal, proportional to the amount of dsDNA in solution. qPCR analysis allows the detection of CLas bacteria in the tissues of citrus plants. For each treatment, cycle threshold (Ct) values were obtained from the qPCR assay. The Ct is the equivalent of the number of PCR cycles required to obtain a relative threshold. As is common practice in the field of molecular biology, the change in Ct value is recorded to determine the relative amount of CLas DNA in treated or untreated samples, or in treated samples at one time point or another time point. The higher the Ct value, the more pronounced the effect of the treatment or the more effective it is, as indicated by the reduction/elimination of CLas bacteria on the tree. The percentage reduction in bacterial load can be calculated as follows:

% reduction in sample over time

or

% reduction in treated sample relative to control =

[0619] The results of the grapefruit test are shown in FIG. 9. Mean values for Ct comparisons (n=10 trees per treatment) obtained in qPCR analysis for time point T0 (day of injection), time points T21 and T56 (21 days and 56 days after injection) are given with the standard error of the means threshold cycle in FIG. 9 (T0=dark gray bars; T21=white bars; T56=light gray bars; threshold cycle averages marked with an "x"). All outliers are marked with small circles outside the standard error bars for each treatment. Control trees, or non-sprayed grapefruit trees, had the lowest cycle threshold values in the Ct range of about 25 for all treatment time points. For leaf samples from grapefruit trees that were sprayed with 1X and 10X Bt.4Q7Flg22 polypeptide formulations, slightly higher Ct values were obtained compared to leaves from control trees (FIG. 9). The higher the Ct. value, the greater the effect of the treatment to control or reduce the spread of CLas bacteria infection. The mean Ct value in leaves taken at T21 was higher than the Ct value in T56 samples, but both values were significantly higher than the values in leaves from control non-injected trees, or in leaves from trees that were injected with Bt polypeptide formulations. .4Q7Flg22 (FIG. 9, threshold cycle averages marked with an "x").

[0620] Another study on the Valencia orange (Citrus sinensis) was also performed in a commercial fruit grove located in central Florida (Okeechobee County). Injection treatments using formulations with Bt.4QFlg22 (SEQ ID NO: 226) were compared with antimicrobial polypeptides known as thionins. Thionin was injected as a mixture of thionin polypeptides (SEQ ID NOS: 651, 652 and 653) which are characterized as "unlabeled", or lacking a phloem localization sequence. Along with a mixture of unlabeled thionins, a "labeled" thionin polypeptide containing a sequence for localization to the phloem (SEQ ID NO: 650) was used as a comparative injectable treatment. A phloem-targeted or "labeled" variant was used to specifically target thionin to the phloem where CLas bacteria live and proliferate. Injection treatments of orange trees were performed using block randomization with full random distribution, on a total of 8 orange trees (8 years old) per treatment, for untreated controls and Bt.4QFlg22 agents, and on a total of 5 orange trees per treatment. each treatment for products with thionin. The injection was carried out in April (2017) at the stage of the first growth, from the appearance of leaves to their full size. Injection into orange trees was carried out using a low pressure injection device, BRANDTENTREE (BRANDT). All polypeptides: Bt.4Q7Flg22 at concentrations of 1X (0.138 μM) and 10X (1.37 μM), "unlabeled" and "labeled" thionine polypeptides were compared with trees that were not treated by injection (control). Leaf samples from orange trees were collected for each treatment at the time of injection (day 0) and at time T56, or 56 days after injection.

[0621] A total of six leaf samples per tree were selected to represent the population of leaves on the tree, including leaf age, location, and presence of visible symptoms. Each central vein was separated from the leaf blade and immediately cut into very small pieces with a new sterile razor blade. Then the leaf samples from each tree were placed in an individual test tube, which was then stored in a freezer at -80°C until further processing. DNA extraction and real-time polymerase chain reaction or quantitative PCR analysis (qPCR) on these leaves was performed at Southern Gardens Citrus (Cleviston, FL) using the methods described above to perform Ct analysis.

[0622] The results of the Valencia orange test are shown in FIG. 10 (T0=dark gray bars; T56=white bars). Leaf tissues from control orange trees exhibited minimum Ct cycle thresholds in the range of approximately 25-30 at T0 and T56 treatment time points, indicating that CLas bacteria titer levels were unchanged in these trees. Treatment with both "unlabeled" and "labeled" thionin showed higher mean cycle thresholds for leaves taken at time T56 compared to mean cycle thresholds for T56 leaves taken from water-injected controls (Fig. 10; threshold cycle averages are marked with an "x"). All outliers are marked with small circles outside the standard error bars for each treatment. Leaf samples from trees that were treated with a phloem-targeted thionin “labeled” agent had a higher mean Ct at time point T56 compared to leaves from trees that were treated with untargeted or “unlabeled” thionin. Leaf samples from orange trees treated with 1X and 10X Bt.4Q7Flg22 polypeptide injection formulations had significantly higher Ct at time points from T0 to T56, as indicated by a mean increase in Ct at T56 compared to T0 (FIG. 10 ; threshold cycle averages are marked with an "x"). Leaves from trees injected with both formulations of Bt.4Q7Flg22 polypeptides (1X and 10X) also showed significantly higher cycle thresholds compared to leaf samples from control trees. These Bt.4Q7Flg22 are effective means to control or reduce titer levels of CLas bacteria in infected orange trees (FIG. 9).

[0623] Both Bt.4Q7 Flg22 polypeptides, when applied as injectables at final concentrations of 1X (0.138 μM) and 10X (1.38 μM), were effective in reducing CLas titer levels in leaf tissue samples taken 8 weeks after injection . However, a higher concentration of Bt.4Q7Flg22 10X polypeptide (1.38 μM) was even more effective, providing a 37% reduction (Trial 1) and a 43% reduction (Trial 2) in CLas titer levels.

Table 84. Efficacy of Bt.4Q7Flg22 treatment to reduce titer levels of CLas bacteria 8 weeks after spray treatment of citrus plants (Valencia orange and Ruby Red grapefruit)

Injection concentration Percentage reduction in CLas titer normalized to control Trial 1 Trial 2 1X Bt.4Q7Flg22
(SEQ ID NO: 226),
calculated concentration in the vasculature of the tree 0.138 µM 33% 21% 10X Bt.4Q7Flg22 (SEQ ID NO: 226),
estimated concentration in tree vasculature 1.38 μM 37% 43%

[0624] Previous results show that Bt.4Q7Flg22 (SEQ ID NO: 226) promotes plant growth in all disease periods (Example 50). To evaluate the potential plant growth benefit of injecting Bt.4Q7Flg22 (SEQ ID NO: 226) into HLB-infected 'Valencia' orange and 'Ruby Red' grapefruit trees, current year growth was measured in May 2018 in the same trees that were treated with Bt.4Q7Flg22 injection in April 2017 and CLas bacterial titer was assessed in a commercial fruit grove located in central Florida (Okeechobee County). Each tree was visually assessed to identify areas of growth in the current season with green colored branches as opposed to older branches with more visible lignification, with a dark greenish brown to brown tint. Three representative incremental branches were selected from each tree and the distance in inches from the start of the green growth (oldest node) to the top of the youngest node was measured with a flexible tape measure. Data were collected for trees sprayed with 1X and 10X Bt.4Q7Flg22 (SEQ ID NO: 226) and for the untreated control, 8 trees per treatment in the Valencia orange test and 9-10 trees per treatment in the Valencia test. grapefruit "Ruby Red" (n=24-30 measurements per processing). In the 'Ruby Red' grapefruit trial, only one tree from the original trial (treatment group 1X Bt.4Q7Flg22) died, presumably due to hurricane damage in September 2017. For each trial, average new shoot length (inches) was calculated and normalized to untreated control (table 85).

Table 85: Bt.4Q7Flg22 Stem Injection Improves New Branch Growth in Valencia Orange and Ruby Red Grapefruit

Trial Treatment Average length of new shoots (inches) Length of new shoots (% of control) Orange "Valencia" - injection in April 2017, measured in May 2018 Control 7.23 100% 1X Bt.4Q7Flg22 (SEQ ID NO: 226), calculated concentration in tree vasculature 0.138 μM 13.33 184% 10X Bt.4Q7Flg22 (SEQ ID NO: 226), calculated concentration in tree vasculature 1.38 μM 12.29 170% Red grapefruit -
injection in April 2017, measurements in May 2018 Control 8.05 100% 1X Bt.4Q7Flg22 (SEQ ID NO: 226), calculated concentration in tree vasculature 0.138 μM 10.83 135% 10X Bt.4Q7Flg22 (SEQ ID NO: 226), calculated concentration in tree vasculature 1.38 μM 9.13 113%

[0625] These results demonstrate the additional ability of Flg22 compositions that provided a reduced titer of CLas bacteria compared to untreated plants (FIG. 9 and FIG. 10) to improve the growth of sweet orange and grapefruit trees (Table 85). Increased branch growth is an indicator of increased fruit yield as more leaves are produced to support fruit growth throughout the season. Compared to untreated controls, orange and grapefruit trees treated with 1X Bt.4Q7Flg22 spray in April 2017 had an average length of 6.1 inches (+85%) or 2.8 inches (+35%) longer new branches, respectively. A 10X dose of Bt.4Q7Flg22 injection was also effective in improving growth, providing 5.1 inches (70%) and +1.1 inches (+13%) more new branch growth in orange and grapefruit trees, respectively. Since 10X Bt.4Q7Flg22 injection was not more effective than 1X injection in enhancing growth in 2018, and bacterial titer reduction was similar in 2017, 1X Bt.4Q7Flg22 injection provides a sufficient response in plants. It is important to note that growth measurement showed no occurrence of phytotoxicity after stem injection of Flg22 at both 1X and 10X doses.

[0626] Since these plants were not 100% free of disease-causing bacteria, these results also demonstrate the ability to continue growing in plants treated by injection of Bt.4Q7Flg22 despite the presence of HLB-causing bacteria. Given the predicted emergence of antibiotic resistant CLas strains that will become an additional hurdle for HLB control, Flg22 injection represents a current alternative to antibiotic treatments to improve plant growth and reduce bacterial titer. The Flg22 sprayed trees in this example were cultivated using a standard commercial citrus treatment program, further demonstrating the ability to complement standard Flg22 spray growing practices in citrus plants.

Example 52 Foliar Treatment and Stem Injection of Flg22 Alone or in Combination with Antimicrobial or Plant Health Compounds Improves New Shoot Growth on Orange Trees

[0627] A follow-up trial in April (2018) applied Flg22 formulations by trunk spray or foliar spray at two independent test sites. A trial design was developed to 1) test synthetic and fermented variants of the Flg22 polypeptide, 2) compare the efficacy of the Flg22 variant previously used for injection in citrus in the 2017 trial, Bt.4Q7Flg22 (SEQ ID NO: 226), and Syn01Bt.4Q7Flg22 (SEQ ID NO: 571) which was effective as both foliar and seed treatment increasing yield in row crops, canopy, and 4) testing combinatorial treatments with Flg22 peptides, oxytetracycline injection, L-cysteine, and benzo(1,2,3)thiadiazole-7-thiocarboxylic acid S-methyl ester (also known as BTH) as a commercial formulation of ACTIGARD WG . L-cysteine is an essential proteinogenic amino acid; BTH is a salicylic acid analog with increased stability that is used in agriculture as an activator of immune responses in plants and is approved for use in citrus trees as a root zone impregnation or irrigation to prevent citrus cancer caused by Xanthomonas axonopodis, citri patovar .

[0628] In March 2018, trees were treated in two separate plots. Three year old 'Gamlin' orange (Citrus sinensis) trees were cultivated in a commercial fruit grove located in central Florida (Okeechobee County). A similar trial was carried out in a commercial grove of 6-year-old Vernia orange trees on Swingle Rootstock in Lake Wales, Florida (Polk County). Treatments were applied as described in Table 85 below using a low pressure injection device, BRANDT ENTREE (BRANDT), for trunk injection, or a pressurized CO2 knapsack sprayer converting the foliar spray into a fine mist. Stem injections were performed as described in Example 51. Bt.4Q7Flg22 foliar treatment compositions were diluted in water with a non-ionic surfactant (NIS from Precision Labs 90:10; 0.1% v/v of sprayer reservoir volume) and evenly applied. on the leaf canopy of a tree with a spraying agent consumption of 3 liters per tree. Blocks of trees treated with a foliar agent in the test area were separated by a "gap" (skipped tree) between treatment blocks to avoid transfer of treatments to adjacent treatment blocks. The treatment was carried out in the early morning or late evening during a period of light wind (<5 miles per hour); conditions were such that all sprays dried on the leaves within a period of 4 hours. The combination treatments described in Table 86 were either injected from a single bottle of BRANDT ENTREE (Citrus Composition 7, Citrus Composition 8) or applied alone as an oxytetracycline injection followed by a Bt.4Q7Flg22-Syn01 foliar treatment on the same day (composition for citrus fruits 11, composition for citrus fruits 12). For all treatments, 10 trees were used, divided into two replica blocks of five trees each. Citrus compositions 1-8 were used in groves in both Okeechobee and Polk County, while citrus compositions 9-12 were used only in Okeechobee grove.

Table 86. Treatment compositions tested for the ability to mitigate the effects of HLB in orange trees

Composition Compound Processing method Operating expense funds Composition for citrus fruits 1 Bt.4Q7Flg22 (SEQ ID NO: 226) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Injection into the barrel 2.75 ml/wood
(calculated concentration 0.138 µM in plant vessels) Composition for citrus fruits 2 Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Injection into the barrel 2.75 ml/wood
(calculated concentration 0.138 µM in plant vessels) Composition for citrus fruits 3 Bt.4Q7Flg22 (SEQ ID NO: 226) (ferment broth filtrate) with (+) enterokinase, 0.8 U/ml Injection into the barrel 80 ml/wood Composition for citrus fruits 4 Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) (ferment broth filtrate)
with (+) enterokinase, 0.8 U/ml Injection into the barrel 80 ml/wood Composition for citrus fruits 5 Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Foliar Spray 3.0 ml/tree in 3 L spray carrier including water + 0.1% v/v Precision Labs NIS 90:10 Composition for citrus fruits 6 Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Foliar Spray 12.0 ml/tree in 3 L spray carrier including water + 0.1% v/v Precision Labs NIS 90:10 Composition for citrus fruits 7 Part A
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Injection into the barrel 2.75 ml/wood
(calculated concentration 0.138 µM in plant vessels) Part B
ACTIGARD WG
(Active ingredient: 50% Acibenzolar-S-methyl: S-methyl ester
benzo(1,2,3)thiadiazole-7-
carbothioacids; BTH)
(solution in water 50 mg/ml) Injection into the barrel 20 ml/wood
(1 g per tree) Composition for citrus fruits 8 Part A
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Injection into the barrel 2.75 ml/wood
(calculated concentration 0.138 µM in plant vessels) Part B
L-cysteine
(solution in water 3 mg/ml) Injection into the barrel 20 ml/wood
(60 mg per tree) Composition for citrus fruits 10 Part A
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Foliar Spray 3.0 ml/tree in 3 L spray carrier including water + 0.1% v/v Precision Labs NIS 90:10 Part B
Oxytetracycline-HCl
(solution in water 22.5 mg/ml) Injection into the barrel 20 ml/wood
(0.45 g per tree) Composition for citrus fruits 11 Part A
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 100 μM,
10 mM sodium phosphate buffer, pH 5.7 Foliar Spray 12.0 ml/tree in 3 L spray carrier including water + 0.1% v/v Precision Labs NIS 90:10 Part B
Oxytetracycline-HCl
(solution in water 22.5 mg/ml) Injection into the barrel 20 ml/wood
(0.45 g per tree)

[0629] To assess the potential plant growth benefit of treating HLB-infected orange trees by injection or spraying with different formulations with Flg22 polypeptides alone or in combination with antimicrobial or plant health promoting compounds, new shoot length was measured in May 2018 in trees treated with in March 2018 at Commercial Groves in Okeechobee and Polk Counties, Florida. During the treatment period at both locations (March 2018), dark green leaves grew on the trees and fruits of the 2018 season began to develop. During the two-month interval between treatments (March 2018) and during the tree measurement period (May 2018). ) trees entered the spring growth period with visible growth in the form of very light green flexible branches with the same light green leaves. Each tree was evaluated for the presence of new shoots, and three representative growth branches were selected from each tree. The distance in inches from the start of the light green growth (oldest node) to the top of the youngest node was measured with a flexible tape measure. Data were collected for 10 trees per treatment, including untreated controls, for a total of 30 measurements per treatment. Table 86 shows the average new shoot length (inches) for each treatment at both plots in groves in Okeechobee and Polk counties; growth normalized to untreated control.

Table 87: Flg22 variants, when used as a stem spray or foliar spray, improve new branch growth in 'Gamlin' and 'Vernia' orange trees

Treatment Average new shoot length (inches) Length of new shoots (% of control) Raw control 3.08 100% Composition for citrus fruits 1
Bt.4Q7Flg22 (SEQ ID NO: 226),
Injection at 2.75 ml/tree 3.84 125% Composition for citrus fruits 2
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571)
Injection at 2.75 ml/tree 4.48 146% Composition for citrus fruits 3
Bt.4Q7Flg22 (SEQ ID NO: 226)
enterokinase (EK) activated filtrate, injection 80 ml/tree 5.18 169% Composition for citrus fruits 4
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571)
enterokinase (EK) activated filtrate, injection 80 ml/tree 3.28 107% Composition for citrus fruits 5
Foliar spray with Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 1X 3.66 119% Composition for citrus fruits 6
Foliar spray with Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571) 4X 3.76 122%

[0630] New shoot growth measurements of 'Gamlin' and 'Vernia' taken two months later either after injection into the trunk or after application of a foliar spray with Flg22 variants showed that both Bt.4Q7Flg22 (SEQ ID NO: 226) , and Syn01Flg22 (SEQ ID NO: 571) are effective in promoting enhanced growth compared to the untreated control. On average, shoot length on the untreated control was 3.08 inches, while trees injected with Bt.4Q7Flg22 had 25% longer shoots (3.84 inches) and trees injected with Syn01Flg22 146% (4.48 inches). Bt.4Q7Flg22 and Syn01Flg22 produced using the fermentation methods described in Example 49 also effectively increased shoot growth when injected into the stem at a rate of 80 ml/tree. Citrus formulation 3 containing Bt.4Q7Flg22, obtained by fermentation of strain H101 and treatment with 0.8 U/mL enterokinase (New England Biolabs; product code P8070), was the most effective, producing longer shoot lengths, averaging 169% (5, 18 inches) from the raw control.

[0631] Foliar application of Flg22 variants effective in promoting growth of disease-bearing kiwi, soybeans, lentils, and potatoes was also tested for the ability to promote the growth of HLB-infected orange trees. Table 88 shows that citrus compositions 5 and 6, consisting of 1X or 4X doses of Syn01Bt.4Q7Flg22 (SEQ ID NO: 571), respectively, are also effective in promoting new shoot growth on orange trees. The 1X and 4X doses were similarly effective, with the 1X leaf treatment resulting in longer shoot lengths as measured, 119% of control, and the 4X treatment providing greater shoot length, as measured, 122% of control. These results indicate that foliar application of the Flg22 polypeptide can be used as part of a standard tree care program in citrus groves.

Table 88 Injection of Bt.4Q7Flg22-Syn01 in combination with plant health promoting compounds improves new branch growth in 'Gamlin' and 'Vernia' orange trees

Treatment Average new shoot length (inches) Length of new shoots
(% of control) Raw control 3.08 100% Composition for citrus fruits 2
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571)
Injection at 2.75 ml/tree 4.48 146% Composition for citrus fruits 7
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571)
Injection at 2.75 ml/tree
+ BTH (ACTIGARD WG; injection at 1 g/tree) 3.44 112% Composition for citrus fruits 8
Bt.4Q7Flg22-Syn01 (SEQ ID NO: 571)
Injection at 2.75 ml/tree + L-Cysteine (injection at 60 mg/tree) 5.87 191%

[0632] The combination of Syn01Bt.4Q7Flg22 (SEQ ID NO: 571) with BTH (ACTIGARD WG) or L-cysteine in both Melvin and Lake Wales Grove was then investigated. shoots compared to an untreated control, showing that Flg22 polypeptides can be used in combination with amino acids, plant hormones, or plant hormone mimetics to improve the health of citrus trees.

Table 89 Use of Bt.4Q7Flg22-Syn01 Foliar Spray in Combination with Oxytetracycline Injection Increases New Branch Growth in 3 Year Old Gamlin Orange Trees

Processing (see table 85) Average new shoot length (inches) Length of new shoots
(% of control) Raw control 1.67 100% Composition for citrus fruits 9
Oxytetracycline-HCl
(0.45 g/wood)
+ foliar spray Syn01Bt.4Q7Flg22 (SEQ ID NO: 571) 1X 3.80 228% Composition for citrus fruits 10
Oxytetracycline-HCl
(0.45 g/wood)
+ foliar spray Syn01Bt.4Q7Flg22 (SEQ ID NO: 571) 4X 3.32 199%

[0633] In a separate trial, the combination was followed by treatment with Syn01Flg22 (SEQ ID NO: 571) and oxytetracycline. On the same day that the trees were sprayed with oxytetracycline, groups of 10 trees were also sprayed with Syn01Flg22 foliar application at 1X or 10X. These results show that antibiotic and polypeptide treatments are compatible and no phytotoxicity was observed as a result of dual treatments. A standard program could be developed in which growers would alternate spraying into trees and foliar treatments to improve control of HLB symptoms and to reduce CLas titer.

Example 53 Disease Protection Using Bt.4Q7Flg22 and Gm.RHPP Foliar Applications in Soybean Plants for Protection Against Diseases Caused by Phakopsora pachyrhizi and Cercospora kikuchii

[0634] Table 90 describes the compositions and corresponding operating flow tested in the example below.

Table 90. Foliar application of Bt.4Q7Flg22 and Gm.RHPP in soybeans protects plants from Phakopsora pachyrhizi and Cercospora kikuchii

Composition Composition for foliar application Operating expense funds
in fluid ounces per acre, or milliliters per hectare (mL/ha) Composition 12 FOX fungicide 5.48 fl oz per acre, or 400 ml/ha Track 13 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT) 2.05 fl oz per acre, or 150 ml/ha Composition 14 Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT) 4.11 fl oz per acre, or 300 ml/ha Composition 15 Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 2.05 fl oz per acre, or 150 ml/ha Composition 16 Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 4.11 fl oz per acre, or 300 ml/ha Composition 17 FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha Composition 18 FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT) 5.48 fl oz per acre, or 400 ml/ha +
4.11 fl oz per acre, or 300 ml/ha Composition 19 FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha Composition 20 FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT) 5.48 fl oz per acre, or 400 ml/ha +
300 ml/ha

*Foliar treatment compositions contained 0.1% (v/v) PROXEL BC preservative, an aqueous dispersion of a mixture of 330.7 mM 1,2-benzisothiazoline (BIT), 53.5 mM 5-chloro-2-methyl-4-isothiazoline- 3-one (CMIT) and 26.1 mM 2-methyl-4-isothiazolin-3-one (MIT). Foliar formulations were applied at a given rate (in fluid ounces per acre, or ml/ha) in a carrier volume of 150 L/ha, or 16 gal per acre of water with 0.5% (v/v) AUREO surfactant, methylated soybean oil (composition 13) or with 0.33% (v/v) Agris Parrafinic mineral oil (stock concentration 795 g/l or 79.5% (w/v) (compositions 13-20).

[0635] Field replicates were tested at three locations in Paraguay (Yatitai, Obligado, and Captain Miranda) using a foliar application containing compositions of Bt.4Q7Flg22 polypeptide and RHPP polypeptide supplemented with a broad spectrum fungicide, Fox (16.0 % prothioconazole and 13.7% trifloxystrobin). FOX is a foliar fungicide commercially available in South America with limited efficacy for the preventive and curative treatment of Asian soybean rust caused by Phakopsora pachyrhizi and soybean leaf damage caused by Cercospora kikuchii, applied as a foliar spray following the recommendations in instructions for use of the drug, with an operating rate of 5.48 fl oz per acre (400 ml/hectare). From the R1 developmental stage, soybean plants were treated twice with foliar applications with the compositions described in Table 90, with an interval of 13-14 days between sprays. Foliar treatments were applied to one soybean cultivar (which cultivar? same cultivar for all 3 plots) in three plots with 4 rep plots (3×10 meters, 30 m ² ; minimum 6 rows per treatment). When assessing disease in naturally occurring infection trials, infection severity (0-100% leaf infestation) was rated for 10 plants at each site for both Phakopsora pachyrhizi soybean rust and Cercospora kikuchii soybean leaf damage at the soybean development stage R4-R5 (4-15 days after the second foliar application) according to Godoy et al (1997; Journal of plant diseases and protection 104:336-345). The percentage of phytotoxicity (0-100% affected foliage) was also recorded at the soybean development stage R4-R5. The severity of infection and phytotoxicity were averaged over all four replicates at each site (12 replicates in total, 3 sites with 4 replicates each). The standard deviation was calculated for each treatment at all three plots. Untreated control plants at the Yatitai site experienced 99% leaf shedding 11 days after application of the second foliar treatment; at this point, leaf shedding rates (deleafization 0-100%) were recorded. The results of monitoring disease severity, phytotoxicity and leaf shedding are shown in Table 91 as percentages with the standard deviation shown in parentheses.

Table 91 Frequency of symptoms of Asian soybean rust following foliar application of fungicide and polypeptide formulations in Paraguay

Composition for foliar application Operating expense funds
in fluid ounces per acre
milliliters per hectare (ml/ha) Frequency of symptoms of Asian soybean rust after 2 foliar applications (% of foliage affected); N=12 replicas per processing Change in symptoms of Asian soybean rust relative to control (%); N=12 replicates per treatment Leaf shedding (% foliage) after 2 foliar applications (Yatitai only; N=4 replications per treatment) Raw control n/a 35.1% (±13.8%) -- 99% FOX fungicide
(track 12) 5.48 fl oz per acre, or 400 ml/ha 19.4% (±10.3%)
(-15.7%) -15.7% 45% Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
Preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 13) 2.05 fl oz per acre, or 150 ml/ha 22.7% (±14.4%) -12.4% 70% Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 14) 4.11 fl oz per acre, or 300 ml/ha 22.1% (±14.6%) -13.0% 60% Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 15) 2.05 fl oz per acre, or 150 ml/ha 24.6% (±13.4%) -10.5% 96% Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 16) 4.11 fl oz per acre, or 300 ml/ha 23.8% (±11.5%) -11.3% 70% FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 17) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha 9.3% (±3.9%) -25.8% 25% FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 18) 5.48 fl oz per acre, or 400 ml/ha +
4.11 fl oz per acre, or 300 ml/ha 8.0% (±5.1%) -27.1% 25% FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 19) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha 8.3% (±5.8%) -26.8% 25% FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 20) 5.48 fl oz per acre, or 400 ml/ha +
300 ml/ha 11.0% (±3.3%) -24.1% 25%

Table 92. Frequency of symptoms of leaf cercosporiosis after foliar application of fungicide and polypeptide compositions in Paraguay

Composition for foliar application Operating expense funds
in fluid ounces per acre
milliliters per hectare (ml/ha) Incidence of symptoms caused by Cercospora after 2 foliar applications (% of affected foliage); N=12 replicas per processing Change in symptoms caused by Cercospora relative to control (%); N=12 replicates per treatment Raw control n/a 19.3% (±5.1%) -- FOX fungicide
(track 12) 5.48 fl oz per acre, or 400 ml/ha 15.0% (±9.6%) -4.3% Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXELBC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 13) 2.05 fl oz per acre, or 150 ml/ha 16.4% (±7.7%) -2.8% Bt.4Q7Flg22 (SEQ ID NO: 226)
16.7 µM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXELBC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 14) 4.11 fl oz per acre, or 300 ml/ha 15.8% (±6.3%) -3.5% Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXELBC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 15) 2.05 fl oz per acre, or 150 ml/ha 15.9% (±6.9%) -3.3% Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXELBC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 16) 4.11 fl oz per acre, or 300 ml/ha 14.8% (±5.3%) -4.5% FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXELBC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 17) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha 10.6% (±3.9%) -8.7% FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXELBC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 18) 5.48 fl oz per acre, or 400 ml/ha +
4.11 fl oz per acre, or 300 ml/ha 10.6% (±4.4%) -9.2% FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 μM (MIT) (composition 19) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha 11.3% (±4.2%) -8.0% FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 20) 5.48 fl oz per acre, or 400 ml/ha +
300 ml/ha 11.3% (±4.2%) -8.0%

Table 93 Phytotoxicity after Foliar Application of Fungicide and Polypeptide Compositions in Paraguay

Composition for foliar application Operating expense funds
in fluid ounces per acre
milliliters per hectare (ml/ha) Phytotoxicity (% affected foliage) after 2 foliar applications; N=12 replicas per processing Raw control n/a 0.00% (±0.00%) FOX fungicide
(track 12) 5.48 fl oz per acre, or 400 ml/ha 2.25% (±32.9%) Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 13) 2.05 fl oz per acre, or 150 ml/ha 0.00% (±0.00%) Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 14) 4.11 fl oz per acre, or 300 ml/ha 0.00% (±0.00%) Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 15) 2.05 fl oz per acre, or 150 ml/ha 0.00% (±0.00%) Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 16) 4.11 fl oz per acre, or 300 ml/ha 0.00% (±0.00%) FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 17) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha 2.33% (±0.14%) FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 18) 5.48 fl oz per acre, or 400 ml/ha +
4.11 fl oz per acre, or 300 ml/ha 2.25% (±0.25%) FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 19) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha 2.42% (±0.29%) FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 20) 5.48 fl oz per acre, or 400 ml/ha +
300 ml/ha 2.17% (±0.29%)

[0636] Foliar application of Bt.4Q7Flg22 and Gm.RHPP during the reproductive phases of soybean development provided increased protection against soybean Asian rust and leaf cercosporiosis compared to untreated controls. Plants treated with foliar application with Bt.4Q7Flg22 at a flow rate of 150 and 300 ml/ha showed a 12.4-13.0% lower area of leaf damage by Asian soybean rust and a 2.8-3.5% lower area of leaf damage Cercospora compared to untreated control; and in the treated foliar application with Gm.RHPP at a flow rate of 150 and 300 ml/ha of plants, a 10.5-11.3% smaller area of damage to the leaves of Asian soybean rust and a 3.3-4.5% smaller area of damage were observed leaves of Cercospora compared to untreated control. Combination treatments comprising either Bt.4Q7Flg22 or RHPP with FOX fungicide increased protection against Asian soybean rust and Cercospora relative to Fox fungicide treatment alone. At the site in Yatitai at the R7 developmental stage, less leaf shedding was observed due to severe disease symptoms when treated with Bt.4Q7Flg22 or Gm.RHPP +/- FOX fungicide. While the untreated control was 99% leafless at this stage, treatment with Bt.4Q7Flg22 at 150 or 300 ml/ha reduced leaf shedding to 70% or 60%, with green leaves still visible, respectively. Gm.RHPP treatment at 150 or 300 ml/ha reduced leaf shedding by up to 96% or 70%, respectively. A combination treatment of Bt.4Q7Flg22 or Gm.RHPP with FOX fungicide reduced leaf shedding by up to 25% with visible green leaves, while Fox fungicide alone only reduced leaf shedding by up to 45% with no visible green leaves. In general, treatment with polypeptides provided increased protection relative to FOX fungicide alone for the control of Asian soybean rust and Cercosporiosis leaves. None of the polypeptide agents alone showed phytotoxicity; the phytotoxicity of the combination of either polypeptide with the FOX fungicide also did not significantly increase or decrease relative to the FOX fungicide alone (Table 93).

Example 54 Flg22-PSA foliar application in kiwi fruit protects plants from Pseudomonas syringae, patovar actinidiae (PSA-V)

[0637] Pseudomonas syringae, patovar actinidiae (PSA) is a devastating plant pathogen that causes bacterial canker of both green (Actinidiae deliciosa) and yellow (Actinidiae chinesis) kiwifruit in all kiwifruit production areas, resulting in severe crop losses in New Zealand, China and Italy. In New Zealand alone, the cumulative loss of revenue from the most destructive biovar PSA-V is projected to approach $740 million New Zealand dollars (NZD) by 2025 (Lincoln University Agricultural Business and Economics Research Institute "The cost of Psa-V to the New Zealand kiwifruit industry and more the wider community”; May 2012). PSA-V colonizes the outer and inner surfaces of kiwi fruit and can spread through xylem and phloem tissues. Symptoms of PSA-V disease in kiwi fruit include bacterial leaf spot, bacterial stem cancer, red exudates, flower rot, branch discoloration, and eventually dieback of kiwi vines. The current standard of care for PSA-V is frequent foliar treatment of kiwifruit vines with metallic copper, which is predicted to select for the copper-resistant form of the pathogen and cause the disease to be out of control. There is an urgent need for new methods of control.

[0638] To test the sensitivity of kiwifruit leaves to 22-amino acid fragments of flagellin, 1 mm pieces were cut from leaf petioles of Actinidiae deliciosa cultivar "Hayward" kiwifruit leaves and placed on the surface of 150 μl of water in the wells of a 96-well plate, one piece per well. Received Flg22 polypeptides from table 94 for analysis, resuspending the lyophilized polypeptide in deionized water to a concentration of 10 mm; then serial dilutions of the peptides were prepared to 10 μM in 100 mM sodium phosphate (pH 7.8-8.0) buffer with 0.1% Tween-20. After 20 hours, water was removed from the kiwi leaf petiole samples and replaced with 100 µl elicitation solution containing 100 nM peptide (diluted from 10 µM stock solution), 34 µg/ml luminol and 20 µg/ml horseradish peroxidase in deionized water. Recognition of the Flg22 polypeptide by plant tissue resulted in the activation of immune signaling and the production of apoplastic reactive oxygen species (ROS). In the presence of ROS (H2O2), horseradish peroxidase catalyzed the oxidation of luminol and the generation of visible light. Relative light units (RLU) were recorded with a SpectraMax L luminometer (integration 0.5 s; intervals 2.0 min) over a time period of 40 minutes. In two independent experiments, a total of 6 kiwi leaf petiole samples were treated with each Flg22 polypeptide from Table 94. For each treatment, the mean total RLUs and standard error of the mean (SEM) were calculated. Two-tailed T-test was used to determine the significance of differences between treatments at 90% confidence level (P<0.1). For each polypeptide, the relative ROS production was determined compared to the total RLU for the 100 nM Bt.4Q7Flg22 control.

Table 94. Kiwi leaf petioles are most sensitive to Flg22-PSA

Treatment Average total relative light units (RLU); SEM in parentheses P-value for comparison with 100 nM Bt.4Q7Flg22 ROS production relative to Bt4Q7Flg22 (%) 100 nM Bt.4Q7Flg22-
(SEQ ID NO: 226) 47.457
(±12,900) n/a 100% 100 nM Syn01Flg22
(SEQ ID: 571) 81.848
(±27.631) p=0.286 172% 100 nM Flg22-PSA
(SEQ ID: 540) 124.550
(±33.555) p=0.058* 262%

*Significant difference at 90% confidence level

[0639] In two independent experiments, 'Hayward' kiwi leaf petioles were significantly more sensitive to Flg22 derived from Pseudomonas syringae, patovar actinidiae (Flg22-PSA; SEQ ID NO:540) compared to Flg22 derived from Bacillus thuringiensis strain 4Q7 (Bt.4Q7Flg22; SEQ ID NO: 226). Although ROS production was increased in kiwi leaf petioles in response to synthetic Syn01Flg22 (SEQ ID NO: 571) compared to Bt.4Q7 Flg22 (SEQ ID NO: 226), this difference was not significant. Based on these results, a formulation with Flg22-PSA (SEQ ID NO: 540) was prepared as indicated at a final concentration of 100 nM (Table 94) for the 'Hayward' kiwi plant disease prevention trial in New Zealand in container culture.

Table 95. Treatment options in kiwifruit container culture trials

Composition Composition for foliar application Dilution of product for spraying,
in milliliters of product/liter of water (ml/l), or in
grams of product/liter of water (g/l) Composition 21 ChampION++™ (46.1% copper hydroxide; equivalent to 30% metallic copper) 0.9 g ChampION++™ /l water Composition 22 Flg22-PSA (SEQ ID NO: 540) 100 µM
10 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT) 4 ml/l water

[0640] The leaf treatment compositions contained 0.1% (v/v) PROXEL BC preservative, an aqueous dispersion of a mixture of 330.7 mM 1,2-benzisothiazoline (BIT), 53.5 mM 5-chloro-2-methyl-4- isothiazolin-3-one (CMIT) and 26.1 mM 2-methyl-4-isothiazolin-3-one (MIT). The foliar treatment compositions were diluted to predetermined concentrations in water (g/l water or ml/l water) with 0.05% (v/v) Contact Xcel™ nonionic surfactant. The diluted products were applied in the form of microdroplets using a pneumatic knapsack sprayer to the foliage of each plant until it was completely covered.

[0641] To evaluate the efficacy of Flg22-PSA (SEQ ID NO: 540) for the control of Pseudomonas syringae, patovar actinidiae (PSA-V), HortEvaluation Ltd, in collaboration with NuFarm Limited, conducted a test on a diseased kiwifruit container culture in the Bay of Plenty in New Zealand. Kiwifruit plants Actinidiae deliciosa 'Hayward' in containers without PSA-V symptoms were evenly distributed among 6 treatment groups, 12 container plants per group. The day before PSA-V inoculation, containerized plants were treated with ChampION++TM, the industry standard for PSA-V control, or Flg22-PSA formulation according to the operating rate from Table 96 (treatment groups 3,4) at the nursery in Te Puka, New Zealand. After 24 hours, all plants, except non-infected controls, were sprayed with 1 x 108 cfu/ml PSA-V inoculum with a 5 liter handheld air sprayer pointed at the underside of the leaves until the foliage was completely covered. Uninfected controls were sprayed separately with water. The containerized plants were then transported to Pekaina and placed in an overhead spray field for 48 hours, simulating environmental conditions for PSA-V infection, with uninfected control plants separated from infected plants. After 48 hours, a subset of plants were removed from the spray area and allowed to dry briefly. After the last treatment, all plants were moved to the final outdoor test site, at randomized locations in Pecaine. The average daily temperature at the test site was 20.75°C with a total rainfall of 277 mm over 34 days. In addition, each plant was watered with drip irrigation twice a day, each time for two hours. Environmental conditions were favorable for the progression of PSA-V disease symptoms. Plants were visually monitored throughout the trial period to assess PSA-V disease, with the same expert assessing % spotted leaf area at 6 days post-inoculation (6 DPI), 16 DPI, 23 DPI, and 29 DPI. In addition, the phytotoxic effects of the treatment were assessed on each plant at 29 DPI on a scale of 0 to 10, where 0=no leaf phytotoxicity and 10=symptoms of very severe leaf phytotoxicity. Mean disease scores at 6, 16, 23 and 29 DPI and phytotoxicity score at 29 DPI are shown in Table 96 for each treatment (n=12 plants per treatment). For each treatment, p-values were calculated for comparison with an untreated control.

Table 96. Flg22-PSA Foliar Application Reduces Symptoms of PSA-V Disease in Kiwifruit

No. processing group / Composition for foliar application Application consumption and processing time Foliage affected (% leaf surface area);
p-values for comparison with untreated control 6 DPI 16 DPI 23 DPI 29 DPI Treatment group 1
Uninfected plants n/a 0.00% 1.66% 7.89% 18.14% Treatment group 2
Raw control n/a 15.12% 40.36% 54.64% 67.82% Treatment group 3
ChampION++™ (track 21) 0.9 g/l;
One day before inoculation 3.23%
(p<0.001) 12.48%
(p<0.001) 16.57%
(p<0.001) 25.20%
(p<0.001) Treatment group 4
Flg22-PSA (composition 22) 4 ml/l;
One day before inoculation 7.31%
(p<0.001) 29.41%
(p=0.013) 45.97%
(p=0.085) 61.91%
(p=0.190)

[0642] Application of Flg22-PSA significantly reduced PSA-V leaf spot symptoms (P<0.1; 90% CI) by 6, 16 and 23 DPI compared to untreated control. The Flg22-PSA pre-treatment combination further reduced the severity of leaf spot compared to Flg22-PSA alone at all time points assessed, and extended the period of significant protection to 29 DPI (14.3% less leaf spot compared to untreated control; P= 0.002). Thus, Flg22-PSA can be used both as a stand-alone treatment and in combination with other treatments aimed at limiting the growth of the pathogen. While the industry standard, ChampION++TM, the currently used copper-based PSA treatment, results in negligible leaf phytotoxicity (mean = 1.6), no significant phytotoxicity was observed for agents 3-4 (Table 97) . Flg22-PSA can be used as an alternative to other phytotoxic treatments.

Table 97. FLG22-PSA foliar application does not result in phytotoxicity in kiwi leaves

No. processing group / Composition for foliar application Application consumption and processing time Average phytotoxicity index (0-10); 29 DPI Treatment group 1
Uninfected plants n/a 0.0 (±0.0) Treatment group 2
Raw control n/a 0.0 (±0.0) Treatment group 3
ChampION++™ (track 21) 0.9 g/l;
One day before inoculation 1.6 (±0.9) Treatment group 4
Flg22-PSA (composition 22) 4 ml/l;
One day before inoculation 0.1 (±0.3)

Example 55: Polypeptides derived from elongation factor Tu

[0643] Elf18 and Elf26 polypeptides derived from the Bacillus cereus elongation factor-TU (EF-Tu) consensus protein were tested for their ability to elicit an ROS response in corn (hybrid 5828 YX), soybean (cv. Morsoy), and Arabidopsis thaliana. The polypeptides were synthesized at Genscript USA (Piscataway, New Jersey) using standard solid phase synthesis methods and provided as a lyophilized powder equal to or greater than 70% purity. The dry powder was resuspended to a concentration of 10 mM in ultrapure water, and then serial dilutions were made in ultrapure water with the concentrations tested in the ROS assay from Table 98.

[0644] For ROS analysis, 4-week-old Arabidopsis plants are leaf-cut, and 4 mm disks are cut from the leaves using a cork drill. Each disk is cut in half with a razor blade, after which each half of the disk is placed on the surface of 150 μl of water in the well of a 96-well plate with the abaxial side touching the water and left overnight. The next day, just prior to polypeptide treatment, water was removed from all wells. RLU values and relative ROS activity were recorded as means of 4 measurements. ROS activity assays were performed using the methods previously described in Example 15). The results for ROS activity are shown in Table 97 below.

Table 98 Elf18 and Elf26 polypeptides from Bacillus cereus

Description of the EF-Tu polypeptide Amino acid sequence length Subsequence N-terminus EF Tu (modified)
Bacillus cereus
(SEQ ID NO: 616) eighteen Ac-AKAKFERSKPHVNIGTIG-conh2 N-terminus EF Tu
(modified)
Bacillus cereus
(SEQ ID NO: 617) 26 Ac-AKAKFERSKPHVNIGTIGHVDHGKTT-conh2

Table 99. Comparison of ROS activity for elf18 and elf26 polypeptides in Arabidopsis leaf tissue

Processing with polypeptides Average RLU
(Magnification factor (X) relative to false processing) Negative control (water) 82896 (1X) N-terminus EF Tu (100 nM) (SEQ ID NO: 616) 264194 (3.2X) N-terminus EF Tu (100 nM) (SEQ ID NO: 617) 211383 (2.5X) Bt.4Q7Flg22 (100 nM) (SEQ ID NO: 226) 258073 (3.1X) N-terminus EF Tu (100 nM) (SEQ ID NO: 616)
+ Bt.4Q7Flg22 (100 nM) (SEQ ID NO: 226) 254344 (3.1X) N-terminus EF Tu (100 nM) (SEQ ID NO: 617) +Bt.4Q7Flg22 (100 nM) (SEQ ID NO: 226) 181504 (2.2X)

[0645] The EF-Tu polypeptide receptor, EF-Tu receptor (EFR), has been previously identified in the Brassica clade, for which the model plant is Arabidsopis thaliana. The results in Table 99 show that the newly identified polypeptides from Bacillus cereus EF-Tu (SEQ ID NO: 616 and SEQ ID NO: 617) can be used to stimulate an ROS response similar in magnitude to Bt.4Q7Flg22 (SEQ ID NO: 226) , when testing each of them at a concentration of 100 nM. Compared to the mock-treated control, the N-terminal EF-Tu polypeptides gave a 3.2-2.5-fold higher response, while Bt.4Q7Flg22 provided a 3.1-fold increase relative to the mock-treated control. These results indicate that 18 and 26 amino acid fragments from the N-terminus of Bacillus cereus polypeptides can be applied in a similar manner to Bt.4Q7Flg22 in Brassica cultures, including, but not limited to, kale, cabbage, kale, cauliflower, Brussels sprouts , savoy cabbage, kohlrabi and gallon, to increase plant biomass, yield and prevent diseases.

[0646] Combined treatments with N-terminal EF-Tu peptides (SEQ ID NO: 616 and SEQ ID NO: 617) and Bt.4Q7Flg22 (SEQ ID NO: 226) provided similar ROS responses to EF-Tu peptides separately, indicating that the combined treatment of these peptides in the field does not interfere with activity; however, since subsequent signaling events for the EF-Tu and Flg22 peptides recognized by the EFR and FLS2 receptors, respectively, involve common mechanisms, the spaced application of peptide agents may provide the maximum benefit for plant growth.

Example 56 Disease Protection Using Bt.4Q7Flg22 and Gm.RHPP Foliar Applications in Soybean Plants for Protection Against Diseases Caused by Phakopsora pachyrhizi and Cercospora kikuchii

[0647] It has previously been found that foliar application of Bt.4Q7Flg22 (SEQ ID NO: 226) and Gm.RHPP (SEQ ID NO: 600) in the reproductive phases of soybean development reduces disease symptoms in infections caused by Phakopsora pachyrhizi and Cercospora kikuchii (example 53). These plants were harvested; foliar application of Bt.4Q7Flg22 (SEQ ID NO: 226) and Gm.RHPP (SEQ ID NO: 600) was found to increase yield compared to untreated controls in a replicate trial in Paraguay, on plants that were infected with Asian rust soybeans and cercosporiosis leaves. Foliar application of Bt.4Q7Flg22 at 150 and 300 ml/ha increased yield by +342.2 kg/ha and +427.2 kg/ha, respectively, in trials where the average yield for untreated plants was 1266.3 Kg/ha . Yield increase with Bt.4Q7Flg22 foliar application at 300 ml/ha (36.1%) was comparable to FOX fungicide alone (36.6%), demonstrating the effectiveness of Bt.4Q7Flg22 as a foliar fungicide in both reducing symptoms of the disease, and to stimulate productivity. Relative yields at all three test sites in plants treated with the combination agent with FOX fungicide and Bt.4Q7Flg22 were slightly higher than when treated with FOX fungicide or foliar application with Bt.4Q7Flg22 alone, demonstrating treatment compatibility. Gm.RHPP foliar applications at 150 and 300 ml/ha further increased yield by +294.2 kg/ha and 506.8 kg/ha, respectively, compared to the untreated control. When used in combination with the FOX fungicide, Gm.RHPP provided maximum protection against the disease in these tests, as evidenced by an increase in yield by +517.6 kg/ha and +539.9 kg/ha at a consumption of 150 ml/g with Gm.RHPP. ha and 300 ml/ha, respectively. Foliar application of Gm.RHPP has consistently improved plant health and increased yield, so Gm.RHPP is an effective agent for promoting growth and resistance to fungal disease.

Table 100. Soybean yield in multiple replication field trials treated with Bt.4Q7Flg22 or RHPP infected Phakopsora pachyrhizi and Cercospora kikuchii plants

Composition for foliar application Operating rate in fl. ounces per acre/
milliliters per hectare (ml/ha) Mean change in yield compared to untreated control [1266.3 kilograms/hectare (Kg/ha)]; N=12 replicas per processing Yield relative to untreated control (%); N=12 replicas per processing Raw control n/a -- 100% FOX fungicide
(track 12) 5.48 fl oz per acre, or 400 ml/ha +445.6 kg/ha 136.6% Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 13) 2.05 fl oz per acre, or 150 ml/ha + 342.2 kg/ha 130.7% Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 14) 4.11 fl oz per acre, or 300 ml/ha + 427.2 kg/ha 136.1% Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 15) 2.05 fl oz per acre, or 150 ml/ha + 294.2 kg/ha 125.5% Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 16) 4.11 fl oz per acre, or 300 ml/ha + 506.8 kg/ha 143.5% FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 μM (MIT)
(track 17) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha + 426.5 kg/ha 138.4% FOX + fungicide
Bt.4Q7Flg22 (SEQ ID NO: 226) 16.7 μM,
1.67 mM sodium phosphate buffer, pH 5.7,
preservative PROXEL BC: 330.7 μM (BIT); 53.5 μM (CMIT); 26.1 µM (MIT)
(track 18) 5.48 fl oz per acre, or 400 ml/ha +
4.11 fl oz per acre, or 300 ml/ha + 418.5 kg/ha 137.2% FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 19) 5.48 fl oz per acre, or 400 ml/ha +
2.05 fl oz per acre, or 150 ml/ha + 517.6 kg/ha 145.5% FOX + fungicide
Gm.RHPP (SEQ ID NO: 600) 100 μM,
preservative PROXEL BC: 330.7 μM; 50.1 μM (CMIT); 21.71 µM (MIT)
(track 20) 5.48 fl oz per acre, or 400 ml/ha +
300 ml/ha + 539.9 kg/ha 146.9%

Example 57 Flg22 Treatment of Candidatus Liberibacter asiaticus Infected Citrus Trees Increases Fruit Set

[0648] Previous results summarized in Example 51 show that stem injection of Bt.4Q7Flg22 (SEQ ID NO: 226) reduces pathogen titers and promotes new growth on citrus trees infected with Candidatus Liberibacter asiaticus, the causative agent of Huanglong disease (HLB) . To assess the potential increase in fruiting and obtain preliminary estimated yield values, the fruit population was measured in June 2018 from the same HLB-infected trees of Valencia orange (harvest in spring 2019) and grapefruit 'Ruby Red' (harvest in autumn 2018). ) that had Bt.4Q7Flg22 injected into their trunk in April 2017 at a commercial fruit grove located in central Florida (Okeechobee County). As described in Example 51, trees were sprayed in April 2017 with either 1X Bt.4Q7Flg22 - low consumption (0.55 µmol peptide; calculated phloem concentration 0.138 µM) or 10X Bt.4Q7Flg22 - high consumption (5.5 µmol peptide; the calculated concentration in the phloem is 1.38 μM). In June 2018, trees sprayed with Bt.4Q7Flg22 were compared with untreated control trees in the same area of the grove using established citrus yield planning methods (“Forecasting Florida Citrus Production: Methodology &Development;1971; by S. R. Williams, for Florida Crop and Livestock Reporting Service). To quantify the fruit population on each tree, three quarter branches at eye level were randomly selected (n=8 trees/treatment for Valencia orange, n=10 trees/treatment for Ruby Red grapefruit). The perimeter of each quaternary branch at the junction where said branch began was measured and used to calculate the cross-sectional area (CSA) of the branch using the following equations (where C=perimeter, CSA=cross-sectional area and r=radius):

[0649] The total number of fetuses on the quaternary branch distal to this articulation was then counted. To normalize the size of the branches, the population of fruits on each quaternary branch was quantified as the number of fruits per branch divided by the CSA of the indicated quaternary branch:

[0650] The counted number of fetuses per quarter branch of the CSA is indicated in FIG. 11 (Valencia orange) and FIG. 12 (red grapefruit) in box-and-whisker charts, where the median value for each treatment is marked with a vertical line in the box, the mean or average value is marked with an "x", the upper and lower quartiles are marked with the box edges, and " whiskers” reach the maximum and minimum observed values of the counted number of fruits on the CSA branch. All outliers are marked with small circles outside the standard error bars for each treatment.

[0651] To further evaluate the size and volume characteristics of the fruits on the tree, the diameter (mm) of at least 10 randomly selected fruits on the tree was measured using calipers placed at the widest point of each fruit. The average fruit diameter (mm) per tree for each treatment is indicated in FIG. 13 (Valencia orange) and FIG. 14 (red grapefruit) in box and whisker charts. The average fruit diameter was used to calculate the total fruit volume per branch for each treatment. To obtain these calculated values, the volume in milliliters (ml) of a theoretically spherical orange was calculated using the following equation, where the radius (r) of the fruit is the average diameter (measured in millimeters) per branch divided by 2:

[0652] The estimated fruit volume normalized to the branch CSA for each treatment is indicated in FIG. 15 (Valencia orange) and FIG. 16 (red grapefruit) in box and whisker charts.

[0653] Measurements taken in June 2018 to evaluate fruit populations on 'Valencia' orange and 'Ruby Red' grapefruit trees in Okeechobee, Florida show an increase in the number of fruits per branch and an increase in fruit size on trees of both varieties treated by injection into stems of Bt.4Q7Flg22 at high 1X and low 10X concentration (SEQ ID NO: 226) in April 2017, when comparing mean and median values of all measured parameters with untreated control. Increased fruit set and size are predictive of increased yields. These results provide additional evidence that stem injection of Bt.4Q7Flg22 citrus trees can be used to reduce bacterial titers of C. liberibacter in orange (Figure 9) and grapefruit (Figure 10; Table 84) and to promote new shoot and fruit growth ( table 85, figures 11-16) on citrus trees.

[0654] As can be seen from the foregoing, a number of objectives of the present invention have been achieved and other favorable results have been obtained.

[0655] Since various changes can be made to the above polypeptides, recombinant organisms, methods and seeds without departing from the scope of the present invention, it is intended that all material contained in the above description is to be interpreted as illustrative and not restrictive.

IMPLEMENTATION OPTIONS

[0656] As additional illustrative material, further non-limiting embodiments of the present invention are described below.

[0657] Embodiment 1 is a polypeptide for bioactively priming a plant or plant part to improve growth, yield, health, increase longevity, productivity, and/or vitality of a plant or plant part, and/or reduce abiotic stress on the plant or plant part. plant, and/or protecting a plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of a plant or plant part, and/or changing plant architecture, characterized in that said polypeptide comprises:

(a) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 1-225, 227-375, 526, 528, 530, 532, 534, 536, 538, 540, 541, 751, 752 and 754-766; or

(b) a mutant flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 571-579 and 753; or

(c) a mutant flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 580-586; or

(d) a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450, 527, 531, 533, 535, 537 and 539; or

(e) a retro inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525 or 768; or

(f) a retro inverse Flg15 polypeptide, wherein the amino acid sequence of said retro inverse Flg15 polypeptide comprises SEQ ID NO: 529 or 767; or

(g) a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises any of SEQ ID NOs: 587, 589, 591, 593, 594, and 595; or

(h) a retro-inverse harpin or harpin-like polypeptide, wherein the amino acid sequence of said retro-inverse harpin or harpin-like polypeptide comprises any of SEQ ID NOs: 588, 590, 592, 596, and 597; or

(i) a root hair stimulator polypeptide (RHPP), wherein the amino acid sequence of said RHPP comprises any of SEQ ID NOs: 600, 603, and 604; or

(j) a Kunitz trypsin inhibitor (KTI) polypeptide, wherein the amino acid sequence of said KTI polypeptide comprises SEQ ID No: 602; or

(k) a retro inverse root hair stimulator polypeptide (RI RHPP), wherein the amino acid sequence of said RI RHPP comprises any of SEQ ID NOs: 601, 605 and 606; or

(l) a Tu elongation factor (EF-Tu) polypeptide, wherein the amino acid sequence of said EF-Tu polypeptide comprises any of SEQ ID NOs: 607-623; or

(m) a retro inverse Tu elongation factor (RI EF-Tu) polypeptide, wherein the amino acid sequence of said EF-Tu RI polypeptide comprises any of SEQ ID NOs: 624-640; or

(n) a fusion polypeptide containing SEQ ID NO: 750; or

(o) a phytosulfokine (FSK) polypeptide, wherein the amino acid sequence of said FSK polypeptide comprises SEQ ID NO: 598; or

(p) a retro-inverse phytosulfokine (RI CSF) polypeptide, wherein the amino acid sequence of said CSF RI polypeptide comprises SEQ ID NO: 599; or

(q) a thionine or thionine-like polypeptide, wherein the amino acid sequence of said thionine or thionine-like polypeptide comprises any of SEQ ID NOs: 650-749, and

optionally, characterized in that said flagellin or flagellin-associated polypeptide according to (a), mutant flagellin or flagellin-associated polypeptide according to (c), harpin or harpin-like polypeptide according to (g), KTI polypeptide according to (j), CSF polypeptide according to ( o) and thionin or thionin-like polypeptide according to (q) or contains a chemical modification; or is a variant characterized by an insertion, deletion, inversion, repetition, duplication, addition or substitution of an amino acid in an amino acid sequence; either is part of a fusion protein; or contains a protease recognition sequence.

[0658] Embodiment 2 is a polypeptide according to embodiment 1, wherein said flagellin or flagellin-associated polypeptide of (a), mutant flagellin or flagellin-associated polypeptide of (c), harpin or harpin-like polypeptide of (g) , the KTI polypeptide at (j), the CSF polypeptide at (o) and the thionine or thionine-like polypeptide at (q) or contains a chemical modification; or is a variant characterized by an insertion, deletion, inversion, repetition, duplication, addition or substitution of an amino acid in an amino acid sequence; either is part of a fusion protein; or contains a protease recognition sequence.

[0659] Embodiment 3 is a polypeptide according to embodiment 2, wherein said chemical modification includes acetylation, acid addition, acylation, ADP-ribosylation, aldehyde addition, alkylamide addition, amidation, amination, biotinylation, carbamate addition, chloromethyl ketone addition , covalent addition of a nucleotide or nucleotide derivative, crosslinking, cyclization, disulfide bonding, demethylation, ester addition, covalent crosslinking, cysteine-cysteine disulfide bonding, pyroglutamate formation, formylation, gamma-carboxylation, glycosylation, GPI anchor formation , hydrazide addition, hydroxamic acid addition, hydroxylation, iodination, lipid addition, methylation, myristiolation, oxidation, pegylation, proteolytic processing, phosphorylation, prenylation, palmitoylated ie, addition of a purification label, addition of pyroglutamyl, racemization, selenoylation, addition of a sulfonamide, sulfation, transfer RNA mediated addition of amino acids to proteins, ubiquitination, or addition of urea.

[0660] Embodiment 4 is a polypeptide according to Embodiment 2, wherein said chemical modification includes an N-terminal modification or a C-terminal modification.

[0661] Embodiment 5 is a polypeptide according to embodiment 3, wherein said chemical modification includes acetylation, amidation, crosslinking, or cyclization.

[0662] Embodiment 6 is a polypeptide according to Embodiment 2, wherein said amino acid substitution in the amino acid sequence of the variant comprises a substitution with a β-amino acid, a D-amino acid, or a non-naturally occurring amino acid.

[0663] Embodiment 7 is a polypeptide according to Embodiment 1, wherein said polypeptide comprises: the mutant flagellin or flagellin-associated polypeptide of (b); or a retro inverse Flg22 polypeptide according to (d); or retro-inverse FlgII-28 polypeptide according to (e); or a retro inverse Flg15 polypeptide at (f); or the retro-inverse harpin or harpin-like polypeptide of (h); or RHPP according to (i); or RI RHPP according to (k); or the EF-Tu polypeptide of (l); or EF-Tu RI polypeptide according to (m); or a fusion polypeptide at (n); or CSF RI polypeptide at (p).

[0664] Embodiment 8 is a polypeptide according to Embodiment 7, wherein the amino acid sequence of said mutant flagellin or flagellin-associated polypeptide of (b) comprises any one of SEQ ID NOs: 571-573.

[0665] Embodiment 9 is a polypeptide according to any one of embodiments 1-6, wherein said polypeptide comprises flagellin or a flagellin-associated polypeptide.

[0666] Embodiment 10 is a polypeptide according to Embodiment 9, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 754-766.

[0667] Embodiment 11 is a polypeptide according to any one of embodiments 1-6, wherein said polypeptide comprises a mutant flagellin or a flagellin-associated polypeptide.

[0668] Embodiment 12 is a polypeptide according to embodiment 11, wherein said mutant flagellin or flagellin-associated polypeptide is from a bacterium of the genus Bacillus, Lysinibacillus, Paenibacillus, or Aneurinibacillus.

[0669] Embodiment 13 is a polypeptide according to Embodiment 1, wherein said polypeptide contains a retro inverse Flg22 polypeptide.

[0670] Embodiment 14 is a polypeptide according to Embodiment 1, wherein said polypeptide comprises a retro-inverse FlgII-28 polypeptide.

[0671] Embodiment 15 is a polypeptide according to Embodiment 1, wherein said polypeptide contains a retro inverse Flg15 polypeptide.

[0672] Embodiment 16 is a polypeptide according to any one of embodiments 1-6, wherein said polypeptide comprises a harpin or a harpin-like polypeptide.

[0673] Embodiment 17 is a polypeptide according to Embodiment 1, wherein said polypeptide comprises a retro-inverse harpin or a harpin-like polypeptide.

[0674] Embodiment 18 is a polypeptide according to Embodiment 1, wherein said polypeptide contains RHPP.

[0675] Embodiment 19 is a polypeptide according to Embodiment 1, wherein said polypeptide contains RHPP RI.

[0676] Embodiment 20 is a polypeptide according to Embodiment 1, said polypeptide comprising an EF-Tu polypeptide.

[0677] Embodiment 21 is a polypeptide according to Embodiment 1, wherein said polypeptide comprises a retro-inverse EF-Tu polypeptide.

[0678] Embodiment 22 is a polypeptide according to any one of embodiments 1-21, wherein said polypeptide further comprises a core sequence.

[0679] Embodiment 23 is a polypeptide according to Embodiment 22, wherein said core sequence contains any of SEQ ID 754-766.

[0680] Embodiment 24 is a polypeptide according to Embodiment 1, wherein said polypeptide contains a fusion polypeptide.

[0681] Embodiment 25 is a polypeptide according to embodiment 24, wherein said fusion polypeptide contains an accessory polypeptide.

[0682] Embodiment 26 is a polypeptide according to embodiment 25, wherein said accessory polypeptide comprises a signature polypeptide, wherein the amino acid sequence of said signature polypeptide comprises any of SEQ ID NOs: 542-548 or any combination thereof.

[0683] Embodiment 27 is a polypeptide according to embodiment 25, wherein said accessory polypeptide comprises a signature polypeptide, wherein the amino acid sequence of said signature polypeptide contains SEQ ID NO: 542.

[0684] Embodiment 28 is a polypeptide according to embodiment 25, wherein said accessory polypeptide comprises a signal anchor sort polypeptide and the amino acid sequence of said signal anchor sort polypeptide comprises any one of SEQ ID NOs: 549-562 or any combination thereof.

[0685] Embodiment 29 is a polypeptide according to embodiment 25, wherein said accessory polypeptide comprises a signal anchor sort polypeptide and the amino acid sequence of said signal anchor sort polypeptide comprises SEQ ID NO: 549.

[0686] Embodiment 30 is a polypeptide according to any one of embodiments 1-6, wherein said polypeptide comprises a phytosulfokino polypeptide.

[0687] Embodiment 31 is a polypeptide according to any one of embodiments 1-6, wherein said polypeptide comprises a retro-inverse phytosulfokine polypeptide.

[0688] Embodiment 32 is a polypeptide according to any one of embodiments 1-6, wherein said polypeptide contains a thionine or a thionine-like polypeptide.

[0689] Embodiment 33 is a polypeptide according to any one of embodiments 1-32, characterized in that said polypeptide further comprises a core sequence comprising any of SEQ ID NOs: 754-768, and in that the inclusion of said core sequence increases priming the bioactivity of said polypeptide.

[0690] Embodiment 34 is a polypeptide according to any one of embodiments 1-33, wherein said polypeptide may contain an amino acid sequence at least 70% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0691] Embodiment 35 is a polypeptide according to any one of embodiments 1-34, wherein said polypeptide may contain an amino acid sequence at least 75% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0692] Embodiment 36 is a polypeptide according to any of embodiments 1-35, wherein said polypeptide may contain an amino acid sequence at least 80% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0693] Embodiment 37 is a polypeptide according to any one of embodiments 1-36, wherein said polypeptide may contain an amino acid sequence at least 85% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0694] Embodiment 38 is a polypeptide according to any one of embodiments 1-37, wherein said polypeptide may contain an amino acid sequence at least 90% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0695] Embodiment 39 is a polypeptide according to any one of embodiments 1-38, wherein said polypeptide may contain an amino acid sequence at least 95% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0696] Embodiment 40 is a polypeptide according to any of embodiments 1-39, wherein said polypeptide may contain an amino acid sequence at least 98% identical to any of SEQ ID NOs: 1-768, wherein said polypeptide has priming activity.

[0697] Embodiment 41 is a polypeptide according to any one of embodiments 1-40, wherein said polypeptide may contain an amino acid sequence at least 99% identical to any of SEQ ID NOs: 1-766, wherein said polypeptide has priming activity.

[0698] Embodiment 42 is a polypeptide according to any one of embodiments 1-41, wherein said polypeptide is isolated, concentrated from a fermentation product, and/or partially purified.

[0699] Embodiment 43 is a polypeptide according to embodiment 42, wherein said polypeptide is isolated, concentrated from a fermentation product, and/or partially purified by filtration or chromatography.

[0700] Embodiment 44 is a polypeptide according to embodiment 42 or 43, wherein said polypeptide is isolated, concentrated from a fermentation product, or partially purified from a recombinant microorganism.

[0701] Embodiment 45 is a composition for bioactively priming a plant or plant part to improve growth, yield, health, increase longevity, productivity, and/or vitality of a plant or plant part, and/or reduce abiotic stress on the plant or plant part. plant, and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering plant architecture, said composition comprising any of the following:

a polypeptide according to any one of embodiments 1-44, or any combination thereof, and an agrochemical or carrier; or

any combination of these polypeptides according to any one of embodiments 1-44.

[0702] Embodiment 46 is a composition according to embodiment 45, wherein said composition comprises the flagellin or flagellin-associated polypeptide of (a), the mutant flagellin or flagellin-associated polypeptide of (c), the harpin or harpin-like polypeptide of ( g), a KTI polypeptide of (j), a CSF polypeptide of (o), a thionin or a thionin-like polypeptide of (q), or any combination thereof, and an agrochemical or carrier, said agrochemical or carrier being not naturally associated with said polypeptide.

[0703] Embodiment 47 is a composition according to embodiment 45, characterized in that said composition contains:

mutant flagellin or flagellin-associated polypeptide according to (b); or a retro inverse Flg22 polypeptide according to (d); or retro-inverse FlgII-28 polypeptide according to (e); or a retro inverse Flg15 polypeptide at (f); or the retro-inverse harpin or harpin-like polypeptide of (h); or RHPP according to (i); or RI RHPP according to (k); or the EF-Tu polypeptide of (l); or EF-Tu RI polypeptide according to (m); or a fusion polypeptide at (n); CSF RI polypeptide at (p), or any combination of the above; and

flagellin or flagellin-associated polypeptide of (a), mutant flagellin or flagellin-associated polypeptide of (c), harpin or harpin-like polypeptide of (g), KTI polypeptide of (j), CSF polypeptide of (o), thionine or thionine-like polypeptide by (q), or any combination of the above.

[0704] Embodiment 48 is a composition according to embodiment 46 or 47, wherein said flagellin or flagellin-associated polypeptide at (a), a mutant flagellin or flagellin-associated polypeptide at (c), a harpin or harpin-like polypeptide at ( g), the KTI polypeptide of (j), the CSF polypeptide of (o), the thionine or thionine-like polypeptide of (q), or any combination of the foregoing, does not contain a chemical modification; is not an option; is not part of a fusion protein; and does not contain a protease recognition sequence.

[0705] Embodiment 49 is a composition according to embodiment 45, wherein said composition comprises: two or more mutant flagellins or flagellin-associated polypeptides of (b); or retro-inverse Flg22 polypeptides of (d); or retro-inverse FlgII-28 polypeptides in (e); or retro-inverse Flg15 polypeptides in (f); or the retro-inverse harpins or harpin-like polypeptides of (h); or RHPP according to (i); or RI RHPP according to (k); or the EF-Tu polypeptides of (l); or EF-Tu RI polypeptides according to (m); or fusion polypeptides at (n); or RI polypeptides of CSF by (p).

[0706] Embodiment 50 is a composition according to embodiment 45, wherein said composition comprises: two or more flagellins or flagellin-associated polypeptides of (a), mutant flagellins or flagellin-associated polypeptides of (c), harpins, or harpin-like polypeptides at (g), KTI polypeptides at (j), CSF polypeptides at (o), or thionins or thionin-like polypeptides at (q), which are any of the following:

at least one of the flagellin or flagellin-associated polypeptide of (a), the mutant flagellin or flagellin-associated polypeptide of (c), the harpin or harpin-like polypeptide of (g), the CSF polypeptide of (o), or the thionine, or the thionin-like polypeptide at (q) contains a chemical modification; is an option; is part of a fusion protein; or contains a protease recognition sequence; or

at least two flagellins or flagellin-associated polypeptides according to (a), a mutant flagellin or flagellin-associated polypeptide according to (c), a harpin or harpin-like polypeptide according to (g), a KTI polypeptide according to (j), a CSF polypeptide according to (o), or the thionin or thionin-like polypeptide at (q) is not naturally associated.

[0707] Embodiment 51 is a composition according to embodiment 45, wherein said flagellin or flagellin-associated polypeptide is produced by a recombinant method using a microorganism.

[0708] Embodiment 52 is a composition according to Embodiment 51, wherein said microorganism comprises Bacillus bacterium, Pseudomonas bacterium, Paenibacillus bacterium, Penicillium fungus, Glomus bacterium, Arthrobacter bacterium , a bacterium of the genus Paracoccus, a bacterium of the genus Rhizobium, a bacterium of the genus Bradyrhizobium, a bacterium of the genus Azosprillium, a bacterium of the genus Enterobacter, a bacterium of the genus Escherichia, or any combination thereof.

[0709] Embodiment 53 is a recombinant microorganism that expresses or overexpresses a polypeptide, said polypeptide comprising a polypeptide according to any one of embodiments 1-44 or any combination thereof.

[0710] Embodiment 54 is a recombinant microorganism according to embodiment 53, wherein said polypeptide comprises: flagellin or the flagellin-associated polypeptide of (a); or a mutant flagellin or flagellin-associated polypeptide according to (b); or a mutant flagellin or flagellin-associated polypeptide according to (c); or the harpin or harpin-like polypeptide of (g); or RHPP according to (i); or a KTI polypeptide according to (j); or the EF-Tu polypeptide of (l); or a fusion polypeptide at (n); or the FSK polypeptide according to (o); or the thionin or thionin-like polypeptide of (q).

[0711] Embodiment 55 is a recombinant microorganism according to embodiment 53 or 54, characterized in that it overexpresses said polypeptide.

[0712] Embodiment 56 is a recombinant microorganism according to embodiment 55, wherein said polypeptide is produced with a secretion signal.

[0713] Embodiment 57 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises flagellin or a flagellin-associated polypeptide.

[0714] Embodiment 58 is a composition or recombinant microorganism according to embodiment 57, characterized in that said flagellin or flagellin-associated polypeptide is chemically modified at the N- or C-terminus.

[0715] Embodiment 59 is a composition or recombinant microorganism according to embodiment 57, wherein said flagellin or flagellin-associated polypeptide is modified by crosslinking or cyclization.

[0716] Embodiment 60 is a composition or recombinant microorganism according to embodiment 57, wherein said flagellin or flagellin-associated polypeptide is from a bacterium of the genus Bacillus, Lysinibacillus, Paenibacillus, Aneurinibacillus, or any combination thereof.

[0717] Embodiment 61 is a composition or recombinant microorganism according to embodiment 57, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any one of SEQ ID NOs: 1-75 or any combination thereof.

[0718] Embodiment 62 is a composition or recombinant microorganism according to embodiment 57, wherein said flagellin or flagellin-associated polypeptide comprises a truncated N-terminal polypeptide, wherein the amino acid sequence of said truncated N-terminal polypeptide comprises SEQ ID NO: 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106,108, 109, 110, 112, 114, 116, 118, 120, 122, 124, 126 128 130 132 134 136 138 140 142 144 146 148 150 152 154.156 158 160 162 164 166 168 170 172 174 174 178, 180, 182,184, 186, 188, 190, 192, 194, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 752 or any of them combination.

[0719] Embodiment 63 is a composition or recombinant microorganism according to embodiment 57, wherein said flagellin or flagellin-associated polypeptide comprises a truncated C-terminal polypeptide, wherein the amino acid sequence of said truncated C-terminal polypeptide comprises SEQ ID NO: 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117, 119, 121, 123, 125, 127, 129, 131, 133, 135, 137, 141, 143, 145, 147, 149, 151, 153, 155, 157, 159, 161, 163, 165, 167, 169, 171, 173, 175, 177, 179, 181, 183, 185, 187, 189, 191, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, or any combination thereof.

[0720] Embodiment 64 is a composition or recombinant microorganism according to embodiment 57, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 289, 290, 291, 293, 294, 295 , 300, 437, 532, 534, 536, 538, 540, 571-586 and 751-768, or any combination thereof.

[0721] Embodiment 65 is a composition or recombinant microorganism according to embodiment 64, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 293, 295, 300, 540, 571, 574 and 752 or any combination thereof.

[0722] Embodiment 66 is a composition or recombinant microorganism according to embodiment 64, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 754-766.

[0723] Embodiment 67 is a composition or recombinant microorganism according to embodiment 66, wherein said flagellin or flagellin-associated polypeptide is included in a non-flagellin or non-flagellin-associated polypeptide or full length protein, wherein said flagellin or flagellin is included β-associated polypeptide results in increased bioactive priming activity of said non-flagellin or non-flagellin-associated polypeptide or full-length protein.

[0724] Embodiment 68 is a composition or recombinant microorganism according to embodiment 57, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any or any combination of SEQ ID NOs: 226-300.

[0725] Embodiment 69 is a composition or recombinant microorganism according to embodiment 57, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 301-375 and 751, or any combination thereof.

[0726] Embodiment 70 is a composition or recombinant microorganism according to embodiment 69, characterized in that the amino acid sequence of said flagellin or flagellin-associated polypeptide contains SEQ ID NO: 301.

[0727] Embodiment 71 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises a retro-inverse Flg22 polypeptide.

[0728] Embodiment 72 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises a retro-inverse FlgII-28 polypeptide.

[0729] Embodiment 73 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide contains a thionine or a thionine-like polypeptide.

[0730] Embodiment 74 is a composition or recombinant microorganism according to embodiment 73, characterized in that the amino acid sequence of said thionine or thionine-like polypeptide contains SEQ ID NO: 651.

[0731] Embodiment 75 is a composition or recombinant microorganism according to embodiment 74, wherein said thionin or thionin-like polypeptide is fused to a phloem targeting sequence to form a fusion polypeptide, wherein the amino acid sequence of said phloem targeting sequence contains any of SEQ ID NOs: 641-649, or any combination thereof, to deliver said fusion polypeptide to vascular tissue or vascular cells and/or phloem or phloem-associated tissue or phloem-associated cells in a plant or plant part.

[0732] Embodiment 76 is a composition or recombinant microorganism according to embodiment 75, characterized in that the amino acid sequence of said phloem targeting sequence contains SEQ ID NO: 641.

[0733] Embodiment 77 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises a CSF polypeptide.

[0734] Embodiment 78 is a composition or recombinant microorganism according to embodiment 77, characterized in that the amino acid sequence of said CSF polypeptide contains SEQ ID NO: 598.

[0735] Embodiment 79 is a composition or recombinant microorganism according to any one of embodiments 45-56, characterized in that said polypeptide contains RHPP.

[0736] Embodiment 80 is a composition or recombinant microorganism according to embodiment 79, characterized in that the amino acid sequence of said RHPP contains SEQ ID NO: 600.

[0737] Embodiment 81 is a composition or recombinant microorganism according to embodiment 80 further comprising flagellin or a flagellin-associated polypeptide.

[0738] Embodiment 82 is a composition or recombinant microorganism according to embodiment 81, characterized in that the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOS: 226, 752, and 571.

[0739] Embodiment 83 is a composition or recombinant microorganism according to embodiment 82, characterized in that the amino acid sequence of said flagellin or flagellin-associated polypeptide contains SEQ ID NO: 226.

[0740] Embodiment 84 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises RHPP RI.

[0741] Embodiment 85 is a composition or recombinant microorganism according to any one of embodiments 38-47, wherein said polypeptide comprises a harpin or harpin-like polypeptide.

[0742] Embodiment 86 is a composition or recombinant microorganism according to embodiment 85, characterized in that the amino acid sequence of said harpin or harpin-like polypeptide contains SEQ ID NO: 587.

[0743] Embodiment 87 is a composition or recombinant microorganism according to any one of embodiments 45-56 containing an CSF polypeptide, RHPP, a harpin, or a harpin-like polypeptide, or a combination thereof.

[0744] Embodiment 88 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises an EF-Tu polypeptide.

[0745] Embodiment 89 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide further comprises a secretion signal.

[0746] Embodiment 90 is a composition or recombinant microorganism according to embodiment 88 or 89, characterized in that the amino acid sequence of said EF-Tu polypeptide contains SEQ ID NO: 616.

[0747] Embodiment 91 is a composition or recombinant microorganism according to embodiment 90, further comprising an EF-Tu polypeptide having an amino acid sequence comprising SEQ ID NO: 617.

[0748] Embodiment 92 is a composition or recombinant microorganism according to any one of embodiments 88-91, further comprising flagellin or a flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 1-525 , 526, 530, 532, 534, 536, 538, 540, 541, 571-586 and 751-766, or any combination thereof.

[0749] Embodiment 93 is a composition or recombinant microorganism according to embodiment 92, further comprising flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, 571, or 752, or a combination thereof .

[0750] Embodiment 94 is a composition or recombinant microorganism according to embodiment 92, further comprising a harpin or a harpin-like polypeptide.

[0751] Embodiment 95 is a composition or recombinant microorganism according to embodiment 94, characterized in that the amino acid sequence of said harpin or harpin-like polypeptide contains SEQ ID NO: 587.

[0752] Embodiment 96 is a composition or recombinant microorganism according to any one of embodiments 45-56, comprising

(a) flagellin or flagellin-associated polypeptides, wherein the amino acid sequences of said flagellin or flagellin-associated polypeptides comprise SEQ ID NOs: 571, 295, 300, 293 and 580; or 295, 300, 293 and 580; or 571, 295, 293 and 580; or 571, 300, 293 and 580; or 571, 293 and 580; or 571, 295, 293; or

(b) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226 and one or more of cellobiose, chitin, chitosan, or cellulose; or

(c) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, and a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises SEQ ID NO: 591; or

(d) a harpin or harpin-like polypeptide, wherein the amino acid sequence of said harpin or harpin-like polypeptide comprises SEQ ID NO: 587, and a CSF polypeptide, wherein the amino acid sequence of said CSF polypeptide comprises SEQ ID NO: 598; or

(e) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, 571 or 752, or any combination thereof; and EF-Tu polypeptides, wherein the amino acid sequences of said EF-Tu polypeptides comprise SEQ ID NOs: 616 and 617; or

(f) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, 540, 571, or 752, or any combination thereof; or

(g) an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide comprises SEQ ID NO: 600; or

(h) flagellin or flagellin-associated polypeptide, wherein the amino acid sequences of said flagellin or flagellin-associated polypeptide comprise SEQ ID NO: 226, 540, 226, 571, or 752, or any combination thereof; and an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide contains SEQ ID NO: 600; or

(i) flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226; and an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide contains SEQ ID NO: 600.

[0753] Embodiment 97 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said polypeptide comprises a fusion polypeptide.

[0754] Embodiment 98 is a composition or recombinant microorganism according to any one of embodiments 45-56, wherein said flagellin or flagellin-associated polypeptide is a polypeptide fusion protein.

[0755] Embodiment 99 is a composition or recombinant microorganism according to any one of embodiments 45-98, further comprising an accessory polypeptide.

[0756] Embodiment 100 is a composition or recombinant microorganism according to embodiment 99, characterized in that said accessory polypeptide comprises a signature polypeptide, wherein the amino acid sequence of said signature polypeptide contains any of SEQ ID NOs: 542-548 or any combination thereof.

[0757] Embodiment 101 is a composition or recombinant microorganism according to embodiment 99, characterized in that said accessory polypeptide comprises a signature polypeptide, wherein the amino acid sequence of said signature polypeptide contains SEQ ID NO: 542.

[0758] Embodiment 102 is a composition or recombinant microorganism according to embodiment 99, wherein said accessory polypeptide comprises a signal anchor sort polypeptide, wherein the amino acid sequence of said signal anchor sort polypeptide comprises any of SEQ ID NOs: 549-562 or any combination of them.

[0759] Embodiment 103 is a composition or recombinant microorganism according to embodiment 102, characterized in that said accessory polypeptide comprises a signal anchor sort polypeptide, wherein the amino acid sequence of said signal anchor sort polypeptide comprises SEQ ID NO: 549.

[0760] Embodiment 104 is a composition or recombinant microorganism according to embodiment 99, characterized in that said accessory polypeptide comprises a secretion polypeptide, wherein the amino acid sequence of said secretion polypeptide comprises any of SEQ ID NOs: 563-570 or 769, or any their combination.

[0761] Embodiment 105 is a composition or recombinant microorganism according to embodiment 104, characterized in that said accessory polypeptide comprises a secretion polypeptide, wherein the amino acid sequence of said secretion polypeptide comprises SEQ ID NO: 563 or 769.

[0762] Embodiment 106 is a composition or recombinant microorganism according to embodiment 99 or 104, characterized in that said accessory polypeptide comprises an enterokinase cleavage sequence, wherein the amino acid sequence of said enterokinase cleavage sequence comprises SEQ ID NO: 772.

[0763] Embodiment 107 is a composition or recombinant microorganism according to embodiment 106, characterized in that the accessory polypeptide includes a junction region between the polypeptide and the protein tag.

[0764] Embodiment 108 is a composition or recombinant microorganism according to embodiment 107, wherein said protein tag comprises a polyhistidine (His) tag, a FLAG tag, an antibody epitope, streptavidin/biotin, glutathione-S-transferase (GST), or any combination of them.

[0765] Embodiment 109 is a composition according to any of embodiments 45-52 and 57-108, further comprising either an agrochemical or a carrier that is naturally associated with said polypeptide.

[0766] Embodiment 110 is a composition according to any one of embodiments 45-52 and 57-109, wherein said agrochemical comprises an antibiotic, a biopesticide, a preservative, a buffering agent, a wetting agent, a surfactant, a coating agent, a monosaccharide, a polysaccharide, an abrasive, a pesticide, an insecticide, a herbicide, a nematocide, a bactericide, a fungicide, a miticide, a fertilizer, a biostimulant, an osmoprotectant, a coloring agent, a humectant, an amino acid, a biological control agent, or a combination thereof.

[0767] Embodiment 111 is a composition according to embodiment 110, wherein said preservative comprises dichlorophen, benzyl alcohol semiformal, isothiazolinone derivative, alkylisothiazolinone, benzisothiazolinone, MIT (2-methyl-4-isothiazolin-3-one), BIT (1,2-benzisothiazolin-3-one), 5-chloro-2-(4-chlorobenzyl)-3(2H)-isothiazolone, 5-chloro-2-methyl-2H-isothiazol-3-one, 5-chloro -2-methyl-2H-isothiazol-3-one, 5-chloro-2-methyl-2H-isothiazol-3-one-hydrochloride, 4,5-dichloro-2-cyclohexyl-4-isothiazolin-3-one, 4 ,5-dichloro-2-octyl-2H-isothiazol-3-one, 2-methyl-2H-isothiazol-3-one, 2-methyl-2H-isothiazol-3-one-calcium chloride complex, 2-octyl-2H -isothiazol-3-one; or any combination of the above.

[0768] Embodiment 112 is a composition according to embodiment 110 or 111, wherein said buffering agent contains potassium, phosphoric acid, phosphate salt, citric acid, citrate salt, sulfate salt, MOPS, HEPES, or any combination thereof.

[0769] Embodiment 113 is a composition according to any one of embodiments 110-112, wherein said wetting agent comprises a silicone, polyoxyethoxylate, polysorbate, polyethylene glycol or derivative thereof, an ethoxylate, a plant treatment oil, a polysaccharide, or any combination of the foregoing. .

[0770] Embodiment 114 is a composition according to any one of Embodiments 110-113, wherein said surfactant comprises a dark petroleum oil, a dark petroleum distillate, a polyol fatty acid ester, a polyethoxylated fatty acid ester, arylalkylpolyoxyethylene glycol, alkylamine acetate, alkylarylsulfonate, polyhydric alcohol, alkyl phosphate, alcohol ethoxylate, alkylphenol ethoxylate, alkoxylated polyols, alkylpolyethoxyethers, ethoxylated soybean oil derivatives, alkylpolyoxyethyleneglycerin, alcohol ethoxylate, polyoxyethylenepolyoxypropylene monobutyl ether, silicone derivative, or any combination of the foregoing.

[0771] Embodiment 115 is a composition according to any one of embodiments 110-114, wherein said coating agent comprises a tackifier, polymers, filler, bulking agent, or any combination thereof.

[0772] Embodiment 116 is a composition according to embodiment 115, wherein said tackifier comprises carboxymethyl cellulose, natural polymer, synthetic polymer, gum arabic, chitin, polyvinyl alcohol, polyvinyl acetate, natural phospholipid, cephalin, lecithin, synthetic phospholipid, polyester, polyester-ether copolymer, polyanhydride, polyesterurethane, polyesteramide; polyvinyl acetate; polyvinyl acetate copolymer; tylose; polyvinyl alcohol copolymer; polyvinylpyrrolidone; polysaccharide, starch, modified starch, starch derivative, dextrin, maltodextrin, alginate, chitosan, cellulose, cellulose ester, cellulose ether, cellulose ethers, ethylcellulose, methylcellulose, hydroxymethylcellulose, hydroxypropylcellulose, carboxymethylcellulose; fat; oil; protein, casein, gelatin, zein; shellac; vinylidene chloride, vinylidene chloride copolymer; lignosulfonate, calcium lignosulfonate; polyacrylate, polymethacrylate, acrylic copolymer; polyvinyl acrylate; polyethylene oxide; polybutene, polyisobutylene, polystyrene, polybutadiene, polyethyleneamine, polyethyleneamide; an acrylamide polymer or copolymer; polyhydroxyethyl acrylate, methylacrylamide; polychloroprene or any combination of the above.

[0773] Embodiment 117 is a composition according to any one of embodiments 110-116, wherein said abrasive agent contains talc, graphite, or a combination thereof.

[0774] Embodiment 118 is a composition according to any one of embodiments 110-117, wherein said pesticide comprises an insecticide, herbicide, fungicide, bactericide, nematocide, miticide, or any combination thereof.

[0775] Embodiment 119 is a composition according to embodiment 118, wherein said insecticide comprises clothianidin, imidacloprid, an organophosphorus compound, carbamate, pyrethroid, acaricide, alkyl phthalate, boric acid, borate, fluoride, sulfur, urea with haloaromatic substituents, a hydrocarbon ester, a biological insecticide, or any combination thereof.

[0776] Embodiment 120 is a composition according to embodiment 118, wherein said herbicide comprises 2,4-D, 2,4-DB, acetochlor, acifluorfen, alachlor, ametrine, atrazine, aminopyralid, benefin, bensulfuron, bensulfuron -methyl, bensulide, bentazone, bispyribac sodium, bromacil, bromoxynil, butylate, carfentrazone, chlorimuron, 2-chlorophenoxyacetic acid, chlorsulfuron, chlorimuron-ethyl, cletodim, clomazone, clopyralid, cloransulam, chloro-2-methylphenoxypropanoic acid dimethylamine salt (CMPP- P_DMA), cycloate, DCPA, desmedifam, dicamba, dichlobenil, diclofop, 2,4-dichlorophenol, dichlorophenoxyacetic acid, dichlorprop, dichloroprop-P, diclosulam, diflufenzopyr, dimethenamide, 2,4-dichlorophenoxyacetic acid dimethylamine salt, diquat, diuron, DSMA , Endothal, EPTC, Etalfluralin, Ethofumesate, Fenoxaprop, Fluazifop-P, Flucarbazone, Flufenacet, Flumetsulam, Flumiclorac, Flumioxazine, Fluometuron, Fluroxypyr, Fluoroxypyr 1-Methylheptyl Ether, Fomesafen , fomesafen sodium, foramsulfuron, glufosinate, ammonium glufosinate, glyphosate, halosulfuron, halosulfuron-methyl, hexazinon, 2-hydroxyphenoxyacetic acid, 4-hydroxyphenoxyacetic acid, imazamethabenz, imazamox, imazapic, imazaquin, imazethapyr, isoxaben, isoxaflutol, lactofenol, mazapyr, MCPA, MCPB, mecoprop, mecoprop-P, mesotrione, C-metolachlor, metribuzin, metsulfuron, metsulfuron-methyl, molinate, MSMA, napropamide, naptalam, nicosulfuron, norflurazon, oryzalin, oxadiazon, oxyfluorophen, paraquat, pelargonic acid, pendimethalin , phenmedifam, picloram, primisulfuron, prodiamine, promethrin, pronamide, propanil, prosulfuron, pyrazon, pyrithiobac, pyroxasulfone, quinclorac, quizalofop, rimsulfuron, sethoxydim, siduron, simazine, sulfentrazone, sulfometuron, sulfosulfuron, tebuthiuron, terbacil, thifenazopyrone, -methyl, thiobencarb, trialkoxydim, triallat, triasulfuron, tribenuron, tribernuron-methyl, triclopyr, trifluralin, triflusul furon or any combination thereof.

[0777] Embodiment 121 is a composition according to embodiment 118, wherein said nematocide comprises Bacillus firmus, fluopyram, antibiotic nematocide, abamectin, carbamate nematocide, acetoprol, Bacillus chitonosporus, chloropicrin, benclothiasis, benomyl, Burholderia cepacia, carbofuran, carbosulfan, cleotocard, dazomet, dibromochloropropane (DBCP), DCIP, alanicarb, aldicarb, aldoxycarb, oxamyl, diamidafos, fenamiphos, fostietane, phosphamidon, cadusafos, chlorpyrifos, diclofenthion, dimethoate, etoprofos, fensulfothion, fostiazate, harpines, imiciafos , isamidophos, isazophos, methomyl, mecarfon, Myrothecium verrucaria, Paecilomyces lilacinus, Pasteuria nishizawae, phorate, phosphocarb, terbufos, thionazine, thioxazafen, triazophos, dazomet, 1,2-dichloropropane, 1,3-dichloropropene, furfural, iodomethane, metam, methyl bromide, methyl isothiocyanate, xylenol; or any combination of them.

[0778] Embodiment 122 is a composition according to embodiment 118, wherein said bacteriocide comprises streptomycin, penicillin, tetracycline, oxytetracycline, ampicillin, oxolinic acid, kasugamycin, chlortetracycline, copper oxide, or any combination thereof.

[0779] Embodiment 123 is a composition according to embodiment 122, wherein said bactericide contains oxytetracycline.

[0780] Embodiment 124 is a composition according to embodiment 118, wherein said biological control agent comprises Bacillus thuringiensis, Bacillus megaterium, Bacillus mycoides, Isolate J, Bacillus methylotrophicus, Bacillus vallismortis, Chromobacterium subtsugae, Delftia acidovorans, Streptomyces lydicus , Streptomyces colombiensis, Streptomyces galbus K61, Penicillium bilaii, a lipopeptide-producing strain of Bacillus subtilis, a lipopeptide-producing strain of Bacillus amyloliquefaciens, a strain of Bacillus firmus, or a strain of Bacillus pumilus.

[0781] Embodiment 125 is a composition according to any one of embodiments 110-124, wherein said fertilizer contains ammonium sulfate, ammonium nitrate, ammonium sulfate nitrate, ammonium chloride, ammonium bisulfate, ammonium polysulfide, ammonium thiosulfate, aqueous ammonia, anhydrous ammonia, ammonium polyphosphate, aluminum sulfate, calcium nitrate, calcium ammonium nitrate, calcium sulfate, burnt magnesite, calcite limestone, calcium oxide, calcium nitrate, dolomitic limestone, hydrated lime, calcium carbonate, diammonium phosphate, monoammonium phosphate, magnesium nitrate, magnesium sulfate , potassium nitrate, potassium chloride, magnesium potassium sulfate, potassium sulfate, sodium nitrates, magnesian limestone, magnesia, urea, formaldehyde urea, urea ammonium nitrate, sulfur-coated urea, polymer-coated urea, isobutylidene diurea, K ₂ SO4-Mg ₂ SO ₄ , kainite, sylvinite, kieserite, Epsom salts, elemental sulfur, marl, ground oyster shells, fish oil meal, fish meal, fish meal, blood meal, phosphate ore, superphosphates, slag, bone meal, wood ash, manure, bat droppings, peat moss, compost, wet sand, cottonseed meal, feather meal, crab feed meal, fish emulsion, humic acid, or any combination thereof.

[0782] Embodiment 126 is a composition according to any one of embodiments 110-125, wherein said fertilizer contains boric acid, borate, boric frit, copper sulfate, copper frit, copper chelate, sodium tetraborate decahydrate, ferrous sulfate, oxide iron, iron-ammonium sulfate, iron frit, iron chelate, manganese sulfate, manganese oxide, manganese chelate, manganese chloride, manganese frit, sodium molybdate, molybdic acid, zinc sulfate, zinc oxide, zinc carbonate, zinc frit, zinc phosphate, chelate zinc or any combination thereof.

[0783] Embodiment 127 is a composition according to any one of embodiments 110-126, wherein said biostimulant comprises seaweed extract, elicitor, polysaccharide, monosaccharide, protein extract, soy extract, humic acid, plant hormone, plant growth regulator or any combination of them.

[0784] Embodiment 128 is a composition according to any one of embodiments 110-126, wherein said amino acid comprises cysteine.

[0785] Embodiment 129 is a composition according to any of embodiments or 57-128, further containing a fungicide.

[0786] Embodiment 130 is the composition of Embodiment 129, wherein said fungicide comprises a strobilurin fungicide or a triazole fungicide.

[0787] Embodiment 131 is a composition according to embodiment 130, wherein said strobilurin fungicide comprises strobilurin A, strobilurin B, strobilurin C, strobilurin D, strobilurin E, strobilurin F, strobilurin G, strobilurin H, azoxystrobin, trifloxystrobin, kresoximmethyl, fluoxastrobin, picoxystrobin, or any combination thereof.

[0788] Embodiment 132 is the composition of Embodiment 131 wherein said strobilurin fungicide comprises azoxystrobin, trifloxystrobin, kresoximmethyl, fluoxastrobin, picoxystrobin, pyraclostrobin, or any combination thereof.

[0789] Embodiment 133 is the composition of Embodiment 131, wherein said strobilurin fungicide comprises trifloxystrobin.

[0790] Embodiment 134 is the composition of Embodiment 131, wherein said strobilurin fungicide comprises fluoxastrobin.

[0791] Embodiment 135 is a composition according to any one of embodiments 130-134, wherein said triazole fungicide comprises prothioconazole, imidazole, imidazyl, prochloraz, propiconazole, triflumizole, diniconazole, flusilazole, penconazole, hexaconazole, cyproconazole, myclobutanil, tebuconazole, difenoconazole, tetraconazole, fenbuconazole, epoxiconazole, metconazole, fluquinconazole, triticonazole, or any combination thereof.

[0792] Embodiment 136 is a composition according to any one of embodiments 130-135, wherein said triazole fungicide comprises prothioconazole.

[0793] Embodiment 137 is a composition according to any one of embodiments 45-52 or 57-136, wherein said humectant comprises glycerol, glycerin, glycerol derivative, glycerol triacetate, triacetin, propylene glycol, hexylene glycol, butylene glycol, triethylene glycol, tripolypropylene glycol , glyceryl triacetate, sucrose, tagatose, sugar alcohol, polyhydric sugar alcohol, sorbitol, xylitol, mannitol, manthitol, polymeric polyhydric alcohol, polydextrose, collagen, aloe, aloe vera gel, alpha hydroxy acid, honey, molasses, quillaya, sodium hexametaphosphate, lithium chloride, urea, butylene glycol or tremella extract

[0794] Embodiment 138 is a composition according to any one of embodiments 45-52 or 57-137, wherein said carrier comprises water, peat, wheat, bran, vermiculite, clay, pasteurized soil, calcium carbonate, calcium bicarbonate, dolomite, gypsum, bentonite, clay, phosphorite, phosphorus compound, titanium dioxide, humus, talc, alginate, activated carbon, or a combination thereof.

[0795] Implementation 139 is a composition according to any one of embodiments 45-52 or 57-138, characterized in that said composition contains from about 0.00001 wt. % to about 95% of the specified polypeptide or polypeptides, from about 0.01% to about 80 wt. % of the specified agrochemical and from about 5 to about 50 wt. % carrier based on the total weight of the composition.

[0796] Embodiment 140 is a composition according to any of embodiments 45-52 or 57-139, wherein said composition contains from about 0.01% to about 5% of said polypeptide or polypeptides, from about 0.2% up to about 70 wt. % of the specified agrochemical, and from about 10 to about 30 wt. % carrier based on the total weight of the composition.

[0797] Embodiment 141 is a composition according to any one of embodiments 45-52 or 57-139, wherein said composition contains from about 0.05% to about 1% of said polypeptide or polypeptides, from about 30% to about 60 wt. % of the specified agrochemical, and from about 40 to about 69 wt. % carrier based on the total weight of the composition.

[0798] Embodiment 142 is a composition according to any of embodiments 45-52 or 57-141, wherein said agrochemical comprises hydrochloric acid, acetic acid, and/or trifluoroacetic acid.

[0799] Embodiment 143 is a composition according to embodiment 142, characterized in that said agrochemical contains hydrochloric acid, acetic acid, and/or trifluoroacetic acid, and contains from about 0.001 wt. % to about 30% of the mass. % of the total weight of the composition.

[0800] Embodiment 144 is a composition according to embodiment 143, characterized in that said agrochemical contains hydrochloric acid, acetic acid, and/or trifluoroacetic acid, and contains from about 0.01 wt. % to about 20% of the mass. % of the total weight of the composition.

[0801] Embodiment 145 is a composition according to embodiment 144, characterized in that said agrochemical contains hydrochloric acid, acetic acid, and/or trifluoroacetic acid, and contains from about 0.1 wt. % to about 5 wt. % of the total weight of the composition

[0802] Embodiment 146 is a seed coated with a polypeptide according to any of embodiments 1-44 or any combination thereof, or a composition according to any of embodiments 45-52 and 57-145, or a recombinant microorganism according to any of embodiments 53- 108.

[0803] Embodiment 147 is a method of improving growth, yield, health, increasing longevity, productivity, and/or vitality of a plant or plant part, and/or reducing abiotic stress in a plant or plant part, and/or protecting a plant, or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering plant architecture, said method comprising any of the following:

(a) using a polypeptide according to any one of embodiments 1-45 or a composition according to any one of embodiments 45-52 and 57-145 to the plant, plant part, or in the plant growth medium, or in the rhizosphere in the region surrounding the plant or plant part to improve growth, yield, health, lifespan, productivity and/or vitality of a plant or plant part, and/or reduce abiotic stress on a plant or plant part; and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering the architecture of the plant; or

(b) using a polypeptide according to any one of embodiments 1-45 or a composition according to any one of embodiments 45-52 and 57-145 in a plant growth medium to improve growth, yield, health, longevity, productivity and/or the vitality of the plant or plant part to be grown in said plant growth medium and/or the reduction of abiotic stress in the plant or plant part to be grown in said plant growth medium and/or the protection of the plant or plant part to be grow in said plant growth medium, against disease, insects and/or nematodes, and/or increase innate immune response, and/or change in architecture of the plant or plant part to be grown in said plant growth medium; or

(c) applying the recombinant microorganism according to any one of embodiments 53-56, 102, and 105 on the plant, on the plant part or in the plant growth medium, or in the rhizosphere in the region surrounding the plant or plant part, to improve growth, yield, condition health, increase in lifespan, productivity and/or vitality of a plant or plant part, and/or reduction of abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease, insects and/or nematodes, and/or enhancing the innate immune response of the plant or plant part, and/or altering the architecture of the plant, wherein said recombinant microorganism expresses the polypeptide and the expression of the polypeptide is increased compared to with the expression level of said polypeptide in a wild-type microorganism of the same species under the same conditions.

[0804] Embodiment 148 is a method according to embodiment 147, wherein said polypeptide or composition comprises: a Flg22 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide comprises any of SEQ ID NOs: 226-300 and 571-573, or any combination of them; a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450 or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0805] Embodiment 149 is the method of Embodiment 147, wherein said polypeptide or composition comprises: a FlgII-28 polypeptide, wherein the amino acid sequence of said FlgII-28 polypeptide comprises any of SEQ ID NOs: 301-375 or any combination of them; retro-inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro-inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525 or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0806] Embodiment 150 is a method according to embodiment 147, wherein said polypeptide or composition comprises: A retro-inverse Flg22 polypeptide, wherein the amino acid sequence of said retro-inverse Flg22 polypeptide contains any of SEQ ID NOs: 376- 450 or any combination thereof; retro-inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro-inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525 or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0807] Embodiment 151 is the method of Embodiment 147, wherein said polypeptide or composition comprises: an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide comprises SEQ ID NOs: 600, 603, 604, or any combination thereof; a Kunitz trypsin inhibitor (KTI) polypeptide, wherein the amino acid sequence of said KTI polypeptide comprises SEQ ID NO: 602; a retro inverse RHPP polypeptide, wherein the amino acid sequence of said RHPP RI contains SEQ ID NOs: 601, 605, 606, or any combination thereof; or any combination of the foregoing, to reduce abiotic stress in a plant or plant part; and/or protecting the plant or plant part from disease; and/or enhancing the innate immune response of the plant or plant part.

[0808] Embodiment 152 is a method according to any one of embodiments 147-151, wherein said abiotic stress includes heat stress, temperature stress, radiation stress, drought stress, cold stress, salinity stress, nutrient deficiency stress high metal stress, water stress, osmotic stress, or any combination of these.

[0809] Embodiment 153 is a method according to embodiment 147, wherein said polypeptide or composition comprises: a Flg22 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide comprises any of SEQ ID NOs: 226-300 and 571-573; a retro inverse Flg22 polypeptide, wherein the amino acid sequence of said retro inverse Flg22 polypeptide comprises any of SEQ ID NOs: 376-450; or any combination of the above, to protect the plant or plant part from disease and/or enhance the innate immune response of the plant or plant part.

[0810] Embodiment 154 is a method according to embodiment 147 or 153, wherein said polypeptide or composition comprises: a FlgII-28 polypeptide, wherein the amino acid sequence of said FlgII-28 polypeptide contains any of SEQ ID NOs: 301- 375; retro-inverse FlgII-28 polypeptide, wherein the amino acid sequence of said retro-inverse FlgII-28 polypeptide comprises any of SEQ ID NOs: 451-525; or any combination of the above, to protect the plant or plant part from disease and/or enhance the innate immune response of the plant or plant part.

[0811] Embodiment 155 is a method according to embodiment 147, wherein said polypeptide or composition comprises: a Flg22 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide comprises SEQ ID NOs: 226, 752, or 571; and EF-Tu polypeptides, wherein the amino acid sequences of said EF-Tu polypeptides comprise SEQ ID NOs: 616 and 617, to protect the plant or plant part from disease and/or enhance the innate immune response of the plant or plant part.

[0812] Embodiment 156 is the method of Embodiment 147, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 289, 290, 291, 293, 294, 295, 300, 437, 532, 534, 536, 538, 540, 571-586 and 751-766, or any combination thereof, for protecting a plant or plant part from disease, insects, or nematodes.

[0813] Embodiment 157 is the method of Embodiment 156, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 293, 295, 300, 540, 571,574, 751, and 752 , or any combination of them.

[0814] Embodiment 158 is a method according to any of embodiments 147 and 150-157, wherein said disease includes Asian citrus greening, Huanglong disease (HLB), Asian soybean rust, Sclerotinia stem rot (or white mold) leaf spot caused by Pseudomonas or leaf spot cercosporiosis.

[0815] Embodiment 159 is a method according to embodiment 158, wherein said polypeptide or composition comprises a Flg22 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide comprises any of SEQ ID NOs: 226-300 and 571-573, or any their combination.

[0816] Embodiment 160 is the method of Embodiment 158, wherein said polypeptide or composition comprises a FlgII-28 polypeptide, wherein the amino acid sequence of said FlgII-28 polypeptide comprises any of SEQ ID NOs: 301-375 or 751 , or any combination of them.

[0817] Embodiment 161 is a method according to embodiment 158, wherein said polypeptide or composition comprises a Flg22 polypeptide and a FlgII-28 polypeptide, wherein the amino acid sequence of said Flg22 polypeptide comprises any of SEQ ID NOs: 226-300 and 571-573 or any combination thereof, and the amino acid sequence of the specified FlgII-28 polypeptide contains any of SEQ ID NO: 301-375 or 751 or any combination thereof.

[0818] Embodiment 162 is the method of Embodiment 161, wherein said polypeptide or composition further comprises a Flg22 retro inverse polypeptide, a FlgII-28 retro inverse polypeptide, or a combination thereof, wherein the amino acid sequence of said retro inverse the Flg22 polypeptide contains any of SEQ ID NOs: 376-450 or any combination thereof, and the amino acid sequence of said retro-inverse FlgII-28 polypeptide contains any of SEQ ID NOs: 451-525 or any combination thereof.

[0819] Embodiment 163 is a method according to embodiment 147, wherein said polypeptide or composition comprises an RHPP polypeptide and/or an RHPP RI polypeptide to increase yield, improve growth and/or productivity of a plant or plant part, and/ or changes in plant architecture.

[0820] Embodiment 164 is the method of Embodiment 163, wherein said RHPP polypeptide comprises SEQ ID NO: 600.

[0821] Embodiment 165 is the method of embodiment 163 or 164, wherein said growth includes root growth, root length, root biomass, nodulation, total biomass, above ground biomass, or any combination thereof.

[0822] Embodiment 166 is a method according to any one of embodiments 163-165, wherein said plant includes soybean, growth includes total root length, root biomass, nodulation, number of nodules per plant, total biomass, biomass above surface land or any combination thereof, and productivity includes the total number of pods or the number of pods per node.

[0823] Embodiment 167 is a method according to any one of embodiments 163-166, wherein the plant architecture includes favorable outcomes for the plant or plant part.

[0824] Embodiment 168 is the method of Embodiment 167 wherein said beneficial outcomes include the possibility of increased planting density in a field of plants.

[0825] Embodiment 169 is a method according to embodiment 147, wherein said polypeptide or composition comprises a harpin-like polypeptide or an RHPP polypeptide, to protect a plant or plant part from disease, insects and/or nematodes, and/or enhance innate immune response of a plant or part of a plant.

[0826] Embodiment 170 is a method according to embodiment 147, wherein said polypeptide or said composition comprises a CSF polypeptide, to increase the yield of a plant or plant part in a heat and drought prone environment.

[0827] Embodiment 171 is a method according to embodiment 170, wherein said polypeptide, said composition, or said recombinant microorganism is applied just prior to flower formation or in a pre-flowering phase.

[0828] Embodiment 172 is a method according to embodiment 147, wherein said polypeptide or composition comprises an CSF, RHPP, harpin or harpin-like polypeptide, or a combination thereof, to improve the growth of a plant or plant part.

[0829] Embodiment 173 is the method of Embodiment 172, wherein said growth includes root and flower apical meristems, flower organ formation, fruit development, fruit formation, number of flower organs, flower organ size, or a combination thereof.

[0830] Embodiment 174 is a method according to embodiment 147, wherein said polypeptide or composition comprises a CSF polypeptide and a harpin or harpin-like polypeptide, to improve the growth and productivity of a plant or plant part in an environment prone to both stress and and to non-stressful conditions for plant growth.

[0831] Embodiment 175 is the method of Embodiment 147, wherein said polypeptide or composition contains a thionine or a thionine-like polypeptide.

[0832] Embodiment 176 is the method of Embodiment 175, wherein said thionin or thionin-like polypeptide is fused to a phloem targeting sequence to form a fusion polypeptide, wherein said phloem targeting sequence contains any of SEQ ID NO:641 in the amino acid sequence -649, or any combination thereof, to deliver said fusion polypeptide to vascular tissue or vascular cells and/or phloem or phloem-associated tissue or phloem-associated cells in a plant or plant part.

[0833] Embodiment 177 is the method of Embodiment 147, wherein said polypeptides include Flg22 polypeptides.

[0834] Embodiment 178 is the method of Embodiment 177, wherein said polypeptides comprise SEQ ID NOS: 526 and 527.

[0835] Embodiment 179 is the method of Embodiment 177, wherein said polypeptides comprise SEQ ID NOS: 226 and 227.

[0836] Embodiment 180 is the method of Embodiment 175 or 176 wherein said disease includes Asian citrus disease (HLB), citrus canker, leaf blight, or disease-causing bacteria.

[0837] Embodiment 181 is the method of Embodiment 180, wherein said disease-causing bacteria include bacterial leaf blight, bacterial stem rot, bacterial leaf spot, bacterial leaf blight, bacterial blossom end rot, bacterial streak, chocolate blotch, bacterial wilt and goss rot, red blotch (holcus), purple leaf sheath blotch, seed rot, white seedling rot, Stewart's disease (bacterial wilt), corn stunting, bacterial blight, Pierce's disease, citrus variegated chlorosis, citrus canker, Pseudomonas syringae serovars; or a combination of the above.

[0838] Embodiment 182 is the method of Embodiment 147, wherein said polypeptide or composition comprises flagellin or a flagellin-like polypeptide, wherein the amino acid sequence of said flagellin or flagellin-like polypeptide comprises any of SEQ ID NO: 226 -525 and 571-573, or any combination of them.

[0839] Embodiment 183 is the method of Embodiment 147, wherein said disease comprises Asian soybean rust caused by Cercospora or Sclerotinia stem rot (or white mold), and said polypeptide or composition comprises:

flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 752 and 571; or

an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide comprises SEQ ID NO: 600; or

flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 752 and 571; and an RHPP polypeptide, wherein the amino acid sequence of said RHPP polypeptide contains SEQ ID NO: 600.

[0840] Embodiment 184 is the method of Embodiment 183, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226.

[0841] Embodiment 185 is the method of 183 or 184, wherein said composition further comprises a fungicide.

[0842] Embodiment 186 is a method according to embodiment 147, wherein said disease comprises a bacterial disease, and said method comprises limiting bacterial growth and/or preventing said disease, and wherein the amino acid sequence of said flagellin or flagellin-associated the polypeptide contains any of SEQ ID NOs: 226, 540, 752 and 571, or any combination thereof.

[0843] Embodiment 187 is the method of Embodiment 186 wherein said bacteria include Pseudomonas syringae, patovar actinidiae.

[0844] Embodiment 188 is the method of Embodiment 187, wherein said plant includes kiwi fruit.

[0845] Embodiment 189 is a method according to embodiment 147, wherein said disease comprises citrus greening and said composition comprises a bactericide and flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 571 and 752, or any combination thereof.

[0846] Embodiment 190 is the method of 189, wherein said bactericide contains oxytetracycline.

[0847] Embodiment 191 is a method according to embodiment 147, wherein said disease comprises stem rot (or white mold) caused by Sclerotinia, and said composition comprises flagellin or a flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin -associated polypeptide contains any of SEQ ID NOS: 226, 540, 571, 751 and 752.

[0848] Embodiment 192 is a method according to any one of embodiments 147-191, wherein protecting a plant or plant part from a disease comprises prophylactic treatment (treatment), treatment (treatment), prevention, and reduction of disease progression on the plant or in plant or part of a plant.

[0849] Embodiment 193 is a method according to any one of embodiments 147-192, wherein said polypeptide, said composition, or said recombinant microorganism is applied exogenously to a plant, to a plant part, or to a plant growth medium.

[0850] Embodiment 194 is a method according to any one of embodiments 147-193, wherein said polypeptide, said composition, or said recombinant microorganism is applied endogenously to a plant or plant part.

[0851] Embodiment 195 is a method according to any one of embodiments 147-194, wherein said plant part includes a cell, leaf, branch, stem, flower, foliage, flower organ, fruit, pollen, vegetable, tuber, branch , bulb, pseudobulb, pod, root, root ball, rootstock, scion or seed.

[0852] Embodiment 196 is a method according to any one of embodiments 147-195, wherein said polypeptide, said composition, or said recombinant microorganism is applied to a plant surface, plant foliage, or plant seed surface.

[0853] Embodiment 197 is a method according to embodiment 196, wherein said polypeptide, said composition, or said recombinant microorganism is applied to a seed surface, and said plant or said plant part is grown from said seed.

[0854] Embodiment 198 is a method according to any one of embodiments 147-197, wherein said polypeptide, said composition, or said recombinant microorganism is used as a foliar application.

[0855] Embodiment 199 is a method according to any one of embodiments 147-198, wherein said plant is a fruit plant or vegetable plant, and said method provides increased fruit or vegetable yield.

[0856] Embodiment 200 is a method for producing a polypeptide, comprising obtaining a fusion protein comprising a polypeptide according to any one of embodiments 1-44 and an enterokinase (EK) cleavage site by fermentation, said enterokinase cleavage site enhancing the activity and stability of said polypeptide.

[0857] Embodiment 201 is the method of embodiment 200, further comprising exposing the prepared fusion protein to an enterokinase to cleave the cleavage site with the enterokinase and isolate said polypeptide.

[0858] Embodiment 202 is a method according to embodiment 200 or 201, wherein said enterokinase cleavage site contains SEQ ID NO: 772.

[0859] Embodiment 203 is a method according to any one of embodiments 200-202, wherein said fusion protein further comprises a protein tag.

[0860] Embodiment 204 is the method of Embodiment 203, wherein said protein tag contains glutathione-S-transferase (GST).

[0861] Embodiment 205 is a method according to any one of embodiments 200-204, wherein said fusion protein further comprises a secretion signal.

[0862] Embodiment 206 is the method of Embodiment 205, wherein said secretion signal comprises an amino acid sequence comprising any of SEQ ID NOs: 563-570 or 769, or any combination thereof.

--->

SEQUENCE LIST

<110>Spogen Biotech Inc./Spogen Biotech Inc.

Thompson, Brian / Thompson, Brian

Leslie, Michelle / Leslie, Michelle

<120>BIOACTIVE POLYPEPTIDES FOR IMPROVEMENTS IN PLANT PROTECTION,

GROWTH AND PRODUCTIVITY / BIOACTIVE POLYPEPTIDES FOR

ENSURE IMPROVED PLANT PROTECTION, GROWTH AND PRODUCTIVITY

<130>ELEN 3016.WO

<150>US 62/534710

<151>2017-07-20

<160>775

<170>PatentIn version 3.5

<210>1

<211>283

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<213>Bacillus thuringiensis

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<400>5

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys His Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg His Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Lys Ile Gly Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Glu Gly Gln Asn Arg Pro Ile Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Ile Asn Met Met Lys His Ile Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Leu Lys Ile Glu Asp Ala Leu Gln Ser Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Leu Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>6

<211>375

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>6

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asp

50 55 60

Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys Ser Ala Leu Gln Lys

100 105 110

Glu Phe Ala Gln Leu Gln Lys Gln Ile Thr Tyr Ile Ala Glu Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Asn Glu Asp Ser Glu Val Lys Ile

130 135 140

Gln Thr Leu Asp Ser Ser Lys Gly Glu Gln Gln Ile Thr Ile Asp Leu

145 150 155 160

Lys Ala Val Thr Leu Glu Lys Leu Asn Ile Lys Asp Ile Ala Ile Gly

165 170 175

Lys Ala Asp Ala Ala Asp Lys Pro Val Thr Pro Gly Ala Thr Val Asp

180 185 190

Gln Lys Asp Leu Asp Ser Val Thr Asp Lys Ile Ala Ala Leu Thr Glu

195 200 205

Thr Ser Ser Lys Ala Asp Ile Asp Ala Ile Gln Ser Ser Leu Asp Asn

210 215 220

Phe Lys Ala Ser Met Thr Pro Glu Asp Val Lys Thr Leu Glu Asp Ala

225 230 235 240

Leu Lys Gly Phe Lys Thr Gly Gln Ala Asn Pro Ala Asp Ala Gly Val

245 250 255

Asp Ala Ile Gln Asp Ala Leu Ser Lys Val Lys Leu Pro Thr Ala Thr

260 265 270

Ala Ala Ala Pro Ala Ala Asp Ala Asp Lys Ser Asp Ala Leu Ala Ala

275 280 285

Ile Ala Ala Ile Asp Ala Ala Leu Thr Lys Val Ala Asp Asn Arg Ala

290 295 300

Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu

305 310 315 320

Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp

325 330 335

Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu

340 345 350

Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln

355 360 365

Met Val Ser Lys Leu Leu Gln

370 375

<210>7

<211>416

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>7

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys Ala Leu Asp

130 135 140

Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Glu Asn Lys Thr Ile

165 170 175

Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Thr Lys Gln Ile Asn Ile

180 185 190

Asn Leu Ala Asp Ser Ser Ser Thr Ser Ala Leu Gln Ile Asp Lys Leu Thr

195 200 205

Ile Ser Gly Lys Thr Thr Asp Thr Thr Lys Thr Glu Thr Ile Thr Val

210 215 220

Thr Asp Asp Glu Ile Lys Ala Ala Lys Thr Asp Ile Asp Glu Phe Asn

225 230 235 240

Asp Ala Lys Lys Ala Leu Ala Asp Leu Lys Ala Glu Thr Ser Ala Gly

245 250 255

Lys Ala Asp Gly Ser Thr Asp Asp Glu Ile Lys Thr Ala Val Ser Asn

260 265 270

Phe Thr Lys Ser Phe Glu Lys Ile Gln Lys Phe Met Asn Asp Ser Asp

275 280 285

Ile Lys Thr Val Gln Thr Glu Ile Glu Lys Phe Asp Ala Ala Ala Pro

290 295 300

Ala Leu Asp Lys Ala Lys Gly Met Gly Ile Ala Phe Thr Ser Ala Met

305 310 315 320

Asp Pro Lys Ala Gly Thr Ile Thr Lys Ala Ala Thr Arg Gln Asn Ala

325 330 335

Ser Asp Ala Ile Lys Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser

340 345 350

Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val

355 360 365

Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln

370 375 380

Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe

385 390 395 400

Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Val

405 410 415

<210>8

<211>368

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>8

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Gln Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Glu Asn Lys Ala Ala Met Glu Lys

100 105 110

Glu Phe Gly Gln Leu Lys Asp Gln Ile Lys Tyr Ile Thr Asp Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Asp Ala Ala Ser Gly Thr Thr Lys

130 135 140

Ser Ile Ala Ile Gln Thr Leu Asp Ser Asp Gln Ala Ser Thr Gln Ile

145 150 155 160

Glu Ile Lys Ile Ala Gly Ser Ser Leu Ala Ala Leu Gly Leu Asp Lys

165 170 175

Val Gln Ile Gly Gln Glu Thr Val Ala Gln Lys Asp Leu Asp Val Leu

180 185 190

Thr Lys Ala Met Gly Arg Leu Ala Ala Pro Asp Ala Asp Ala Thr Thr

195 200 205

Arg Asp Leu Asp Val Gln Val Ala Lys Asp Ala Phe Asp Lys Val Lys

210 215 220

Gly Phe Ile Ala Asp Pro Ala Gln Ala Lys Ala Val Glu Arg Ala Phe

225 230 235 240

Glu Asp Tyr Thr Ala Ala Glu Ala Gly Lys Glu Glu Asp Ala Ala Lys

245 250 255

Ala Ile Asp Ala Ala Tyr Lys Lys Val Thr Gly Leu Thr Ala Gly Thr

260 265 270

Thr Gly Thr Val Asp Ala His Asn Ala Val Asn Lys Ile Asp Ala Ala

275 280 285

Leu Lys Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn

290 295 300

Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ala Ser Met

305 310 315 320

Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met

325 330 335

Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met

340 345 350

Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>9

<211>374

<212>PRT/Protein

<213>Bacillus cereus

<400>9

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Val Ala Leu Gln Lys

100 105 110

Glu Phe Gly Glu Leu Gln Lys Gln Ile Asp Tyr Ile Ala Lys Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Ser Gly Lys Ala Gly Ala Pro Asp

130 135 140

Gln Ala Leu Glu Ile Asn Ile Gln Thr Leu Asp Ser Ser Asp Pro Asn

145 150 155 160

Gln Gln Ile Lys Ile Ser Leu Asp Ser Val Ser Thr Ala Gln Leu Gly

165 170 175

Val Lys Asp Leu Gln Ile Gly Ser Ser Ser Ile Thr Gln Gln Gln Leu

180 185 190

Asp Thr Leu Asp Asn Ala Met Lys Arg Leu Glu Thr Ala Ser Thr Thr

195 200 205

Ala Ala Val Arg Asp Gln Asp Val Ala Asp Ala Lys Ala Ala Phe Glu

210 215 220

Asn Val Lys Gly Phe Phe Ser Glu Gly Asn Val Asp Ser Ile Asn Arg

225 230 235 240

Ala Phe Thr Asp Phe Ala Asn Glu Thr Thr Asn Lys Asp Asp Lys Ala

245 250 255

Glu Ala Ile Tyr Ala Leu Tyr Asn Asn Ala Thr Leu Ile Thr Lys Pro

260 265 270

Thr Pro Asp Ala Ser Asn Pro Ala Ser Val Asp Pro Ala Asn Ala Ile

275 280 285

Lys Lys Ile Asp Gln Ala Ile Glu Lys Ile Ala Ser Ser Arg Ala Thr

290 295 300

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

305 310 315 320

Ser Gln Gln Ser Ser Met Ala Ser Ala Ala Ser Gln Val Glu Asp Ala

325 330 335

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

340 345 350

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

355 360 365

Val Ser Lys Leu Leu Gln

370

<210>10

<211>266

<212>PRT/Protein

<213>Bacillus cereus

<400>10

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Phe

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Ile Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Val Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Thr Ser Gly Ile His Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Ile Leu Gln Arg Met Arg Asp Val Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Asp Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Arg Gln Asn Cys Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Ile Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Asn Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Thr Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Gln Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Tyr Lys Leu Leu Gln Ser

260 265

<210>11

<211>341

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>11

Met Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp

1 5 10 15

Ala Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly

20 25 30

Leu Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg

35 40 45

Thr Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met

50 55 60

Arg Asp Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ala Asp Asn

65 70 75 80

Gln Gln Ala Leu Gln Lys Glu Phe Gly Gln Leu Lys Glu Gln Ile Ser

85 90 95

Tyr Ile Ala Asp Asn Thr Glu Phe Asn Asp Lys Thr Leu Leu Lys Ala

100 105 110

Asp Asn Ser Val Lys Ile Gln Thr Leu Asp Ser Ala Asp Thr Asn Lys

115 120 125

Gln Ile Ser Ile Asp Leu Lys Gly Val Thr Leu Asn Gln Leu Gly Leu

130 135 140

Asp Thr Val Asn Ile Gly Ser Glu Lys Leu Ser Ala Glu Ser Leu Asn

145 150 155 160

Val Ala Lys Ala Thr Met Ala Arg Leu Val Lys Ala Asp Gln Asn Ala

165 170 175

Asp Pro Ser Thr Phe Ala Leu Asp Val Asn Thr Ala Lys Glu Ser Phe

180 185 190

Asp Lys Ile Lys Gly Phe Ile Ala Asn Lys Thr Asn Val Gln Asn Val

195 200 205

Glu Asn Ala Phe Asn Asp Tyr Ala Val Ala Asp Pro Ala Asp Lys Ala

210 215 220

Asp Lys Ala Asp Ala Ile Gln Ala Ala Phe Asn Thr Ala Ile Thr Gly

225 230 235 240

Leu Thr Ala Gly Thr Pro Asn Thr Ser Asn Pro Ser Ser Ala Val Asp

245 250 255

Ser Ile Asp Ala Ala Leu Lys Thr Val Ala Ser Asn Arg Ala Thr Leu

260 265 270

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

275 280 285

Gln Ser Ala Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp

290 295 300

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

305 310 315 320

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

325 330 335

Ser Lys Leu Leu Gln

340

<210>12

<211>367

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>12

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn Val Ala Ala Arg

50 55 60

Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala Met Gln Lys

100 105 110

Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile Ala Asp Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Ser Thr Ile Asn

130 135 140

Ile Gln Thr Leu Asp Ser His Asp Lys Asn Lys Gln Ile Thr Ile Ser

145 150 155 160

Leu Asp Ser Ala Ser Leu Lys Asn Leu Asp Ile Lys Asp Leu Ala Ile

165 170 175

Gly Ser Ala Thr Ile Asn Gln Thr Asp Leu Asp Thr Ala Thr Asn Ser

180 185 190

Met Lys Arg Leu Ala Thr Pro Ala Thr Asp Gly Lys Val Leu Ala Gln

195 200 205

Asp Ile Ala Asp Ala Lys Ala Ala Phe Asn Lys Val Gln Ser Ala Tyr

210 215 220

Thr Pro Ala Glu Val Asp Lys Ile Gln Asp Ala Phe Lys Ala Tyr Asp

225 230 235 240

Lys Leu Ala Ala Asp Pro Ala Ser Lys Ala Thr Asp Ile Ala Asp Ala

245 250 255

Ala Lys Asn Val Asn Thr Val Phe Gly Thr Leu Ala Thr Pro Thr Ala

260 265 270

Thr Lys Phe Asp Pro Ser Ser Ala Val Glu Lys Ile Asp Lys Ala Ile

275 280 285

Glu Thr Ile Ala Ser Ser Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Thr Asn Leu Lys Ser Gln Glu Asn Ser Met Ala

305 310 315 320

Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>13

<211>400

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>13

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn Val Ala Ala

85 90 95

Arg Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn

115 120 125

Gln Ser Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala Met Gln

130 135 140

Lys Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile Ala Asp Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Ser Thr Ile

165 170 175

Asn Ile Gln Thr Leu Asp Ser His Asp Lys Asn Lys Gln Ile Thr Ile

180 185 190

Ser Leu Asp Ser Ala Ser Leu Lys Asn Leu Asp Ile Lys Asp Leu Ala

195 200 205

Ile Gly Ser Ala Thr Ile Asn Gln Thr Asp Leu Asp Thr Ala Thr Asn

210 215 220

Ser Met Lys Arg Leu Ala Thr Pro Ala Thr Asp Gly Lys Val Leu Ala

225 230 235 240

Gln Asp Ile Ala Asp Ala Lys Ala Ala Phe Asn Lys Val Gln Ser Ala

245 250 255

Tyr Thr Pro Ala Glu Val Asp Lys Ile Gln Asp Ala Phe Lys Ala Tyr

260 265 270

Asp Lys Leu Ala Ala Asp Pro Ala Ser Lys Asp Thr Asp Ile Ala Asp

275 280 285

Ala Ala Lys Asn Val Asn Thr Val Phe Gly Thr Leu Ala Thr Pro Thr

290 295 300

Ala Thr Lys Phe Asp Pro Ser Ser Ala Val Glu Lys Ile Asp Lys Ala

305 310 315 320

Ile Glu Thr Ile Ala Ser Ser Arg Ala Thr Leu Gly Ala Thr Leu Asn

325 330 335

Arg Leu Asp Phe Asn Val Thr Asn Leu Lys Ser Gln Glu Asn Ser Met

340 345 350

Ala Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met

355 360 365

Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met

370 375 380

Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390 395 400

<210>14

<211>367

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>14

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn Val Ala Ala Arg

50 55 60

Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala Met Gln Lys

100 105 110

Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile Ala Asp Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Ser Thr Ile Asn

130 135 140

Ile Gln Ala Leu Asp Ser His Asp Lys Asn Lys Gln Ile Thr Ile Ser

145 150 155 160

Leu Asp Ser Ala Ser Leu Lys Asn Leu Asp Ile Lys Asp Leu Ala Ile

165 170 175

Gly Ser Ala Thr Ile Asn Gln Thr Asp Leu Asp Thr Ala Thr Asn Ser

180 185 190

Met Lys Arg Leu Ala Thr Pro Ala Thr Asp Gly Lys Val Leu Ala Gln

195 200 205

Asp Ile Ala Asp Ala Lys Ala Ala Phe Asn Lys Val Gln Ser Ala Tyr

210 215 220

Thr Pro Ala Glu Val Asp Lys Ile Gln Asp Ala Phe Lys Ala Tyr Asp

225 230 235 240

Lys Leu Ala Ala Asp Pro Ala Ser Lys Asp Thr Asp Ile Ala Asp Ala

245 250 255

Ala Lys Asn Val Asn Thr Val Phe Gly Thr Leu Ala Thr Pro Thr Ala

260 265 270

Thr Lys Phe Asp Pro Ser Ser Ala Val Glu Lys Ile Asp Lys Ala Ile

275 280 285

Glu Thr Ile Ala Ser Ser Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Thr Asn Leu Lys Ser Gln Glu Asn Ser Met Ala

305 310 315 320

Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>15

<211>397

<212>PRT/Protein

<213>Bacillus cereus

<400>15

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Thr Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Ser Thr Ser Ala Leu Lys Ile Glu Lys Leu Thr Ile

165 170 175

Ser Gly Ser Thr Ala Ile Ala Gly Lys Thr Glu Lys Val Thr Ile Thr

180 185 190

Ala Glu Asp Ile Lys Ala Ala Glu Glu Asp Ile Lys Ala Phe Thr Gln

195 200 205

Ala Gln Glu Gly Leu Ala Asn Leu Val Lys Glu Val Lys Asp Thr Asp

210 215 220

Gly Ser Val Lys Thr Pro Gly Ser Thr Pro Asp Asp Ile Lys Lys Ala

225 230 235 240

Val Thr Ala Phe Thr Glu Ser Phe Glu Lys Met Lys Lys Phe Met Asn

245 250 255

Asp Glu Asp Ile Thr Lys Val Glu Glu Lys Ile Lys Ala Phe Asp Ala

260 265 270

Ala Ser Pro Asp Leu Asp Ala Ala Lys Glu Met Gly Thr Ala Phe Thr

275 280 285

Ala Ala Met Lys Pro Ala Ala Gly Glu Ile Thr Lys Ala Ala Met Lys

290 295 300

Pro Asn Ala Ser Asp Ala Ile Lys Ser Ile Asp Glu Ala Leu Glu Thr

305 310 315 320

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

325 330 335

Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala

340 345 350

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

355 360 365

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

370 375 380

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390 395

<210>16

<211>266

<212>PRT/Protein

<213>Bacillus cereus

<400>16

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Leu Ala Ile Arg

50 55 60

Asn Asn Glu Asp Thr Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Leu Thr Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Asp His Thr Ile Asn Met Thr Lys His Ile Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Leu Lys Ile Glu Glu Ala Leu Gln Ser Val Ser Ile His

180 185 190

Arg Ala Asp Leu Gly Ser Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>17

<211>266

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>17

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Val Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Val Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Leu Asn Lys Asn Arg Asp Ser Leu Asn Asn

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Asp Glu Thr Thr

115 120 125

Ala Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Ile Ser Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Asn Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu Tyr

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Tyr Lys Leu Leu Gln Ser

260 265

<210>18

<211>460

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>18

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Asn Val Ala Ala Asp

50 55 60

Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Ser Asn Lys Ser Ala Leu Gln Lys

100 105 110

Glu Phe Ala Glu Leu Gln Lys Gln Ile Thr Tyr Ile Ala Asp Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Lys Glu Asp Ser Glu Val Lys Ile

130 135 140

Gln Thr Leu Asp Ser Ser Lys Gly Glu Gln Gln Ile Gly Ile Asp Leu

145 150 155 160

Lys Ala Val Thr Leu Glu Lys Leu Gly Ile Asn Asn Ile Ser Ile Gly

165 170 175

Lys Ala Asp Gly Thr Thr Glu Gly Thr Lys Ala Asp Leu Thr Ala Leu

180 185 190

Gln Ala Ala Ala Lys Lys Leu Glu Lys Pro Asp Thr Gly Thr Met Glu

195 200 205

Lys Asp Val Lys Asp Ala Lys Glu Glu Phe Asp Lys Val Lys Ala Ser

210 215 220

Leu Ser Asp Glu Asp Val Lys Lys Ile Glu Ala Ala Phe Gly Glu Phe

225 230 235 240

Asp Lys Asp Lys Thr Asn Thr Thr Lys Ala Ser Asp Ile Phe Asn Ala

245 250 255

Ile Lys Asp Val Lys Leu Ala Asp Lys Ala Ala Ala Ala Pro Ala Pro

260 265 270

Ala Asp Leu Thr Lys Phe Lys Ala Ala Leu Asp Lys Leu Gln Thr Pro

275 280 285

Asn Ala Gly Thr Met Val Asp Asp Val Lys Asp Ala Lys Asp Glu Phe

290 295 300

Glu Lys Ile Lys Gly Ser Leu Ser Asp Ala Asp Ala Gln Lys Ile Gln

305 310 315 320

Ala Ala Phe Glu Glu Glu Phe Glu Lys Ala Asn Thr Asp Asp Ser Lys Ala

325 330 335

Ser Ala Ile Tyr Asn Leu Ala Lys Asp Val Lys Val Asn Ala Thr Asp

340 345 350

Thr Thr Thr Gly Thr Asp Lys Asp Thr Thr Thr Ser Thr Asp Lys Asp

355 360 365

Ala Ala Leu Ala Ala Ile Ala Ala Ile Asp Ala Ala Leu Thr Lys Val

370 375 380

Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe

385 390 395 400

Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala

405 410 415

Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr

420 425 430

Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala

435 440 445

Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

450 455 460

<210>19

<211>367

<212>PRT/Protein

<213>Bacillus cereus

<400>19

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Ala Glu Asn Lys Ala Ala Met Gln Lys

100 105 110

Glu Phe Gly Glu Leu Lys Asp Gln Ile Lys Tyr Ile Ser Glu Asn Thr

115 120 125

Gln Phe Asn Asp Gln His Leu Leu Asn Ala Ala Lys Gly Ser Thr Asn

130 135 140

Glu Ile Ala Ile Gln Thr Leu Asp Ser Asp Ser Ser Ser Lys Gln Ile

145 150 155 160

Lys Ile Thr Leu Gln Gly Ala Ser Leu Asp Ser Leu Asp Ile Lys Asp

165 170 175

Leu Gln Ile Gly Ser Gly Ser Thr Val Ser Gln Thr Asp Leu Asp Val

180 185 190

Leu Asp Ala Thr Met Thr Arg Val Lys Thr Ala Thr Gly Ala Thr Arg

195 200 205

Asp Val Asp Val Gln Ala Ala Lys Ser Ala Phe Asp Lys Val Lys Gly

210 215 220

Leu Met Thr Lys Pro Ala Glu Val Lys Ala Ile Glu Arg Ala Phe Glu

225 230 235 240

Asp Tyr Asn Ala Gly Lys Thr Asp Ala Leu Ala Thr Ala Ile Glu Ala

245 250 255

Ala Tyr Thr Ala Asn Lys Thr Gly Leu Pro Ala Pro Ala Ala Ala Ala

260 265 270

Gly Thr Val Asp Ala Leu Gly Ala Ile Thr Lys Ile Asp Ala Ala Leu

275 280 285

Lys Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ala Ser Met Ala

305 310 315 320

Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>20

<211>377

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>20

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Thr Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Thr Thr Ala Leu Asn Ile Asp Lys Leu Ser Ile

165 170 175

Glu Gly Thr Gly Asn Lys Thr Ile Thr Leu Thr Ala Ala Asp Ile Ala

180 185 190

Lys Asp Lys Ala Asn Ile Asp Ala Val Gly Thr Ala Lys Thr Ala Leu

195 200 205

Ala Gly Leu Thr Gly Thr Pro Ala Ala Ala Ala Ile Asn Ser Ala Val

210 215 220

Ala Asp Phe Lys Thr Ala Phe Ala Lys Ala Asp Lys Asn Leu Met Ser

225 230 235 240

Asp Ala Gln Ile Lys Ala Val Thr Asp Ala Ile Thr Ala Phe Glu Ala

245 250 255

Asp Ala Thr Pro Asp Leu Thr Lys Ala Lys Ala Ile Gly Thr Ala Tyr

260 265 270

Thr Ala Pro Ala Ala Gly Asp Ile Thr Lys Ala Ser Pro Asn Ala Ser

275 280 285

Glu Ala Ile Lys Ser Ile Asp Ala Ala Leu Asp Thr Ile Ala Ser Asn

290 295 300

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

305 310 315 320

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

325 330 335

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

340 345 350

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

355 360 365

Pro Gln Met Val Ser Lys Leu Leu Gln

370 375

<210>21

<211>367

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>21

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln Gln Ala Leu Gln Lys

100 105 110

Glu Phe Gly Gln Leu Lys Glu Gln Ile Ser Tyr Ile Ala Asp Asn Thr

115 120 125

Glu Phe Asn Asp Lys Thr Leu Leu Lys Ala Asp Asn Ser Val Lys Ile

130 135 140

Gln Thr Leu Asp Ser Ala Asp Thr Asn Lys Gln Ile Ser Ile Asp Leu

145 150 155 160

Lys Gly Val Thr Leu Asn Gln Leu Gly Leu Asp Thr Val Asn Ile Gly

165 170 175

Ser Glu Thr Leu Ser Ala Glu Ser Leu Asn Val Ala Lys Ala Thr Met

180 185 190

Ala Arg Leu Val Lys Ala Asp Gln Asn Ala Asp Pro Ser Thr Phe Ala

195 200 205

Leu Asp Val Asn Thr Ala Lys Glu Ser Phe Asp Lys Ile Lys Gly Phe

210 215 220

Ile Thr Asn Lys Thr Asn Val Gln Asn Val Glu Asn Ala Phe Asn Asp

225 230 235 240

Tyr Thr Val Ala Asp Pro Ala Asp Lys Ala Asp Lys Ala Asp Ala Ile

245 250 255

Gln Ala Ala Phe Asn Thr Ala Ile Thr Gly Leu Thr Ala Gly Thr Pro

260 265 270

Asn Thr Ser Asn Pro Ser Ser Ala Val Asp Ala Ile Asp Ala Ala Leu

275 280 285

Lys Thr Val Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ala Ser Met Ala

305 310 315 320

Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>22

<211>266

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>22

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Phe Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Val Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Thr Ser Pro

145 150 155 160

Ser Pro Thr Lys His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Phe Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>23

<211>367

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>23

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln Gln Ala Leu Gln Lys

100 105 110

Glu Phe Gly Gln Leu Lys Glu Gln Ile Ser Tyr Ile Ala Asp Asn Thr

115 120 125

Glu Phe Asn Asp Lys Thr Leu Leu Lys Ala Asp Asn Ser Val Lys Ile

130 135 140

Gln Thr Leu Asp Ser Ala Asp Thr Asn Lys Gln Ile Ser Ile Asp Leu

145 150 155 160

Lys Gly Val Thr Leu Asn Gln Leu Gly Leu Asp Thr Val Asn Ile Gly

165 170 175

Ser Glu Thr Leu Ser Ala Glu Ser Leu Asn Val Ala Lys Ala Thr Met

180 185 190

Ala Arg Leu Val Lys Ala Asp Gln Asn Ala Asp Pro Ser Thr Phe Ala

195 200 205

Leu Asp Val Asn Thr Ala Lys Glu Ser Phe Asp Lys Ile Lys Gly Phe

210 215 220

Ile Thr Asn Lys Thr Asn Val Gln Asn Val Glu Asn Ala Phe Asn Asp

225 230 235 240

Tyr Thr Val Ala Asp Pro Ala Asp Lys Ala Asp Lys Ala Asp Ala Ile

245 250 255

Gln Ala Ala Phe Asn Thr Ala Ile Thr Gly Leu Thr Ala Gly Thr Pro

260 265 270

Asn Thr Ser Asn Pro Ser Ser Ala Val Asp Ala Ile Asp Ala Ala Leu

275 280 285

Lys Thr Val Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ala Ser Met Ala

305 310 315 320

Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>24

<211>266

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>24

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Ile Val Ile

35 40 45

Val Thr Arg Met Tyr Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Ile Leu Gln His Met Arg Asp Phe Ala Ile Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Asn Thr Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Pro Ile Gly Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Ile Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Ile Asn Met Thr Lys His Ile Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ser Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Met Ala Leu Ile Asp Thr Ala Ser Gln Val

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Ile Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Ala Val Ala Leu Ser Val Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Ile Val Ser Lys Leu Leu Gln Ser

260 265

<210>25

<211>381

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>25

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala Leu Asp Lys

100 105 110

Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Gln Lys Leu Leu Asp Gly Ser Lys Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Asn Lys Gln Ile Asp Ile Gln

145 150 155 160

Leu Ser Asn Val Ser Thr Lys Glu Leu Lys Leu Asp Thr Leu Ser Ile

165 170 175

Glu Gly Ser Ser Ser Lys Thr Phe Thr Ile Thr Ala Asp Asp Met Leu

180 185 190

Ala Val Gly Thr Ala Asn Ala Thr Ala Lys Ala Lys Ala Gly Thr Leu

195 200 205

Lys Gly Leu Asn Val Thr Thr Gly Asp Leu Thr Ala Ala Lys Thr Asp

210 215 220

Val Gln Asp Phe Arg Ala Ala Phe Asp Lys Val Lys Gly Phe Met Gly

225 230 235 240

Ser Thr Glu Val Thr Asn Ile Glu Lys Ala Leu Thr Lys Phe Asp Gly

245 250 255

Asp Gln Ser Leu Ala Asn Ala Lys Ala Ile Gly Asp Ala Leu Thr Ser

260 265 270

Asp Leu Ala Thr Thr Ile Ala Lys Asp Gln Thr Tyr Ser Lys Asn Val

275 280 285

Ser Asn Ala Ser Ser Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser

290 295 300

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

305 310 315 320

Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala

325 330 335

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

340 345 350

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

355 360 365

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

370 375 380

<210>26

<211>381

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>26

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala Leu Asp Lys

100 105 110

Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Gln Lys Leu Leu Asp Gly Ser Lys Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Asn Lys Gln Ile Asp Ile Gln

145 150 155 160

Leu Ser Asn Val Ser Thr Lys Glu Leu Lys Leu Asp Thr Leu Ser Ile

165 170 175

Glu Gly Ser Ser Ser Lys Thr Phe Thr Ile Thr Ala Asp Asp Met Leu

180 185 190

Ala Val Gly Thr Ala Asn Ala Thr Ala Lys Ala Lys Ala Gly Thr Leu

195 200 205

Lys Gly Leu Asn Val Thr Thr Gly Asp Leu Thr Ala Ala Lys Thr Asp

210 215 220

Val Gln Asp Phe Arg Ala Ala Phe Asp Lys Val Lys Gly Phe Met Gly

225 230 235 240

Ser Thr Glu Val Thr Asn Ile Glu Lys Ala Leu Thr Lys Phe Asp Gly

245 250 255

Asp Gln Ser Leu Ala Asn Ala Lys Ala Ile Gly Asp Ala Leu Thr Ser

260 265 270

Asp Leu Ala Thr Thr Ile Ala Lys Asp Gln Thr Tyr Ser Lys Asn Val

275 280 285

Ser Asn Ala Ser Ser Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser

290 295 300

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

305 310 315 320

Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala

325 330 335

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

340 345 350

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

355 360 365

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

370 375 380

<210>27

<211>381

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>27

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala Leu Asp Lys

100 105 110

Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Gln Lys Leu Leu Asp Gly Ser Lys Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Asn Lys Gln Ile Asp Ile Gln

145 150 155 160

Leu Ser Asn Val Ser Thr Lys Glu Leu Lys Leu Asp Thr Leu Ser Ile

165 170 175

Glu Gly Ser Ser Ser Lys Thr Phe Thr Ile Thr Ala Asp Asp Met Leu

180 185 190

Ala Val Gly Thr Ala Asn Ala Thr Ala Lys Ala Lys Ala Gly Thr Leu

195 200 205

Lys Gly Leu Asn Val Thr Thr Gly Asp Leu Thr Ala Ala Lys Thr Asp

210 215 220

Val Gln Asp Phe Arg Ala Ala Phe Asp Lys Val Lys Gly Phe Met Gly

225 230 235 240

Ser Thr Glu Val Thr Asn Ile Glu Lys Ala Leu Thr Lys Phe Asp Gly

245 250 255

Asp Gln Ser Leu Ala Asn Ala Lys Ala Ile Gly Asp Ala Leu Thr Ser

260 265 270

Asp Leu Ala Thr Thr Ile Ala Lys Asp Gln Thr Tyr Ser Lys Asn Val

275 280 285

Ser Asn Ala Ser Ser Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser

290 295 300

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

305 310 315 320

Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala

325 330 335

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

340 345 350

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

355 360 365

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

370 375 380

<210>28

<211>397

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>28

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala Ala Leu Asn

130 135 140

Lys Glu Phe Asp Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Thr Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Thr Ile

165 170 175

Ala Val Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys Gln Ile Asn Ile

180 185 190

Asn Leu Ser Asn Val Ser Thr Lys Glu Leu Gly Leu Asp Thr Leu Ser

195 200 205

Ile Gly Thr Asp Lys Val Glu Lys Thr Val Tyr Asp Ala Thr Thr Lys

210 215 220

Ala Phe Ala Asp Leu Gly Ala Lys Thr Gly Ala Asp Lys Ala Ala Phe

225 230 235 240

Asp Ala Asp Val Thr Ala Ala Met Lys Glu Phe Asp Lys Val Lys Pro

245 250 255

Phe Met Ser Ala Asp Asp Val Lys Lys Ile Glu Thr Lys Leu Glu Asp

260 265 270

Tyr Asn Lys Ala Asn Asp Ala Gly Ala Gln Thr Ala Ala Gln Ala Leu

275 280 285

Gly Lys Glu Phe Ala Thr Leu Thr Lys Leu Glu Thr Thr Asp Leu Lys

290 295 300

Ala Asn Ala Ser Gly Ala Ile Ala Ser Ile Asp Thr Ala Leu Lys Asn

305 310 315 320

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

325 330 335

Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala

340 345 350

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

355 360 365

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

370 375 380

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390 395

<210>29

<211>397

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>29

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala Ala Leu Asn

130 135 140

Lys Glu Phe Asp Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Thr Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Thr Ile

165 170 175

Ala Val Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys Gln Ile Asn Ile

180 185 190

Asn Leu Ser Asn Val Ser Thr Lys Glu Leu Gly Leu Ser Thr Leu Ser

195 200 205

Ile Gly Thr Asp Lys Val Glu Lys Thr Val Tyr Asp Ala Thr Thr Lys

210 215 220

Ala Phe Ala Asp Leu Gly Ala Lys Thr Gly Thr Asp Lys Ala Ala Phe

225 230 235 240

Ala Ala Asp Val Thr Ala Ala Met Lys Glu Phe Asp Lys Val Lys Pro

245 250 255

Phe Met Ser Ala Asp Asp Val Lys Lys Ile Glu Thr Lys Leu Glu Asp

260 265 270

Tyr Asn Lys Ala Asn Asp Ala Gly Ala Glu Ala Ala Ala Gln Ala Leu

275 280 285

Gly Lys Glu Phe Ala Thr Leu Thr Lys Leu Glu Thr Thr Asp Leu Lys

290 295 300

Ala Asn Ala Ser Gly Ala Ile Ala Ser Ile Asp Thr Ala Leu Lys Asn

305 310 315 320

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

325 330 335

Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala

340 345 350

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

355 360 365

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

370 375 380

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390 395

<210>30

<211>406

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>30

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Ser Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ser Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Glu Asn Gln Gln Ala Leu Asn Lys

100 105 110

Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Thr Lys Gln Ile Asn Ile Asp

145 150 155 160

Leu Ser Asn Val Ser Thr Asp Thr Leu Asn Ile Ser Gly Leu Thr Ile

165 170 175

Asn Gly Lys Lys Asp Ile Thr Val Thr Ile Ser Asp Lys Asp Ile Ala

180 185 190

Asn Ala Ala Thr Asp Ile Gly Lys Ala Thr Ser Ala Gln Gln Gly Leu

195 200 205

Ala Asp Leu Thr Asp Thr Thr Pro Ala Val Pro Asp Thr Pro Ala Val

210 215 220

Ile Gly Thr Gly Thr Ala Gly Asn Pro Gln Phe Pro Ala Val Lys Gly

225 230 235 240

Thr Pro Glu Ile Pro Gly Ser Ser Pro Ala Glu Ile Ala Lys Ala Val

245 250 255

Asp Asp Phe Lys Gln Ala Phe Asn Lys Val Lys Gly Leu Met Ser Asp

260 265 270

Ser Ala Val Ser Ala Met Glu Gln Lys Phe Ala Thr Phe Glu Lys Asp

275 280 285

Lys Ser Leu Ala Asn Ala Lys Asp Ile Gly Thr Ala Phe Ser Ala Pro

290 295 300

Ile Ala Gly Asn Ile Thr Lys Gly Glu Gln Asn Ala Ser Gly Ala Ile

305 310 315 320

Lys Ser Ile Asp Ala Ala Leu Glu Lys Ile Ala Ser Asn Arg Ala Thr

325 330 335

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

340 345 350

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

355 360 365

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

370 375 380

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

385 390 395 400

Val Ser Lys Leu Leu Gln

405

<210>31

<211>406

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>31

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala Leu Asp

130 135 140

Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile

165 170 175

Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Ala Lys Gln Ile Asn Ile

180 185 190

Asn Leu Ala Asp Ser Ser Thr Lys Ala Leu Asn Ile Asp Thr Leu Ser

195 200 205

Ile Ala Gly Thr Thr Asp Lys Thr Ile Thr Ile Thr Ala Lys Asp Leu

210 215 220

Thr Asp Asn Lys Thr Thr Leu Asp Ala Leu Lys Thr Ala Lys Asp Asp

225 230 235 240

Leu Ala Lys Leu Asp Asp Lys Ser Asp Gln Ala Thr Ile Asp Lys Ala

245 250 255

Val Asp Ala Phe Lys Thr Ala Phe Asn Asn Val Asp Lys Asn Leu Leu

260 265 270

Ser Asp Lys Ala Ile Glu Gly Ile Thr Glu Lys Met Thr Ala Phe Asp

275 280 285

Gly Thr His Thr Ala Ala Ala Ala Ile Gly Ala Ala Tyr Thr Glu Pro

290 295 300

Thr Ala Ala Asp Ile Lys Lys Ser Ala Pro Asn Ala Ser Gly Ala Ile

305 310 315 320

Lys Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr

325 330 335

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

340 345 350

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

355 360 365

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

370 375 380

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

385 390 395 400

Val Ser Lys Leu Leu Gln

405

<210>32

<211>266

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>32

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Val Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Leu Ser Met Leu Arg Thr Ala Glu Ala Thr Leu

65 70 75 80

Gln Thr Val Ala Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ser Asn Asp Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Ser Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Ile Ser Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Leu Leu His

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Ser Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Glu Leu Leu Gln Ser

260 265

<210>33

<211>393

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>33

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Glu Asn Lys Thr Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Thr Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Ser Thr Ser Ala Leu Gln Ile Asp Lys Leu Thr Ile

165 170 175

Ser Gly Lys Thr Thr Asp Thr Thr Lys Thr Gln Thr Ile Thr Val Thr

180 185 190

Asp Asp Glu Ile Lys Ala Ala Lys Thr Asp Ile Asp Glu Phe Asn Asp

195 200 205

Ala Lys Lys Ala Leu Ala Asp Leu Lys Ala Glu Ser Ala Pro Ser Lys

210 215 220

Gly Asp Gly Ser Ser Asp Asp Glu Ile Lys Glu Ala Val Ser Asn Phe

225 230 235 240

Lys Lys Ser Phe Glu Lys Ile Gln Lys Phe Met Asn Asp Ser Asp Ile

245 250 255

Lys Thr Val Gln Thr Glu Ile Glu Lys Phe Asp Ala Ala Ala Pro Ala

260 265 270

Leu Asp Lys Ala Lys Gly Met Gly Ile Ala Phe Thr Ser Ala Met Asp

275 280 285

Pro Lys Ala Gly Thr Ile Thr Lys Ala Ala Thr Arg Gln Asn Ala Ser

290 295 300

Asp Ala Ile Lys Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser Asn

305 310 315 320

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

325 330 335

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln Ile

340 345 350

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

355 360 365

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

370 375 380

Pro Gln Met Val Ser Lys Leu Leu Gln

385 390

<210>34

<211>426

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>34

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys Ala Leu Asp

130 135 140

Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Glu Asn Lys Thr Ile

165 170 175

Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Thr Lys Gln Ile Asn Ile

180 185 190

Asn Leu Ala Asp Ser Ser Ser Thr Ser Ala Leu Gln Ile Asp Lys Leu Thr

195 200 205

Ile Ser Gly Lys Thr Thr Asp Thr Thr Lys Thr Gln Thr Ile Thr Val

210 215 220

Thr Asp Asp Glu Ile Lys Ala Ala Lys Thr Asp Ile Asp Glu Phe Asn

225 230 235 240

Asp Ala Lys Lys Ala Leu Ala Asp Leu Lys Ala Glu Ser Ala Pro Ser

245 250 255

Lys Gly Asp Gly Ser Ser Asp Asp Glu Ile Lys Glu Ala Val Ser Asn

260 265 270

Phe Lys Lys Ser Phe Glu Lys Ile Gln Lys Phe Met Asn Asp Ser Asp

275 280 285

Ile Lys Thr Val Gln Thr Glu Ile Glu Lys Phe Asp Ala Ala Ala Pro

290 295 300

Ala Leu Asp Lys Ala Lys Gly Met Gly Ile Ala Phe Thr Ser Ala Met

305 310 315 320

Asp Pro Lys Ala Gly Thr Ile Thr Lys Ala Ala Thr Arg Gln Asn Ala

325 330 335

Ser Asp Ala Ile Lys Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser

340 345 350

Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val

355 360 365

Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln

370 375 380

Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe

385 390 395 400

Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln

405 410 415

Thr Pro Gln Met Val Ser Lys Leu Leu Gln

420 425

<210>35

<211>269

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>35

Met Ser Ile Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg

1 5 10 15

Gln Ser Leu Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His

20 25 30

Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn

35 40 45

Ile Val Ile Val Thr Arg Met Tyr Ala Arg Ala Ser Gly Met Arg Val

50 55 60

Ala Ile Arg Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu

65 70 75 80

Ala Ala Leu Gln Thr Val Thr Asn Ile Leu Gln His Met Arg Asp Phe

85 90 95

Ala Ile Gln Ser Ala Asn Gly Thr Asn Ser Asn Thr Asn Arg Asp Ser

100 105 110

Leu Asn Lys Glu Phe Gln Ser Leu Thr Glu Pro Ile Gly Tyr Ile Gly

115 120 125

Glu Thr Thr Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg

130 135 140

Pro Ile Thr Leu Asp Asp Ile Gly His Thr Ile Asn Met Thr Lys His

145 150 155 160

Ile Pro Pro Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln

165 170 175

Glu Ala Arg Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val

180 185 190

Ser Leu His Arg Ala Asp Leu Gly Ser Met Ile Asn Arg Leu Gln Phe

195 200 205

Asn Ile Glu Asn Leu Asn Ser Gln Ser Met Ala Leu Ile Asp Thr Ala

210 215 220

Ser Gln Val Glu Asp Ala Asp Met Ala Gln Glu Ile Ser Asp Phe Leu

225 230 235 240

Lys Phe Lys Leu Leu Thr Ala Val Ala Leu Ser Val Val Ser Gln Ala

245 250 255

Asn Gln Ile Pro Gln Ile Val Ser Lys Leu Leu Gln Ser

260 265

<210>36

<211>414

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>36

Met Ala Arg Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Asp Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala Leu Asp

130 135 140

Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile Ser Lys Asn

145 150 155 160

Thr Glu Phe Asn Asp Gln Lys Leu Leu Asp Gly Ser Lys Lys Ser Ile

165 170 175

Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Asn Lys Gln Ile Asp Ile

180 185 190

Gln Leu Ser Asn Val Ser Thr Lys Glu Leu Lys Leu Asp Thr Leu Ser

195 200 205

Ile Glu Gly Ser Ser Ser Lys Thr Phe Thr Ile Thr Ala Asp Asp Met

210 215 220

Leu Ala Val Gly Thr Ala Asn Ala Thr Ala Lys Ala Lys Ala Gly Thr

225 230 235 240

Leu Lys Gly Leu Asn Val Thr Thr Gly Asp Leu Thr Ala Ala Lys Thr

245 250 255

Asp Val Gln Asp Phe Arg Ala Ala Phe Asp Lys Val Lys Gly Phe Met

260 265 270

Gly Ser Thr Glu Val Thr Asn Ile Glu Lys Ala Leu Thr Lys Phe Asp

275 280 285

Gly Asp Gln Ser Leu Ala Asn Ala Lys Ala Ile Gly Asp Ala Leu Thr

290 295 300

Ser Asp Leu Ala Thr Thr Ile Ala Lys Asp Gln Thr Tyr Ser Lys Asn

305 310 315 320

Val Ser Asn Ala Ser Ser Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu

325 330 335

Ser Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

340 345 350

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser

355 360 365

Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

370 375 380

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

385 390 395 400

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

405 410

<210>37

<211>266

<212>PRT/Protein

<213>Bacillus cereus

<400>37

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asn Asn Pro Ala Asn Val Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Val Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Ser Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Asp Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Thr Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Ile Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Asn Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>38

<211>494

<212>PRT/Protein

<213>Bacillus cereus

<400>38

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Ser Val Ala Ala Asp

50 55 60

Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Val Ala Leu Gln Lys

100 105 110

Glu Phe Ala Ala Leu Lys Glu Gln Ile Thr Tyr Ile Ala Asp Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Asn Gly Asn Gln Thr Ile Asn Ile

130 135 140

Gln Thr Leu Asp Ser His Asp Ser Thr Lys Gln Ile Gly Ile Asp Leu

145 150 155 160

Lys Ser Ala Thr Leu Glu Ala Leu Gly Ile Lys Asp Leu Thr Val Gly

165 170 175

Ala Val Gly Ser Thr Glu Ala Lys Asn Tyr Val Asp Ala Lys Glu Ala

180 185 190

Leu Ala Lys Asn Val Ala Ala Asn Glu Phe Ile Asp Ala Lys Lys Ala

195 200 205

Leu Asp Gly Asn Ala Ile Ala Lys Gly Tyr Val Glu Ala Lys Thr Ala

210 215 220

Phe Asp Asp Ala Lys Pro Glu Val Lys Ala Leu Val Ser Asn Tyr Thr

225 230 235 240

Asp Ala Leu Ala Ala Leu Ala Lys Asp Asp Thr Asn Asp Asp Leu Lys

245 250 255

Lys Asp Val Ala Asp Thr Lys Ala Leu Met Asp Ala Asn Thr Val Ala

260 265 270

Lys Thr Tyr Phe Glu Ala Lys Thr Ala His Asp Gly Ala Asp Gln Ala

275 280 285

Ile Lys Asp Ile Val Thr Thr Tyr Asp Ser Lys Leu Gly Ala Leu Asp

290 295 300

Asp Ala Ala Asn Lys Ala Ile Ser Asp Phe Asp Lys Ala Lys Ala Ala

305 310 315 320

Phe Asp Glu Ser Pro Ala Ala Lys Glu Leu Val Lys Thr Met Asp Asp

325 330 335

Ala Lys Gln Ala Ala Thr Gln Asn Asn Thr Ala Asn Ala Tyr Leu Val

340 345 350

Ala Lys Ala Ala Ala Glu Leu Ala Pro Asn Asp Ala Asp Lys Lys Ala

355 360 365

Glu Leu Glu Asn Ala Thr Lys Ala Leu Glu Lys Asp Asp Thr Ala Lys

370 375 380

Gly Leu Val Lys Thr Tyr Glu Asn Ala Lys Glu Ala Leu Asn Pro Ala

385 390 395 400

Asn Ala Met Pro Leu Asp Ala Val Lys Gln Ile Asp Ala Ala Leu Lys

405 410 415

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

420 425 430

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ala Met Ala Ala

435 440 445

Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

450 455 460

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

465 470 475 480

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

485 490

<210>39

<211>267

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>39

Met Arg Ile Gly Thr Asn Phe Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Asn Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Ile Gln

85 90 95

Ser Ala Asn Ser Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Ser Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val His Ile Ser Lys Ser Ile Pro Pro

145 150 155 160

Pro Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala

165 170 175

Arg Ala Ala Ile Leu Lys Ile Glu Glu Ala Leu Gln Ser Val Ser Leu

180 185 190

His Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu His Phe Asn Ile

195 200 205

Glu Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg

210 215 220

Ile Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe

225 230 235 240

Lys Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln

245 250 255

Ile Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>40

<211>377

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>40

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Thr Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Thr Ser Ala Leu Asn Ile Asp Lys Leu Ser Ile

165 170 175

Glu Gly Thr Gly Asn Lys Thr Ile Thr Leu Thr Ala Ala Asp Ile Ala

180 185 190

Lys Asp Lys Thr Asn Ile Asp Ala Val Gly Thr Ala Lys Thr Ala Leu

195 200 205

Ala Gly Leu Thr Gly Thr Pro Ala Ala Ala Ala Ile Asn Ser Ala Val

210 215 220

Ala Asp Phe Lys Thr Ala Phe Ala Lys Ala Asp Lys Asn Leu Met Ser

225 230 235 240

Asp Ala Gln Ile Lys Ser Val Thr Asp Ala Ile Thr Ala Phe Glu Ala

245 250 255

Asp Ala Thr Pro Asp Leu Thr Lys Ala Lys Ala Ile Gly Thr Ala Tyr

260 265 270

Thr Ala Pro Ala Ala Gly Asp Ile Thr Lys Ala Ser Pro Asn Ala Ser

275 280 285

Glu Ala Ile Lys Ser Ile Asp Ala Ala Leu Asp Thr Ile Ala Ser Asn

290 295 300

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

305 310 315 320

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

325 330 335

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

340 345 350

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

355 360 365

Pro Gln Met Val Ser Lys Leu Leu Gln

370 375

<210>41

<211>406

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>41

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala Leu Asp

130 135 140

Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile

165 170 175

Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Ala Lys Gln Ile Asn Ile

180 185 190

Asn Leu Ala Asp Ser Ser Thr Lys Ala Leu Asn Ile Asp Thr Leu Ser

195 200 205

Ile Ala Gly Thr Thr Asp Lys Thr Ile Thr Ile Thr Ala Lys Asp Leu

210 215 220

Thr Asp Asn Lys Ala Thr Leu Asp Ala Leu Lys Thr Ala Lys Ala Asp

225 230 235 240

Leu Ala Lys Leu Asp Asp Lys Ser Asp Gln Ala Thr Ile Asp Lys Ala

245 250 255

Val Asp Ala Phe Lys Thr Ala Phe Asn Asn Val Asp Lys Asn Leu Leu

260 265 270

Ser Asp Lys Ala Ile Glu Gly Ile Thr Asp Lys Met Thr Ala Phe Asp

275 280 285

Gly Thr His Thr Ala Ala Ala Ala Ile Gly Thr Ala Tyr Thr Glu Pro

290 295 300

Thr Ala Gly Asp Ile Thr Lys Ser Ala Pro Asn Ala Ser Gly Ala Ile

305 310 315 320

Lys Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr

325 330 335

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

340 345 350

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

355 360 365

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

370 375 380

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

385 390 395 400

Val Ser Lys Leu Leu Gln

405

<210>42

<211>373

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>42

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Ala Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Thr Lys Ala Leu Asn Ile Asp Thr Leu Ser Ile

165 170 175

Ala Gly Thr Thr Asp Lys Thr Ile Thr Ile Thr Ala Lys Asp Leu Thr

180 185 190

Asp Asn Lys Ala Thr Leu Asp Ala Leu Lys Thr Ala Lys Ala Asp Leu

195 200 205

Ala Lys Leu Asp Asp Lys Ser Asp Gln Ala Thr Ile Asp Lys Ala Val

210 215 220

Asp Ala Phe Lys Thr Ala Phe Asn Asn Val Asp Lys Asn Leu Leu Ser

225 230 235 240

Asp Lys Ala Ile Glu Gly Ile Thr Asp Lys Met Thr Ala Phe Asp Gly

245 250 255

Thr His Thr Ala Ala Ala Ala Ile Gly Thr Ala Tyr Thr Glu Pro Thr

260 265 270

Ala Gly Asp Ile Thr Lys Ser Ala Pro Asn Ala Ser Gly Ala Ile Lys

275 280 285

Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr Leu

290 295 300

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

305 310 315 320

Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp

325 330 335

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

340 345 350

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

355 360 365

Ser Lys Leu Leu Gln

370

<210>43

<211>361

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>43

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asn Gly Asn Gln Ala Ala Leu Asn Lys

100 105 110

Glu Phe Asp Ala Leu Lys Gln Gln Ile Asn Tyr Ile Ser Thr Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Thr Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys Lys Ile Asp Ile Gln

145 150 155 160

Leu Ala Asp Val Ser Thr Lys Ser Leu Asn Ile Asp Lys Leu Lys Ile

165 170 175

Gly Gly Val Ser Lys Glu Thr Thr Asp Ala Val Gly Asp Thr Phe Thr

180 185 190

Lys Leu Ser Thr Thr Ala Thr Thr Asp Met Gly Ala Leu Lys Ile Glu

195 200 205

Val Glu Ala Ala Met Lys Glu Phe Asp Lys Val Lys Gly Ala Met Ser

210 215 220

Ala Glu Asp Ala Lys Ala Val Thr Asp Lys Leu Asp Ala Phe Asn Thr

225 230 235 240

Ala Ala Ala Ala Thr Asn Asp Ala Ala Thr Ile Ala Ala Ala Lys Ala

245 250 255

Leu Gly Ala Ala Phe Asp Lys Thr Lys Val Glu Met Ala Asp Pro Asn

260 265 270

Ala Ser Val Ala Ala Ile Asp Ser Ala Leu Glu Asn Ile Ala Ser Asn

275 280 285

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

290 295 300

Asn Leu Lys Ser Gln Gln Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

305 310 315 320

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

325 330 335

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

340 345 350

Pro Gln Met Val Ser Lys Leu Leu Gln

355 360

<210>44

<211>465

<212>PRT/Protein

<213>Bacillus cereus

<400>44

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ala Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala Leu Gln Lys

100 105 110

Glu Phe Gly Glu Leu Gln Lys Gln Ile Asp Tyr Ile Ala Gly Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Asp Gly Ser Asn Pro Ser Ile Ser

130 135 140

Ile Gln Thr Leu Asp Ser Ala Asp Gln Ser Lys Gln Ile Ser Ile Asp

145 150 155 160

Leu Lys Ser Ala Thr Leu Glu Ala Leu Gly Ile Lys Asp Leu Thr Val

165 170 175

Gly Ala Thr Glu Asn Thr Leu Ala Lys Ala Thr Ile Thr Ala Lys Asp

180 185 190

Ala Phe Asp Ala Ala Lys Asp Ala Ser Asp Ala Ala Lys Lys Glu Ile

195 200 205

Asp Ala Ala Ala Lys Asp Thr Pro Ser Lys Asn Asp Ala Gln Leu Ala

210 215 220

Lys Glu Tyr Ile Glu Ala Lys Ala Thr Leu Ala Thr Leu Lys Pro Thr

225 230 235 240

Asp Ala Thr Tyr Ala Ala Lys Ala Ala Glu Leu Asp Ala Ala Thr Thr

245 250 255

Ala Leu Asn Asp Asn Ala Lys Val Leu Val Asp Gly Tyr Glu Lys Lys

260 265 270

Leu Thr Thr Thr Lys Thr Lys Glu Ala Glu Tyr Thr Ala Ala Lys Glu

275 280 285

Gln Ser Thr Lys Ser Thr Ala Ala Ala Asp Leu Val Thr Lys Tyr Glu

290 295 300

Thr Ala Lys Ser Asn Ala Leu Gly Asn Asp Ile Ala Lys Glu Tyr Leu

305 310 315 320

Glu Ala Lys Thr Ala Tyr Glu Ala Asn Lys Asn Asp Ile Ser Ser Lys

325 330 335

Ser Arg Phe Glu Ala Ala Glu Thr Glu Leu Asn Lys Asp Ile Thr Ala

340 345 350

Asn Lys Ala Ala Lys Val Leu Val Glu Thr Tyr Glu Lys Ala Lys Thr

355 360 365

Ala Gly Thr Thr Glu Lys Ser Leu Val Ala Val Asp Lys Ile Asp Glu

370 375 380

Ala Leu Lys Thr Ile Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu

385 390 395 400

Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ala Ser

405 410 415

Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu

420 425 430

Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser

435 440 445

Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu

450 455 460

Gln

465

<210>45

<211>394

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>45

Met Thr Gly Ile Thr Ile Asn Leu Glu Ile Asp Phe Phe Ala Tyr Tyr

1 5 10 15

Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys Trp Gly Phe Leu

20 25 30

Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr

35 40 45

Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser

50 55 60

Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala

65 70 75 80

Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala

85 90 95

Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala

100 105 110

Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn

115 120 125

Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala Ala Leu Asn

130 135 140

Lys Glu Phe Asp Ala Leu Lys Glu Gln Ile Asn Tyr Ile Ser Thr Asn

145 150 155 160

Thr Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Thr Ile

165 170 175

Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys Lys Ile Asp Ile

180 185 190

Lys Leu Ala Asp Val Ser Thr Glu Ser Leu Lys Ile Asp Lys Leu Lys

195 200 205

Ile Gly Gly Val Ser Lys Glu Thr Thr Asp Ala Val Ser Glu Thr Phe

210 215 220

Thr Lys Leu Ser Thr Thr Lys Thr Thr Asp Lys Asp Ala Leu Lys Ala

225 230 235 240

Glu Val Glu Ala Ala Met Lys Glu Phe Asp Lys Val Lys Gly Ala Met

245 250 255

Ser Thr Glu Asp Ala Lys Ala Val Thr Asp Lys Leu Gly Leu Phe Asn

260 265 270

Thr Ala Ala Ala Gly Thr Asp Asp Thr Ala Ile Ala Thr Ala Ala Lys

275 280 285

Asn Leu Gly Ala Ala Phe Asp Lys Thr Lys Val Asn Met Ala Asp Pro

290 295 300

Asn Ala Ser Val Ala Ala Ile Asp Ser Ala Leu Glu Asn Ile Ala Ser

305 310 315 320

Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val

325 330 335

Asn Asn Leu Lys Ser Gln Gln Ser Ser Met Ala Ser Ala Ala Ser Gln

340 345 350

Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe

355 360 365

Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln

370 375 380

Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390

<210>46

<211>266

<212>PRT/Protein

<213>Bacillus cereus

<400>46

Met Arg Ile Gly Thr Asn Val Leu Ser Leu Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Ser Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ala Asn Asp Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Asp Glu Thr Thr

115 120 125

Asp Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Thr Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Ile Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Asn Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>47

<211>373

<212>PRT/Protein

<213>Bacillus cereus

<400>47

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ser Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys Ala Ala Met Gln Lys

100 105 110

Glu Phe Gly Glu Leu Lys Glu Gln Ile Lys Tyr Ile Ala Glu Asn Thr

115 120 125

Gln Phe Asn Asp Gln His Leu Leu Asn Ala Asp Lys Gly Ile Thr Lys

130 135 140

Glu Ile Ala Ile Gln Thr Leu Asp Ser Asp Ser Asp Ser Lys Gln Ile

145 150 155 160

Lys Ile Lys Leu Gln Gly Ser Ser Leu Glu Ala Leu Asp Ile Lys Asp

165 170 175

Leu Gln Ile Gly Asn Thr Glu Leu Ala Gln Lys Asp Leu Asp Leu Leu

180 185 190

Asn Ala Thr Met Asp Arg Leu Asp Ala Thr Val Pro Gly Thr Arg Asp

195 200 205

Val Asp Val Gln Ala Ala Lys Asp Ala Phe Asp Lys Val Lys Gly Phe

210 215 220

Tyr Thr Asn Ser Asp Ser Val Lys Ala Ile Glu Arg Ala Phe Glu Asp

225 230 235 240

Tyr Ala Thr Ala Ser Thr Ala Gly Thr Ala Lys Ala Asp Ala Ala Thr

245 250 255

Ala Ile Lys Ala Ala Phe Asp Leu Ala Ala Asn Lys Val Gly Lys Pro

260 265 270

Ala Thr Gly Gly Ala Gln Gly Ser Ala Asn Ser Leu Gly Ala Ile Thr

275 280 285

Lys Ile Asp Ala Ala Leu Lys Thr Val Ala Asp Asn Arg Ala Thr Leu

290 295 300

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

305 310 315 320

Gln Ala Ser Ser Met Ala Ala Ala Ala Ser Gln Val Glu Asp Ala Asp

325 330 335

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

340 345 350

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

355 360 365

Ser Lys Leu Leu Gln

370

<210>48

<211>447

<212>PRT/Protein

<213>Bacillus cereus

<400>48

Met Arg Ile Asn Thr Asn Ile Asn Ser Leu Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Asn Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Gly Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Ala Ala Met Gln Lys

100 105 110

Glu Phe Ala Glu Leu Gln Lys Gln Ile Thr Tyr Ile Ala Asp Asn Thr

115 120 125

Gln Phe Asn Asp Lys Asn Leu Leu Gln Ser Asn Ser Ser Ile Asn Ile

130 135 140

Gln Thr Leu Asp Ser Ser Asp Gly Asn Gln Gln Ile Gly Ile Glu Leu

145 150 155 160

Lys Ser Ala Ser Leu Lys Ser Leu Gly Ile Glu Asp Leu Ala Ile Gly

165 170 175

Ala Ser Val Asn Pro Leu Ala Lys Ala Thr Val Glu Ala Ser Glu Ala

180 185 190

Tyr Asp Lys Ala Lys Ala Asp Thr Ala Ala Phe Ala Lys Ser Ile Ala

195 200 205

Asp Thr Ala Ala Thr Gly Thr Gly Ala Ala Lys Ala Asp Ala Ala Ala

210 215 220

Val Asp Ala Tyr Ile Lys Glu Ala Asp Pro Thr Ala Lys Gly Asn Leu

225 230 235 240

Tyr Thr Gly Leu Thr Ala Asp Gln Lys Lys Leu Ala Asp Glu His Asn

245 250 255

Thr Leu Lys Ala Ala Glu Asp Gly Lys Lys Ala Glu Leu Thr Met Ala

260 265 270

Thr Thr Lys Ser Thr Ala Asp Gly Thr Ala Lys Gly Leu Val Asp Ala

275 280 285

Tyr Asp Asn Ala Lys Ser Asp Ala Met Asn Asp Pro Lys Ala Lys Ala

290 295 300

Tyr Leu Glu Ala Lys Met Ala Tyr Glu Lys Asp Thr Ser Asn Val Ala

305 310 315 320

Asn Lys Gln Lys Leu Asp Ser Thr Lys Glu Ala Met Glu Lys Asp Pro

325 330 335

Ala Ser Lys Asp Leu Val Val Lys Leu Asp Ala Ala Lys Ala Ala Ala

340 345 350

Thr Asn Gly Thr Pro Leu Asp Ala Val Ser Lys Ile Asp Ala Ala Leu

355 360 365

Lys Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

370 375 380

Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala

385 390 395 400

Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

405 410 415

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

420 425 430

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

435 440 445

<210>49

<211>373

<212>PRT/Protein

<213>Bacillus cereus

<400>49

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ser Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys Ala Ala Met Gln Lys

100 105 110

Glu Phe Gly Glu Leu Lys Glu Gln Ile Lys Tyr Ile Ala Glu Asn Thr

115 120 125

Gln Phe Asn Asp Gln His Leu Leu Asn Ala Asp Lys Gly Ile Thr Lys

130 135 140

Glu Ile Ala Ile Gln Thr Leu Asp Ser Asp Ser Asp Ser Lys Gln Ile

145 150 155 160

Lys Ile Lys Leu Gln Gly Ser Ser Leu Glu Ala Leu Asp Ile Lys Asp

165 170 175

Leu Gln Ile Gly Asn Thr Glu Leu Ala Gln Lys Asp Leu Asp Leu Leu

180 185 190

Asn Ala Thr Met Asp Arg Leu Asp Ala Thr Val Pro Gly Thr Arg Asp

195 200 205

Val Asp Val Gln Ala Ala Lys Asp Ala Phe Asp Lys Val Lys Gly Phe

210 215 220

Tyr Thr Asn Ser Asp Ser Val Lys Ala Ile Glu Arg Ala Phe Glu Asp

225 230 235 240

Tyr Ala Thr Ala Ser Thr Ala Gly Thr Ala Lys Ala Asp Ala Ala Thr

245 250 255

Ala Ile Lys Ala Ala Phe Asp Leu Ala Ala Asn Lys Val Gly Lys Pro

260 265 270

Ala Thr Gly Gly Ala Gln Gly Ser Ala Asn Ser Leu Gly Ala Ile Thr

275 280 285

Lys Ile Asp Ala Ala Leu Lys Thr Val Ala Asp Asn Arg Ala Thr Leu

290 295 300

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

305 310 315 320

Gln Ala Ser Ser Met Ala Ala Ala Ala Ser Gln Val Glu Asp Ala Asp

325 330 335

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

340 345 350

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

355 360 365

Ser Lys Leu Leu Gln

370

<210>50

<211>397

<212>PRT/Protein

<213>Bacillus cereus

<400>50

Met Asp Phe Phe Ala Tyr Tyr Arg Phe Ser Ile Cys Arg Lys Val Asn

1 5 10 15

Ile Lys Lys Trp Gly Phe Phe Tyr Met Arg Ile Asn Thr Asn Ile Asn

20 25 30

Ser Met Arg Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser

35 40 45

Asn Ala Met Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser

50 55 60

Asp Asp Ala Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu

65 70 75 80

Ser Gly Leu Gly Val Ala Ser Asn Asn Thr Gln Asp Gly Met Ser Leu

85 90 95

Ile Arg Thr Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu

100 105 110

Arg Met Arg Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn

115 120 125

Glu Asn Lys Ala Ala Met Gln Lys Glu Phe Gly Glu Leu Lys Glu Gln

130 135 140

Ile Lys Tyr Ile Ala Glu Asn Thr Gln Phe Asn Asp Gln His Leu Leu

145 150 155 160

Asn Ala Asp Lys Gly Ile Thr Lys Glu Ile Ala Ile Gln Thr Leu Asp

165 170 175

Ser Asp Ser Asp Ser Lys Gln Ile Lys Ile Lys Leu Gln Gly Ser Ser

180 185 190

Leu Glu Ala Leu Asp Ile Lys Asp Leu Gln Ile Gly Asn Thr Glu Leu

195 200 205

Ala Gln Lys Asp Leu Asp Leu Leu Asn Ala Thr Met Asp Arg Leu Asp

210 215 220

Ala Thr Val Pro Gly Thr Arg Asp Val Asp Val Gln Ala Ala Lys Asp

225 230 235 240

Ala Phe Asp Lys Val Lys Gly Phe Tyr Thr Asn Ser Asp Ser Val Lys

245 250 255

Ala Ile Glu Arg Ala Phe Glu Asp Tyr Ala Thr Ala Ser Thr Ala Gly

260 265 270

Thr Ala Lys Ala Asp Ala Ala Thr Ala Ile Lys Ala Ala Phe Asp Leu

275 280 285

Ala Ala Asn Lys Val Gly Lys Pro Ala Thr Gly Gly Ala Gln Gly Ser

290 295 300

Ala Asn Ser Leu Gly Ala Ile Thr Lys Ile Asp Ala Ala Leu Lys Thr

305 310 315 320

Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

325 330 335

Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Met Ala Ala Ala

340 345 350

Ala Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

355 360 365

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

370 375 380

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390 395

<210>51

<211>455

<212>PRT/Protein

<213>Bacillus cereus

<400>51

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Glu Asn Thr Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Ser Ala Asp Thr Ala Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Thr Ser Ala Leu Leu Ile Asp Lys Leu Ser Ile

165 170 175

Ser Gly Ala Gly Ala Gly Thr Ala Leu Ala Gly Val Ala Thr Ala Asp

180 185 190

Ile Asn Ala Ala Gly Thr Lys Gln Ala Ala Leu Ser Gly Leu Thr Gly

195 200 205

Ser Lys Thr Thr Asp Glu Leu Asp Asp Ala Val Lys Glu Phe Lys Thr

210 215 220

Glu Phe Asp Lys Val Lys Ser Gly Leu Ser Ala Glu Asn Ala Asp Lys

225 230 235 240

Ile Thr Ala Ala Met Asp Lys Tyr Thr Asn Asn Lys Thr Leu Asp Asn

245 250 255

Ala Lys Ala Ile Gly Asp Leu Tyr Lys Thr Met Ala Pro Ala Asp Ser

260 265 270

Thr Val Val Gly Thr Ala Gly Thr Lys Gly Gln Ala Leu Ile Asp Leu

275 280 285

Asn Ala Thr Ala Thr Gly Asp Thr Ala Gln Lys Arg Gln Val Ala Val

290 295 300

Asp Ala Phe Lys Asp Asp Phe Asp Lys Ile Lys Gly Gly Leu Asn Ala

305 310 315 320

Gln Asp Ala Ala Lys Val Thr Ala Ala Leu Asp Lys Phe Asn Lys Ala

325 330 335

Asp Gly Ser Gly Asn Thr Leu Glu Asn Ala Gln Glu Ile Gly Lys Val

340 345 350

Phe Ala Glu Val Ala Ala Gly Ser Thr Lys Ser Asn Ala Ser Asp Ala

355 360 365

Ile Lys Ser Ile Asp Lys Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala

370 375 380

Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu

385 390 395 400

Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp

405 410 415

Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu

420 425 430

Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln

435 440 445

Met Val Ser Lys Leu Leu Gln

450 455

<210>52

<211>367

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>52

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn Val Ala Ala Arg

50 55 60

Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Ser Glu Thr Asn Thr Ser Lys Asn Gln Ala Ala Met Gln Lys

100 105 110

Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile Ala Asp Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Ser Thr Ile Asn

130 135 140

Ile Gln Thr Leu Asp Ser His Asp Lys Asn Lys Gln Ile Thr Ile Ser

145 150 155 160

Leu Asp Ser Ala Ser Leu Lys Asn Leu Asp Ile Thr Asp Leu Ala Ile

165 170 175

Gly Ser Asn Thr Val Asn Lys Asn Asp Leu Asp Thr Leu Asn Asn Ser

180 185 190

Met Lys Arg Leu Glu Thr Ala Ala Ala Asp Ala Ala Val Gln Ala Gln

195 200 205

Asp Val Thr Asp Ala Lys Asn Ala Phe Asn Lys Val Lys Ser Gly Tyr

210 215 220

Thr Pro Ala Glu Val Glu Lys Met Glu Asp Ala Phe Lys Ala Tyr Asp

225 230 235 240

Lys Val Val Ala Asp Pro Ala Lys Thr Asp Ala Leu Leu Lys Ala Ala

245 250 255

Ala Glu Lys Ile Asn Thr Glu Phe Lys Thr Leu Thr Ala Pro Thr Ala

260 265 270

Thr Ala Phe Asp Pro Ser Ser Ser Val Glu Lys Ile Asp Lys Ala Ile

275 280 285

Glu Thr Ile Ala Ser Ser Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Thr Asn Leu Lys Ser Gln Glu Asn Ser Met Ala

305 310 315 320

Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>53

<211>367

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>53

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn Val Ala Ala Arg

50 55 60

Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Ser Glu Thr Asn Thr Ser Lys Asn Gln Ala Ala Met Gln Lys

100 105 110

Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile Ala Asp Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Ser Thr Ile Asn

130 135 140

Ile Gln Thr Leu Asp Ser His Asp Lys Asn Lys Gln Ile Thr Ile Ser

145 150 155 160

Leu Asp Ser Ala Ser Leu Lys Asn Leu Asp Ile Thr Asp Leu Ala Ile

165 170 175

Gly Ser Asn Thr Val Asn Lys Asn Asp Leu Asp Thr Leu Asn Asn Ser

180 185 190

Met Lys Arg Leu Glu Thr Ala Ala Ala Asp Ala Ala Val Gln Ala Gln

195 200 205

Asp Val Thr Asp Ala Lys Asn Ala Phe Asn Lys Val Lys Ser Gly Tyr

210 215 220

Thr Pro Ala Glu Val Glu Lys Met Glu Asp Ala Phe Lys Ala Tyr Asp

225 230 235 240

Lys Val Val Ala Asp Pro Ala Lys Thr Asp Ala Leu Leu Lys Ala Ala

245 250 255

Ala Glu Lys Ile Asn Thr Glu Phe Lys Thr Leu Thr Ala Pro Thr Ala

260 265 270

Thr Ala Phe Asp Pro Ser Ser Ser Val Glu Lys Ile Asp Lys Ala Ile

275 280 285

Glu Thr Ile Ala Ser Ser Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

290 295 300

Leu Asp Phe Asn Val Thr Asn Leu Lys Ser Gln Glu Asn Ser Met Ala

305 310 315 320

Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

325 330 335

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

340 345 350

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360 365

<210>54

<211>381

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>54

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln

100 105 110

Lys Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp

130 135 140

Asn Lys Ser Ile Ala Ile Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys

145 150 155 160

Gln Ile Asn Ile Asp Leu Ala Asn Thr Ser Thr Ser Ser Leu Lys Ile

165 170 175

Asp Lys Leu Ser Ile Glu Gly Lys Gly Asn Gln Thr Ile Ala Ile Thr

180 185 190

Ala Ala Asp Ile Ala Lys Asp Thr Asn Ile Ala Ala Leu Thr Ser Ala

195 200 205

Gln Gly Lys Leu Ala Ala Leu Thr Gly Thr Pro Ala Pro Ala Ala Leu

210 215 220

Thr Thr Ala Val Asp Glu Phe Lys Ala Ala Phe Glu Lys Val Asp Lys

225 230 235 240

Asn Leu Met Ser Asp Thr Gln Ile Thr Gly Ile Glu Asn Ala Ile Lys

245 250 255

Ala Tyr Asp Gly Ala Thr Thr Lys Thr Leu Ala Leu Ala Gln Ala Val

260 265 270

Gly Thr Ala Tyr Thr Ala Pro Thr Pro Gly Asp Ile Thr Lys Glu Leu

275 280 285

Pro Asn Ala Ser Ser Ser Ile Lys Ser Ile Asp Ala Ala Leu Glu Thr

290 295 300

Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp

305 310 315 320

Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Met Ala Ser Ala

325 330 335

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

340 345 350

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

355 360 365

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

370 375 380

<210>55

<211>364

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>55

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ser Glu Asn Gln

100 105 110

Ala Ala Leu Asp Lys Glu Phe Gly Ala Leu Lys Glu Gln Ile Asn Tyr

115 120 125

Ile Ser Thr Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser

130 135 140

Asn Glu Thr Ile Ala Ile Gln Thr Leu Asp Asn Ala Asp Glu Gly Lys

145 150 155 160

Lys Ile Asp Ile Lys Leu Ala Asn Val Ser Thr Asp Ser Leu Lys Ile

165 170 175

Asp Lys Leu Thr Ile Gly Gly Ala Ala Gln Lys Thr Val Asp Ala Val

180 185 190

Ala Asp Lys Phe Asn Ala Leu Lys Thr Thr Thr Thr Thr Asp Lys Ala

195 200 205

Ala Ile Gln Thr Glu Val Asp Ala Val Met Lys Glu Phe Asp Lys Val

210 215 220

Lys Gly Ser Met Ser Ala Glu Asp Ala Lys Val Ile Thr Asp Lys Leu

225 230 235 240

Lys Asp Tyr Asn Asp Ala Ala Asp Thr Asp Thr Ala Lys Ala Thr Ala

245 250 255

Ala Lys Asp Leu Gly Ala Ala Phe Asp Lys Thr Lys Val Asn Ile Ala

260 265 270

Asn Pro Asn Ala Ala Val Ala Ala Ile Asp Ser Ala Leu Glu Asn Ile

275 280 285

Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe

290 295 300

Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala

305 310 315 320

Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr

325 330 335

Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala

340 345 350

Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

355 360

<210>56

<211>266

<212>PRT/Protein

<213>Bacillus cereus

<400>56

Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asn Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Leu Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ala Asn Val Thr Asn Ser Asn Lys Asn Arg Asn Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Ser Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly Tyr Thr Val Asn Val Thr Lys His Thr Pro Pro

145 150 155 160

Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ser Met Met Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>57

<211>460

<212>PRT/Protein

<213>Bacillus cereus

<400>57

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Thr Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Gly Ala Leu Asp Lys

100 105 110

Glu Phe Ala Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Ala Ile Ala

130 135 140

Ile Gln Thr Leu Asp Ser Asp Asp Lys Gly Lys Gln Ile Asp Ile Ser

145 150 155 160

Leu Ser Asp Thr Ser Thr Thr Ala Leu Lys Ile Asn Asn Leu Ser Ile

165 170 175

Ala Ala Asn Gly Leu Gly Ile Gly Ser Gly Lys Glu Leu Val Gly Val

180 185 190

Ala Asp Asn Thr Ile Ala Asn Ala Ser Ala Glu Ala Leu Lys Lys Leu

195 200 205

Asp Gly Thr Thr Gly Asp Thr Asp Val Lys Arg Ser Asn Ala Val Lys

210 215 220

Ala Phe Thr Asp Gln Tyr Lys Asp Leu Lys Val Ala Met Asn Ala Lys

225 230 235 240

Asp Val Glu Thr Ile Asp Ala Ala Ile Lys Lys Phe Glu Gly Ala Asn

245 250 255

Thr Leu Glu Asn Ala Gln Ala Ile Gly Ala Ala Phe Glu Gly Ala Ala

260 265 270

Lys Ala Thr Leu Thr Thr Asp Ile Asn Asn Ala Thr Leu Thr Ser Lys

275 280 285

Ala Leu Ser Asp Leu Asp Thr Asp Ser Thr Thr Glu Thr Arg Lys Ala

290 295 300

Ala Met Lys Asp Phe Val Ala Ala Phe Asp Lys Val Lys Gly Ser Met

305 310 315 320

Asn Ser Ser Asp Val Thr Lys Ile Ser Asp Ala Ile Asp Arg Phe Ser

325 330 335

Lys Thr Asp Asp Ser Gly Asn Thr Leu Glu Ala Ala Arg Ala Ile Gly

340 345 350

Asp Ala Phe Lys Ala Ala Thr Thr Asn Gly Lys Thr Ser Thr Ala Thr

355 360 365

Asp Ala Asn Ser Ala Ile Lys Ala Ile Asp Glu Ala Leu Glu Thr Ile

370 375 380

Ala Ser Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe

385 390 395 400

Asn Val Asn Asn Leu Lys Asn Gln Ala Ser Ser Met Ala Ser Ala Ala

405 410 415

Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr

420 425 430

Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala

435 440 445

Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

450 455 460

<210>58

<211>399

<212>PRT/Protein

<213>Bacillus cereus

<400>58

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Thr Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala Leu Asp Lys

100 105 110

Glu Phe Asn Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn Lys Ser Ile Ala

130 135 140

Val Gln Thr Leu Asp Asn Ala Asp Thr Ser Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ser Asn Thr Ser Thr Lys Ala Leu Glu Ile Asn Ser Leu Thr Ile

165 170 175

Ser Gly Thr Thr Pro Ile Ala Gly Lys Asn Glu Thr Ser Lys Ile Thr

180 185 190

Ala Glu Gln Met Thr Ala Ala Ser Asp Ala Leu Glu Lys Phe Lys Thr

195 200 205

Ala Gln Glu Gly Leu Ala Asn Leu Thr Glu Pro Thr Lys Gly Ser Asp

210 215 220

Gly Lys Pro Glu Ala Gly Thr Gly Ser Ser Asn Glu Asp Ile Val Lys

225 230 235 240

Ala Val Lys Ala Phe Lys Glu Ala Phe Lys Asn Ile Gln Pro Leu Met

245 250 255

Ser Asp Thr Asp Ile Thr Thr Val Gln Asn Lys Ile Asp Leu Phe Asp

260 265 270

Glu Asp Ala Pro Asp Leu Ser Ala Ala Lys Leu Ile Gly Thr Thr Phe

275 280 285

Glu Glu Ser Met Lys Pro Val Ala Asp Lys Glu Ile Thr Lys Ala Ala

290 295 300

Val Lys Pro Asn Ala Ser Asp Ala Ile Ala Ala Ile Asp Ala Ala Leu

305 310 315 320

Thr Lys Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

325 330 335

Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Met Ala

340 345 350

Ser Ala Ala Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser

355 360 365

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

370 375 380

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

385 390 395

<210>59

<211>266

<212>PRT/Protein

<213>Bacillus cereus

<400>59

Met Arg Ile Gly Thr Asn Val Leu Ser Leu Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Leu Ala Val Gln

85 90 95

Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile Asp Glu Thr Thr

115 120 125

Glu Phe Asn Asn Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val Asn Val Thr Lys His Ile Pro Pro

145 150 155 160

Phe Pro Thr Gln His Asp Ile Asn Ile Ser Thr Glu Gln Glu Ala Arg

165 170 175

Ala Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His

180 185 190

Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

195 200 205

Asn Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile

210 215 220

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

225 230 235 240

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Val

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>60

<211>269

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>60

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala His Glu Ser Gly Leu Ser Val Ala Ala Arg

50 55 60

Asn Thr Ser Asp Gly Ile Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Gln Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Thr Ala Asn Gly Thr Asn Lys Asp Thr Asp Ile Glu Ala Leu Gly Lys

100 105 110

Glu Phe Ala Ala Leu Lys Glu Gln Ile Thr Tyr Val Ser Asp Asn Thr

115 120 125

Lys Phe Asn Gly Arg Glu Leu Leu Lys Gly Gly Asp Asp Ile Asn Ile

130 135 140

Gln Thr Tyr Asp Gly Ser Asp Glu Ser Gln Gln Ile Lys Ile Lys Ile

145 150 155 160

Ser Glu Leu Asp Leu Ser Ser Leu Asp Thr Gly Glu Val Thr Asp Ser

165 170 175

Asp Thr Ala Arg Gly Thr Val Ser Thr Leu Asp Asp Ala Ile Thr Asn

180 185 190

Ile Ala Ser Lys Arg Ala Glu Leu Gly Ala Thr Leu Asn Arg Leu Asp

195 200 205

Tyr Asn Thr Gln Asn Val Asn Ser Glu Ala Ala Ser Met Ala Ala Ser

210 215 220

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

225 230 235 240

Thr Lys Phe Lys Ile Leu Ser Glu Ala Gly Ile Ser Met Leu Ser Gln

245 250 255

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

260 265

<210>61

<211>269

<212>PRT/Protein

<213>Bacillus cereus

<400>61

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala His Glu Ser Gly Leu Ser Val Ala Ala Arg

50 55 60

Asn Thr Ser Asp Gly Ile Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Gln Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Thr Ala Asn Gly Thr Asn Lys Asp Thr Asp Ile Glu Ala Leu Gly Lys

100 105 110

Glu Phe Ala Ala Leu Lys Glu Gln Ile Thr Tyr Val Ser Asp Asn Thr

115 120 125

Lys Phe Asn Gly Arg Glu Leu Leu Lys Gly Gly Asp Asp Ile Asn Ile

130 135 140

Gln Thr Tyr Asp Gly Ser Asp Glu Ser Gln Gln Ile Lys Ile Lys Ile

145 150 155 160

Ser Glu Leu Asp Leu Ser Ser Leu Asp Thr Gly Glu Val Thr Asp Ser

165 170 175

Asp Thr Ala Arg Gly Thr Val Ser Thr Leu Asp Asp Ala Ile Thr Asn

180 185 190

Ile Ala Ser Lys Arg Ala Glu Leu Gly Ala Thr Leu Asn Arg Leu Asp

195 200 205

Tyr Asn Thr Gln Asn Val Asn Ser Glu Ala Ala Ser Met Ala Ala Ser

210 215 220

Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

225 230 235 240

Thr Lys Phe Lys Ile Leu Ser Glu Ala Gly Ile Ser Met Leu Ser Gln

245 250 255

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

260 265

<210>62

<211>267

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>62

Met Arg Ile Gly Thr Asn Phe Leu Ser Met Asn Ala Arg Gln Ser Leu

1 5 10 15

Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu His Leu Ala Thr

20 25 30

Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala Asn Ile Ala Ile

35 40 45

Val Thr Arg Met His Ala Arg Ala Asn Gly Met Arg Val Ala Ile Arg

50 55 60

Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala Glu Ala Ala Leu

65 70 75 80

Gln Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Ile Gln

85 90 95

Ser Ala Asn Ser Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn Lys

100 105 110

Glu Phe Gln Ser Leu Thr Glu Gln Ile Ser Tyr Ile Gly Glu Thr Thr

115 120 125

Glu Phe Asn Asp Leu Ser Val Phe Asp Gly Gln Asn Arg Pro Val Thr

130 135 140

Leu Asp Asp Ile Gly His Thr Val His Ile Ser Lys Ser Ile Pro Pro

145 150 155 160

Pro Ser Pro Thr Gln His Asp Ile Lys Ile Ser Thr Glu Gln Glu Ala

165 170 175

Arg Ala Ala Ile Leu Lys Ile Glu Glu Ala Leu Gln Ser Val Ser Leu

180 185 190

His Arg Ala Asp Leu Gly Ala Met Ile Asn Arg Leu His Phe Asn Ile

195 200 205

Glu Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg

210 215 220

Ile Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe

225 230 235 240

Lys Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln

245 250 255

Ile Pro Gln Met Val Ser Lys Leu Leu Gln Ser

260 265

<210>63

<211>373

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>63

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala Leu Asp Lys

100 105 110

Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Ala Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Thr Lys Ala Leu Asn Ile Asp Thr Leu Ser Ile

165 170 175

Ala Gly Thr Thr Asp Lys Thr Ile Thr Ile Thr Ala Lys Asp Leu Thr

180 185 190

Asp Asn Lys Ala Thr Leu Asp Ala Leu Lys Thr Ala Lys Ala Asp Leu

195 200 205

Ala Lys Leu Asp Asp Lys Ser Asp Gln Ala Thr Ile Asp Lys Ala Val

210 215 220

Asp Ala Phe Lys Thr Ala Phe Asn Asn Val Asp Lys Asn Leu Leu Ser

225 230 235 240

Asp Lys Ala Ile Glu Gly Ile Thr Asp Lys Met Thr Ala Phe Asp Gly

245 250 255

Thr His Thr Ala Ala Ala Ala Ile Gly Thr Ala Tyr Thr Glu Pro Thr

260 265 270

Ala Gly Asp Ile Thr Lys Ser Ala Pro Asn Ala Ser Gly Ala Ile Lys

275 280 285

Ser Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr Leu

290 295 300

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

305 310 315 320

Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp

325 330 335

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

340 345 350

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

355 360 365

Ser Lys Leu Leu Gln

370

<210>64

<211>257

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>64

Met Arg Ile Asn His Asn Ile Thr Ala Leu Asn Thr Tyr Arg Gln Phe

1 5 10 15

Asn Asn Ala Asn Asn Ala Gln Ala Lys Ser Met Glu Lys Leu Ser Ser

20 25 30

Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Asp Gln Ala Ser Arg

50 55 60

Asn Ala Gln Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala Leu

65 70 75 80

Asn Glu Thr His Asp Ile Leu Gln Arg Met Arg Glu Leu Val Val Gln

85 90 95

Ala Gly Asn Gly Thr Asn Lys Thr Glu Asp Leu Asp Ala Ile Gln Asp

100 105 110

Glu Ile Gly Ser Leu Ile Glu Glu Ile Gly Gly Glu Thr Asp Ser Lys

115 120 125

Gly Ile Ser Asp Arg Ala Gln Phe Asn Gly Arg Asn Leu Leu Asp Gly

130 135 140

Ser Leu Asp Ile Thr Leu Gln Val Gly Ala Asn Ala Gly Gln Gln Val

145 150 155 160

Asn Leu Lys Ile Gly Asp Met Ser Ala Gly Ala Leu Gly Ala Asp Thr

165 170 175

Asp Ser Asp Gly Ala Ala Asp Ala Phe Val Asn Ser Ile Asn Val Lys

180 185 190

Asp Phe Ala Thr Thr Ser Phe Asp Gln Leu Ala Ile Ile Asp Gly

195 200 205

Ala Ile Asn Gln Val Ser Glu Gln Arg Ser Gly Leu Gly Ala Thr Gln

210 215 220

Asn Arg Leu Asp His Thr Ile Asn Asn Leu Ser Thr Ser Ser Glu Asn

225 230 235 240

Leu Thr Ala Ser Glu Ser Arg Ile Arg Asp Val Asp Tyr Ala Leu Ala

245 250 255

Ala

<210>65

<211>270

<212>PRT/Protein

<213>Bacillus manliponensis

<400>65

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Asp Lys Met Asn Thr Ser Met Asn Arg Leu Ser Ser

20 25 30

Gly Lys Gln Ile Asn Ser Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Lys Glu Gly Gly Leu Asn Val Gly Ala Lys

50 55 60

Asn Thr Gln Asp Gly Met Ser Ala Leu Arg Thr Met Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Thr Gln

85 90 95

Ser Ala Thr Gly Thr Asn Gln Gly Asn Asp Arg Glu Ser Leu Asp Leu

100 105 110

Glu Phe Gln Gln Leu Thr Glu Glu Ile Thr His Ile Ala Glu Lys Thr

115 120 125

Asn Phe Asn Gly Asn Ala Leu Leu Ser Gly Ser Gly Ser Ala Ile Asn

130 135 140

Val Gln Leu Ser Asp Ala Ala Glu Asp Lys Leu Thr Ile Ala Ala Ile

145 150 155 160

Asp Ala Thr Ala Ser Thr Leu Leu Lys Gly Ala Val Asp Val Lys Thr

165 170 175

Glu Asp Lys Ala Asp Ala Ala Ile Thr Lys Ile Asp Gln Ala Ile Gln

180 185 190

Asp Ile Ala Asp Asn Arg Ala Thr Tyr Gly Ser Gln Leu Asn Arg Leu

195 200 205

Asp His Asn Leu Asn Asn Val Asn Ser Gln Ala Thr Asn Met Ala Ala

210 215 220

Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

225 230 235 240

Met Thr Lys Phe Lys Ile Leu Ser Glu Ala Gly Val Ser Met Leu Ser

245 250 255

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

260 265 270

<210>66

<211>273

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>66

Met Arg Ile Gly Ser Trp Thr Ala Thr Gly Met Ser Ile Val Asn His

1 5 10 15

Met Asn Arg Asn Trp Asn Ala Ala Ser Lys Ser Met Leu Arg Leu Ser

20 25 30

Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala

35 40 45

Ile Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Thr Met Ala Ser

50 55 60

Lys Asn Ile Met Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala

65 70 75 80

Leu Asn Glu Thr His Ala Ile Val Gln Arg Met Arg Glu Leu Ala Val

85 90 95

Gln Ala Ala Thr Asp Thr Asn Thr Asp Asp Asp Arg Ala Lys Leu Asp

100 105 110

Leu Glu Phe Gln Glu Leu Lys Lys Glu Ile Asp Arg Ile Ser Thr Asp

115 120 125

Thr Glu Phe Asn Thr Arg Thr Leu Leu Asn Gly Asp Tyr Lys Asp Asn

130 135 140

Gly Leu Lys Ile Gln Val Gly Ala Asn Ser Gly Gln Ala Ile Glu Val

145 150 155 160

Lys Ile Gly Asp Ala Gly Leu Ala Gly Ile Gly Leu Ser Thr Glu Ser

165 170 175

Ile Ala Thr Arg Glu Gly Ala Asn Ala Ala Leu Gly Lys Leu Asp Glu

180 185 190

Ala Thr Lys Asn Val Ser Met Glu Arg Ser Arg Leu Gly Ala Tyr Gln

195 200 205

Asn Arg Leu Glu His Ala Tyr Asn Val Ala Glu Asn Thr Ala Ile Asn

210 215 220

Leu Gln Asp Ala Glu Ser Arg Ile Arg Asp Val Asp Ile Ala Lys Glu

225 230 235 240

Met Met Asn Met Val Lys Ser Gln Ile Leu Ala Gln Val Gly Gln Gln

245 250 255

Val Leu Ala Met His Met Gln Gln Ala Gln Gly Ile Leu Arg Leu Leu

260 265 270

gly

<210>67

<211>273

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>67

Met Lys Ile Gly Ser Trp Thr Ala Thr Gly Met Ser Ile Val Asn His

1 5 10 15

Met Asn Arg Asn Trp Asn Ala Ala Ser Lys Ser Met Leu Arg Leu Ser

20 25 30

Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala

35 40 45

Ile Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Thr Met Ala Ser

50 55 60

Lys Asn Ile Met Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala

65 70 75 80

Leu Asn Glu Thr His Ala Ile Val Gln Arg Met Arg Glu Leu Ala Val

85 90 95

Gln Ala Ala Thr Asp Thr Asn Thr Asp Asp Asp Arg Ala Lys Leu Asp

100 105 110

Leu Glu Phe Gln Glu Leu Lys Lys Glu Ile Asp Arg Ile Ser Thr Asp

115 120 125

Thr Ala Phe Asn Thr Arg Thr Leu Leu Asn Gly Asp Tyr Lys Asp Asn

130 135 140

Gly Leu Lys Ile Gln Val Gly Ala Asn Ser Gly Gln Ala Ile Glu Val

145 150 155 160

Lys Ile Gly Asp Ala Gly Leu Ala Gly Ile Gly Leu Ser Thr Glu Ser

165 170 175

Ile Ala Thr Arg Glu Gly Ala Asn Ala Ala Leu Gly Lys Leu Asp Glu

180 185 190

Ala Thr Lys Asn Val Ser Met Glu Arg Ser Arg Leu Gly Ala Tyr Gln

195 200 205

Asn Arg Leu Glu His Ala Tyr Asn Val Ala Glu Asn Thr Ala Ile Asn

210 215 220

Leu Gln Asp Ala Glu Ser Arg Ile Arg Asp Val Asp Ile Ala Lys Glu

225 230 235 240

Met Met His Met Val Lys Ser Gln Ile Leu Ala Gln Val Gly Gln Gln

245 250 255

Val Leu Ala Met His Ile Gln Gln Ala Gln Gly Ile Leu Arg Leu Leu

260 265 270

gly

<210>68

<211>418

<212>PRT/Protein

<213>Paenibacillus sp.

<400>68

Met Ile Ile Ser His Asn Leu Thr Ala Leu Asn Thr Met Asn Lys Leu

1 5 10 15

Lys Gln Lys Asp Leu Ala Val Ser Lys Ser Leu Gly Lys Leu Ser Ser

20 25 30

Gly Leu Arg Ile Asn Gly Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Asn Gln Ala Ser Arg

50 55 60

Asn Ile Gln Asp Gly Ile Ser Leu Ile Gln Val Ala Asp Gly Ala Met

65 70 75 80

Gln Glu Ile His Ser Met Leu Gln Arg Met Asn Glu Leu Ala Val Gln

85 90 95

Ala Ser Asn Gly Thr Tyr Ser Gly Ser Asp Arg Leu Asn Ile Gln Ser

100 105 110

Glu Val Glu Gln Leu Ile Glu Glu Ile Asp Glu Ile Ala Gly Asn Thr

115 120 125

Gly Phe Asn Gly Ile Lys Leu Leu Asn Gly Asn Asn Glu Lys Thr Glu

130 135 140

Lys Thr Glu Lys Thr Gly Ser Val Val Ser Val Asn Asn Pro Pro Asn

145 150 155 160

Asn Lys Leu Ile Thr Ile Ser Ser Pro Val Gly Thr Ser Val Ser Glu

165 170 175

Ile Leu Asn Asn Leu Leu Thr Val Phe Asn Glu Ala Lys Asn Gly Gln

180 185 190

Val Gly Asp Ser Asp Ser Lys Arg Val Ser Ser Lys Phe Thr Leu Ser

195 200 205

Ile Asn Asn Asp Glu Leu Ser Ile Val Cys Asp Thr Gly Asp Gly Phe

210 215 220

Leu Leu Ser Gly Gly Ser Pro Asn Leu Phe Tyr Gln Gly Tyr Ile Gly

225 230 235 240

Gly Ser Tyr Lys Tyr Lys Phe Thr Glu Phe Ile Asn Glu Asn Asp Phe

245 250 255

Ile Asn Ile Met Asp Ile Gly Gly Ala Asn Gly Gly Asp Thr Leu Lys

260 265 270

Phe Asn Phe Ser Ser Ile Ser Lys Glu Pro Glu Glu Gln Lys Glu Gln

275 280 285

Lys Gly Leu Thr Leu Gln Ile Gly Ala Asn Ser Gly Glu Thr Leu Asn

290 295 300

Ile Lys Leu Pro Asn Val Thr Thr Ser Ala Ile Gly Ile Ser Ser Ile

305 310 315 320

Asp Val Ser Thr Ile Pro Asn Ala Glu Ser Ser Leu Ser Ser Ile Ser

325 330 335

Ala Ala Ile Asp Lys Val Ser Ala Glu Arg Ala Arg Met Gly Ala Tyr

340 345 350

Gln Asn Arg Leu Glu His Ser Arg Asn Asn Val Val Thr Tyr Ala Glu

355 360 365

Asn Leu Thr Ala Ala Glu Ser Arg Ile Arg Asp Val Asp Met Ala Lys

370 375 380

Glu Met Met Glu Leu Met Lys Asn Gln Ile Phe Thr Gln Ala Gly Gln

385 390 395 400

Ala Met Leu Leu Gln Thr Asn Thr Gln Pro Gln Ala Ile Leu Gln Leu

405 410 415

Leu Lys

<210>69

<211>387

<212>PRT/Protein

<213>Bacillus anthracis

<400>69

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Lys Glu Asn Gln Asp Ala Leu Asp Lys

100 105 110

Glu Phe Gly Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu Asp Asn Ala Asp Thr Ala Lys Gln Ile Asn Ile Asn

145 150 155 160

Leu Ala Asp Ser Ser Thr Lys Ala Leu Asn Ile Asp Ser Leu Thr Ile

165 170 175

Ser Gly Ser Lys Asp Ala Thr Ile Thr Ile Thr Ala Glu Asp Ile Thr

180 185 190

Ala Ala Ser Ala Glu Ile Thr Ala Ala Lys Gly Ala Arg Thr Ala Leu

195 200 205

Ala Asn Leu Lys Asp Thr Pro Ala Asp Pro Thr Lys Asp Pro Ala Ala

210 215 220

Ser Thr Pro Ala Glu Ile Lys Ala Ala Val Asp Asp Phe Lys Gly Lys

225 230 235 240

Phe Glu Lys Ile Lys Gly Leu Met Asn Asp Thr Asp Val Lys Ala Val

245 250 255

Glu Glu Lys Ile Lys Glu Phe Glu Thr Thr Ser Thr Leu Ala Lys Ala

260 265 270

Gln Ala Ile Gly Thr Ala Phe Thr Thr Gly Met Glu Pro Lys Ala Gly

275 280 285

Asn Ile Thr Lys Asn Val Pro Ala Ala Ser Ser Ser Ile Lys Ala Ile

290 295 300

Asp Ser Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr Leu Gly Ala

305 310 315 320

Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser

325 330 335

Ser Ala Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala

340 345 350

Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly

355 360 365

Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys

370 375 380

Leu Leu Gln

385

<210>70

<211>300

<212>PRT/Protein

<213>Bacillus anthracis

<400>70

Met Gln Lys Ser Gln Tyr Lys Lys Met Gly Val Leu Lys Met Arg Ile

1 5 10 15

Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met Arg Gln Asn

20 25 30

Gln Asp Lys Met Asn Val Ser Met Asn Arg Leu Ser Ser Gly Lys Arg

35 40 45

Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile Ala Thr Arg

50 55 60

Met Arg Ala Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln Asn Thr Gln

65 70 75 80

Asp Gly Met Ser Leu Ile Arg Thr Ala Glu Ser Ala Met Asn Ser Val

85 90 95

Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser Ser Asn

100 105 110

Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys Glu Phe Ala

115 120 125

Glu Leu Gln Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr Glu Phe Asn

130 135 140

Asp Lys Asn Leu Leu Ala Gly Thr Gly Ala Val Thr Ile Gly Ser Thr

145 150 155 160

Ser Ile Ser Gly Ala Glu Ile Ser Ile Glu Thr Leu Asp Ser Ser Ala

165 170 175

Thr Asn Gln Gln Ile Thr Ile Lys Leu Ala Asn Thr Thr Thr Ala Glu Lys

180 185 190

Leu Gly Ile Asp Ala Thr Thr Ser Asn Ile Ser Ile Ser Gly Ala Ala

195 200 205

Ser Ala Leu Ala Ala Ile Ser Ala Leu Asn Thr Ala Leu Asn Thr Val

210 215 220

Ala Gly Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Arg

225 230 235 240

Asn Val Glu Asn Leu Asn Asn Gln Ala Thr Asn Met Ala Ser Ala Ala

245 250 255

Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr

260 265 270

Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala

275 280 285

Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

290 295 300

<210>71

<211>287

<212>PRT/Protein

<213>Bacillus anthracis

<400>71

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Asp Lys Met Asn Val Ser Met Asn Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Glu Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln

85 90 95

Ser Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys

100 105 110

Glu Phe Ala Glu Leu Gln Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Asn Leu Leu Ala Gly Thr Gly Ala Val Thr Ile

130 135 140

Gly Ser Thr Ser Ile Ser Gly Ala Glu Ile Ser Ile Glu Thr Leu Asp

145 150 155 160

Ser Ser Ala Thr Asn Gln Gln Ile Thr Ile Lys Leu Ala Asn Thr Thr

165 170 175

Ala Glu Lys Leu Gly Ile Asp Ala Thr Thr Ser Asn Ile Ser Ile Ser

180 185 190

Gly Ala Ala Ser Ala Leu Ala Ala Ile Ser Ala Leu Asn Thr Ala Leu

195 200 205

Asn Thr Val Ala Gly Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

210 215 220

Leu Asp Arg Asn Val Glu Asn Leu Asn Asn Gln Ala Thr Asn Met Ala

225 230 235 240

Ser Ala Ala Ser Gln Ile Lys Asp Ala Asp Lys Ala Lys Glu Met Ser

245 250 255

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

260 265 270

Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

275 280 285

<210>72

<211>282

<212>PRT/Protein

<213>Bacillus anthracis

<400>72

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Asp Lys Met Asn Val Ser Met Asn Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Glu Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln

85 90 95

Ser Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys

100 105 110

Glu Phe Ala Glu Leu Gln Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Asn Leu Leu Ala Gly Thr Gly Ala Val Thr Ile

130 135 140

Gly Ser Thr Ser Ile Ser Gly Ala Glu Ile Ser Ile Glu Thr Leu Asp

145 150 155 160

Ser Ser Ala Thr Asn Gln Gln Ile Thr Ile Lys Leu Ala Asn Thr Thr

165 170 175

Ala Glu Lys Leu Gly Ile Asp Ala Thr Thr Ser Asn Ile Ser Ile Ser

180 185 190

Gly Ala Ala Ser Ala Leu Ala Ala Ile Ser Ala Leu Asn Thr Ala Leu

195 200 205

Asn Thr Val Ala Gly Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg

210 215 220

Leu Asp Arg Asn Val Glu Asn Leu Asn Asn Gln Ala Thr Asn Met Ala

225 230 235 240

Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser

245 250 255

Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu

260 265 270

Ser Gln Ala Asn Gln Thr Pro Gln Met Val

275 280

<210>73

<211>265

<212>PRT/Protein

<213>Bacillus anthracis

<400>73

Met Asn Val Ser Met Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser

1 5 10 15

Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala

20 25 30

Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln Asn Thr Gln Asp Gly Met

35 40 45

Ser Leu Ile Arg Thr Ala Glu Ser Ala Met Asn Ser Val Ser Asn Ile

50 55 60

Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser Ser Asn Gly Thr Asn

65 70 75 80

Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys Glu Phe Ala Glu Leu Gln

85 90 95

Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr Glu Phe Asn Asp Lys Asn

100 105 110

Leu Leu Ala Gly Thr Gly Ala Val Thr Ile Gly Ser Thr Ser Ile Ser

115 120 125

Gly Ala Glu Ile Ser Ile Glu Thr Leu Asp Ser Ser Ala Thr Asn Gln

130 135 140

Gln Ile Thr Ile Lys Leu Ala Asn Thr Thr Ala Glu Lys Leu Gly Ile

145 150 155 160

Asp Ala Thr Thr Ser Asn Ile Ser Ile Ser Gly Ala Ala Ser Ala Leu

165 170 175

Ala Ala Ile Ser Ala Leu Asn Thr Ala Leu Asn Thr Val Ala Gly Asn

180 185 190

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Arg Asn Val Glu

195 200 205

Asn Leu Asn Asn Gln Ala Thr Asn Met Ala Ser Ala Ala Ser Gln Ile

210 215 220

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

225 230 235 240

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

245 250 255

Pro Gln Met Val Ser Lys Leu Leu Gln

260 265

<210>74

<211>257

<212>PRT/Protein

<213>Bacillus megaterium

<400>74

Met Arg Ile Asn His Asn Ile Thr Ala Leu Asn Thr Tyr Arg Gln Phe

1 5 10 15

Asn Asn Ala Asn Asn Ala Gln Ala Lys Ser Met Glu Lys Leu Ser Ser

20 25 30

Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Asp Gln Ala Ser Arg

50 55 60

Asn Ala Gln Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala Leu

65 70 75 80

Asn Glu Thr His Asp Ile Leu Gln Arg Met Arg Glu Leu Val Val Gln

85 90 95

Ala Gly Asn Gly Thr Asn Lys Thr Glu Asp Leu Asp Ala Ile Gln Asp

100 105 110

Glu Ile Gly Ser Leu Ile Glu Glu Ile Gly Gly Glu Ala Asp Ser Lys

115 120 125

Gly Ile Ser Asp Arg Ala Gln Phe Asn Gly Arg Asn Leu Leu Asp Gly

130 135 140

Ser Leu Asp Ile Thr Leu Gln Val Gly Ala Asn Ala Gly Gln Gln Val

145 150 155 160

Asn Leu Lys Ile Gly Asp Met Ser Ala Gly Ala Leu Gly Ala Asp Thr

165 170 175

Asn Ser Asp Gly Ala Ala Asp Ala Phe Val Asn Ser Ile Asn Val Lys

180 185 190

Asp Phe Thr Ala Thr Ser Phe Asp Gln Leu Ala Ile Ile Asp Gly

195 200 205

Ala Ile Asn Gln Val Ser Glu Gln Arg Ser Gly Leu Gly Ala Thr Gln

210 215 220

Asn Arg Leu Asp His Thr Ile Asn Asn Leu Ser Thr Ser Ser Glu Asn

225 230 235 240

Leu Thr Ala Ser Glu Ser Arg Ile Arg Asp Val Asp Tyr Ala Leu Ala

245 250 255

Ala

<210>75

<211>286

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>75

Met Arg Ile Asn His Asn Leu Pro Ala Leu Asn Ala Tyr Arg Asn Leu

1 5 10 15

Ala Gln Asn Gln Ile Gly Thr Ser Lys Ile Leu Glu Arg Leu Ser Ser

20 25 30

Gly Tyr Arg Ile Asn Arg Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Glu Gln Gly Gln Arg

50 55 60

Asn Thr Met Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala Leu

65 70 75 80

Gln Glu Ile His Glu Met Leu Gln Arg Met Arg Glu Leu Ala Val Gln

85 90 95

Ala Ala Asn Gly Thr Tyr Ser Asp Lys Asp Lys Lys Ala Ile Glu Asp

100 105 110

Glu Ile Asn Gln Leu Thr Ala Gln Ile Asp Gln Ile Ala Lys Thr Thr

115 120 125

Glu Phe Asn Gly Ile Gln Leu Ile Gly Asp Ser Asp Ser Thr Ser Leu

130 135 140

Gln Asp Val Lys Ile Gln Tyr Gly Pro Lys Lys Glu Asp Ser Leu Thr

145 150 155 160

Leu Glu Leu Thr Thr Gln Pro Glu Ala Asp Pro Pro Phe Ala Ala Gly

165 170 175

Cys Lys Ala Asp Lys Ala Ser Leu Lys Ile Asp Asn Val Asp Val Ile

180 185 190

Ser Asp Pro Glu Gly Ala Ile Glu Thr Phe Lys Ala Ala Ile Asp Gln

195 200 205

Val Ser Arg Ile Arg Ser Tyr Phe Gly Ala Ile Gln Asn Arg Leu Glu

210 215 220

His Val Val Asn Asn Leu Ser Asn Tyr Thr Glu Asn Leu Thr Gly Ala

225 230 235 240

Glu Ser Arg Ile Arg Asp Ala Asp Met Ala Lys Glu Met Thr Glu Phe

245 250 255

Thr Arg Phe Asn Ile Ile Asn Gln Ser Ala Thr Ala Met Leu Ala Gln

260 265 270

Ala Asn Gln Leu Pro Gln Gly Val Leu Gln Leu Leu Lys Gly

275 280 285

<210>76

<211>152

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>76

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Lys Ala Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Gly Arg Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala

100 105 110

Ser Leu Gln Lys Glu Phe Ala Gln Leu Thr Glu Gln Ile Asp Tyr Ile

115 120 125

Ala Lys Asn Thr Gln Phe Asn Asp Gln Gln Leu Leu Gly Thr Ala Asp

130 135 140

Lys Lys Ile Lys Ile Gln Thr Leu

145 150

<210>77

<211>84

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>77

Ile Asp Ala Ala Ile Thr Thr Val Ala Gly Gln Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Phe Glu Phe Asn Ala Asn Asn Leu Lys Ser Gln

20 25 30

Glu Thr Ser Met Ala Asp Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>78

<211>151

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>78

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Lys Ala Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Gly Arg Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala

100 105 110

Ser Leu Gln Lys Glu Phe Ala Gln Leu Thr Glu Gln Ile Asp Tyr Ile

115 120 125

Ala Lys Asn Thr Gln Phe Asn Asp Gln Gln Leu Leu Gly Thr Ala Asp

130 135 140

Lys Lys Ile Lys Ile Gln Thr

145 150

<210>79

<211>84

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>79

Ile Asp Ala Ala Ile Thr Thr Val Ala Gly Gln Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Phe Glu Phe Asn Ala Asn Asn Leu Lys Ser Gln

20 25 30

Glu Thr Ser Met Ala Asp Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>80

<211>152

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>80

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Lys Ala Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Gly Arg Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala

100 105 110

Ser Leu Gln Lys Glu Phe Ala Gln Leu Thr Glu Gln Ile Asp Tyr Ile

115 120 125

Ala Lys Asn Thr Gln Phe Asn Asp Gln Gln Leu Leu Gly Thr Ala Asp

130 135 140

Lys Lys Ile Lys Ile Gln Thr Leu

145 150

<210>81

<211>84

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>81

Ile Asp Ala Ala Ile Thr Thr Val Ala Gly Gln Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Phe Glu Phe Asn Ala Asn Asn Leu Lys Ser Gln

20 25 30

Glu Thr Ser Met Ala Asp Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>82

<211>152

<212>PRT/Protein

<213>Bacillus cereus

<400>82

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Lys Ala Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Gly Arg Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala

100 105 110

Ser Leu Gln Lys Glu Phe Ala Gln Leu Thr Glu Gln Ile Asp Tyr Ile

115 120 125

Ala Lys Asn Thr Gln Phe Asn Asp Gln Gln Leu Leu Gly Thr Ala Asp

130 135 140

Lys Lys Ile Lys Ile Gln Thr Leu

145 150

<210>83

<211>84

<212>PRT/Protein

<213>Bacillus cereus

<400>83

Ile Asp Ala Ala Ile Thr Thr Val Ala Gly Gln Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Phe Glu Phe Asn Ala Asn Asn Leu Lys Ser Gln

20 25 30

Glu Thr Ser Met Ala Asp Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>84

<211>151

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>84

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Lys Ala Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Ala Arg Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Thr Gly Thr Asn Thr Thr Lys Asn Gln Val

100 105 110

Ala Leu Asn Lys Glu Phe Ala Ala Leu Lys Glu Gln Ile Thr Tyr Ile

115 120 125

Ala Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Lys Ser Thr Gln

130 135 140

Glu Ile Lys Ile Gln Thr Leu

145 150

<210>85

<211>85

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>85

Gln Leu Asp Ala Ala Leu Thr Lys Val Ala Asp Asn Arg Ala Thr Leu

1 5 10 15

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

20 25 30

Gln Glu Asn Ser Met Ala Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp

35 40 45

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

50 55 60

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

65 70 75 80

Ser Lys Leu Leu Gln

85

<210>86

<211>154

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>86

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asp Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys

100 105 110

Ser Ala Leu Gln Lys Glu Phe Ala Gln Leu Gln Lys Gln Ile Thr Tyr

115 120 125

Ile Ala Glu Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Asn Glu Asp

130 135 140

Ser Glu Val Lys Ile Gln Thr Leu Asp Ser

145 150

<210>87

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>87

Ala Ile Ala Ala Ile Asp Ala Ala Leu Thr Lys Val Ala Asp Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>88

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>88

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>89

<211>62

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>89

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn

50 55 60

<210>90

<211>142

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>90

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Gln Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Glu Asn Lys Ala

100 105 110

Ala Met Glu Lys Glu Phe Gly Gln Leu Lys Asp Gln Ile Lys Tyr Ile

115 120 125

Thr Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Asp Ala

130 135 140

<210>91

<211>84

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>91

Ile Asp Ala Ala Leu Lys Thr Val Ala Asp Asn Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln

20 25 30

Ser Ala Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>92

<211>137

<212>PRT/Protein

<213>Bacillus cereus

<400>92

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

100 105 110

Val Ala Leu Gln Lys Glu Phe Gly Glu Leu Gln Lys Gln Ile Asp Tyr

115 120 125

Ile Ala Lys Asn Thr Gln Phe Asn Asp

130 135

<210>93

<211>73

<212>PRT/Protein

<213>Bacillus cereus

<400>93

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Gln Ser Ser Met Ala Ser Ala Ala Ser Gln Val

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>94

<211>137

<212>PRT/Protein

<213>Bacillus cereus

<400>94

Met Gly Val Leu Asn Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn

1 5 10 15

Ala Arg Gln Ser Phe Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Ile

20 25 30

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

35 40 45

Ala Asn Val Ala Ile Val Thr Arg Met His Ala Arg Thr Ser Gly Ile

50 55 60

His Val Ala Ile Arg Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr

65 70 75 80

Ala Glu Ala Ala Leu Gln Thr Val Thr Asn Ile Leu Gln Arg Met Arg

85 90 95

Asp Val Ala Val Gln Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg

100 105 110

Asp Ser Leu Asn Lys Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr

115 120 125

Ile Asp Glu Thr Thr Glu Phe Asn Asp

130 135

<210>95

<211>73

<212>PRT/Protein

<213>Bacillus cereus

<400>95

Arg Ala Asp Leu Gly Ala Met Ile Asn Gln Leu Gln Phe Asn Ile Glu

1 5 10 15

Asn Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile

20 25 30

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

35 40 45

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

50 55 60

Pro Gln Met Val Tyr Lys Leu Leu Gln

65 70

<210>96

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>96

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln Gln

100 105 110

Ala Leu Gln Lys Glu Phe Gly Gln Leu Lys Glu Gln Ile Ser Tyr Ile

115 120 125

Ala Asp Asn Thr Glu Phe Asn Asp Lys Thr Leu Leu

130 135 140

<210>97

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>97

Ala Val Asp Ser Ile Asp Ala Ala Leu Lys Thr Val Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ala Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>98

<211>128

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>98

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Ala Arg Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala

100 105 110

Ala Met Gln Lys Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile

115 120 125

<210>99

<211>70

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>99

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Thr Asn Leu Lys

1 5 10 15

Ser Gln Glu Asn Ser Met Ala Ala Ser Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>100

<211>128

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>100

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Ala Arg Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala

100 105 110

Ala Met Gln Lys Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile

115 120 125

<210>101

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>101

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Thr

1 5 10 15

Asn Leu Lys Ser Gln Glu Asn Ser Met Ala Ala Ser Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>102

<211>128

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>102

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Ala Arg Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala

100 105 110

Ala Met Gln Lys Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile

115 120 125

<210>103

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>103

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Thr

1 5 10 15

Asn Leu Lys Ser Gln Glu Asn Ser Met Ala Ala Ser Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>104

<211>140

<212>PRT/Protein

<213>Bacillus cereus

<400>104

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>105

<211>73

<212>PRT/Protein

<213>Bacillus cereus

<400>105

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>106

<211>136

<212>PRT/Protein

<213>Bacillus cereus

<400>106

Gly Phe Leu Asn Met Arg Ile Gly Thr Asn Val Leu Ser Met Asn Ala

1 5 10 15

Arg Gln Ser Leu Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu

20 25 30

His Leu Ala Thr Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro Ala

35 40 45

Asn Ile Ala Ile Val Thr Arg Met His Ala Arg Ala Ser Gly Met Arg

50 55 60

Leu Ala Ile Arg Asn Asn Glu Asp Thr Ile Ser Met Leu Arg Thr Ala

65 70 75 80

Glu Ala Ala Leu Gln Thr Leu Thr Asn Ile Leu Gln Arg Met Arg Asp

85 90 95

Leu Ala Val Gln Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp

100 105 110

Ser Leu Asn Lys Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr Ile

115 120 125

Gly Glu Thr Thr Glu Phe Asn Asp

130 135

<210>107

<211>73

<212>PRT/Protein

<213>Bacillus cereus

<400>107

Arg Ala Asp Leu Gly Ser Met Ile Asn Arg Leu Gln Phe Asn Ile Glu

1 5 10 15

Asn Leu Asn Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg Ile

20 25 30

Glu Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys

35 40 45

Leu Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>108

<211>153

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>108

Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Asn

50 55 60

Val Ala Ala Asp Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Ser Asn Lys Ser

100 105 110

Ala Leu Gln Lys Glu Phe Ala Glu Leu Gln Lys Gln Ile Thr Tyr Ile

115 120 125

Ala Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Lys Glu Asp Ser

130 135 140

Glu Val Lys Ile Gln Thr Leu Asp Ser

145 150

<210>109

<211>85

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>109

Ala Ile Asp Ala Ala Leu Thr Lys Val Ala Asp Asn Arg Ala Thr Leu

1 5 10 15

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

20 25 30

Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp

35 40 45

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

50 55 60

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

65 70 75 80

Ser Lys Leu Leu Gln

85

<210>110

<211>153

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>110

Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Asn

50 55 60

Val Ala Ala Asp Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Ser Asn Lys Ser

100 105 110

Ala Leu Gln Lys Glu Phe Ala Glu Leu Gln Lys Gln Ile Thr Tyr Ile

115 120 125

Ala Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Lys Glu Asp Ser

130 135 140

Glu Val Lys Ile Gln Thr Leu Asp Ser

145 150

<210>111

<211>86

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>111

Ala Ala Ile Asp Ala Ala Leu Thr Lys Val Ala Asp Asn Arg Ala Thr

1 5 10 15

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

20 25 30

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

35 40 45

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

50 55 60

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

65 70 75 80

Val Ser Lys Leu Leu Gln

85

<210>112

<211>140

<212>PRT/Protein

<213>Bacillus cereus

<400>112

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ala Glu Asn Lys Ala

100 105 110

Ala Met Gln Lys Glu Phe Gly Glu Leu Lys Asp Gln Ile Lys Tyr Ile

115 120 125

Ser Glu Asn Thr Gln Phe Asn Asp Gln His Leu Leu

130 135 140

<210>113

<211>78

<212>PRT/Protein

<213>Bacillus cereus

<400>113

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ala Ser Met Ala Ser

20 25 30

Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

35 40 45

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

50 55 60

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>114

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>114

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>115

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>115

Ala Ile Lys Ser Ile Asp Ala Ala Leu Asp Thr Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>116

<211>137

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>116

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln

100 105 110

Gln Ala Leu Gln Lys Glu Phe Gly Gln Leu Lys Glu Gln Ile Ser Tyr

115 120 125

Ile Ala Asp Asn Thr Glu Phe Asn Asp

130 135

<210>117

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>117

Ala Val Asp Ala Ile Asp Ala Ala Leu Lys Thr Val Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ala Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>118

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>118

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln

100 105 110

Gln Ala Leu Gln Lys Glu Phe Gly Gln Leu Lys Glu Gln Ile Ser Tyr

115 120 125

Ile Ala Asp Asn Thr Glu Phe Asn Asp Lys Thr Leu Leu

130 135 140

<210>119

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>119

Ala Val Asp Ala Ile Asp Ala Ala Leu Lys Thr Val Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ala Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>120

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>120

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

100 105 110

Ser Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

130 135 140

<210>121

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>121

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>122

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>122

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser

100 105 110

Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

130 135 140

<210>123

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>123

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>124

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>124

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser

100 105 110

Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

130 135 140

<210>125

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>125

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>126

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>126

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser

100 105 110

Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

130 135 140

<210>127

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>127

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>128

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>128

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser

100 105 110

Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

130 135 140

<210>129

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>129

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>130

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>130

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala

100 105 110

Ala Leu Asn Lys Glu Phe Asp Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Thr Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>131

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>131

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>132

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>132

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala

100 105 110

Ala Leu Asn Lys Glu Phe Asp Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Thr Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>133

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>133

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>134

<211>140

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>134

Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Ser

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Glu Asn Gln Gln

100 105 110

Ala Leu Asn Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>135

<211>73

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>135

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>136

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>136

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>137

<211>85

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>137

Ile Asp Ala Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln

20 25 30

Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln Ser

85

<210>138

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>138

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln

100 105 110

Lys Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>139

<211>70

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>139

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>140

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>140

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln

100 105 110

Lys Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>141

<211>70

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>141

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>142

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>142

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln

100 105 110

Lys Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>143

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>143

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ala Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>144

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>144

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Asp Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser

100 105 110

Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

130 135 140

<210>145

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>145

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>146

<211>173

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>146

Gly Phe Leu Asn Met Ala Arg Ile Thr Ile Asn Leu Glu Ile Asp Phe

1 5 10 15

Phe Ala Tyr Tyr Arg Phe Ser Ile Cys Arg Lys Val Asn Ile Lys Lys

20 25 30

Trp Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

35 40 45

Thr Gln Asp Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

50 55 60

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

65 70 75 80

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

85 90 95

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

100 105 110

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

115 120 125

Asp Ile Ser Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

130 135 140

Ser Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Asp Gln Ile Asp Tyr

145 150 155 160

Ile Ser Lys Asn Thr Glu Phe Asn Asp Gln Lys Leu Leu

165 170

<210>147

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>147

Ala Ile Ala Ser Ile Asp Ala Ala Leu Glu Ser Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>148

<211>157

<212>PRT/Protein

<213>Bacillus cereus

<400>148

Gly Val Leu Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Ser

50 55 60

Val Ala Ala Asp Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Val

100 105 110

Ala Leu Gln Lys Glu Phe Ala Ala Leu Lys Glu Gln Ile Thr Tyr Ile

115 120 125

Ala Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Asn Gly Asn Gln

130 135 140

Thr Ile Asn Ile Gln Thr Leu Asp Ser His Asp Ser Thr

145 150 155

<210>149

<211>78

<212>PRT/Protein

<213>Bacillus cereus

<400>149

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ala Met Ala Ala

20 25 30

Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

35 40 45

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

50 55 60

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>150

<211>157

<212>PRT/Protein

<213>Bacillus cereus

<400>150

Gly Val Leu Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Ser

50 55 60

Val Ala Ala Asp Asn Thr Gln Asn Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Val

100 105 110

Ala Leu Gln Lys Glu Phe Ala Ala Leu Lys Glu Gln Ile Thr Tyr Ile

115 120 125

Ala Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu Asn Gly Asn Gln

130 135 140

Thr Ile Asn Ile Gln Thr Leu Asp Ser His Asp Ser Thr

145 150 155

<210>151

<211>78

<212>PRT/Protein

<213>Bacillus cereus

<400>151

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ser Ser Ala Met Ala Ala

20 25 30

Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

35 40 45

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

50 55 60

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>152

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>152

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>153

<211>70

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>153

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>154

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>154

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Asn Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>155

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>155

Ala Ile Lys Ser Ile Asp Ala Ala Leu Asp Thr Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>156

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>156

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>157

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>157

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>158

<211>140

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>158

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>159

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>159

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>160

<211>153

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>160

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Gly Asn Gln Ala

100 105 110

Ala Leu Asn Lys Glu Phe Asp Ala Leu Lys Gln Gln Ile Asn Tyr Ile

115 120 125

Ser Thr Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu Asp Gly Ser Asn

130 135 140

Lys Thr Ile Ala Ile Gln Thr Leu Asp

145 150

<210>161

<211>70

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>161

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Ser Gln Gln Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>162

<211>136

<212>PRT/Protein

<213>Bacillus cereus

<400>162

Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ala Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Arg Asp Ile

85 90 95

Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala

100 105 110

Leu Gln Lys Glu Phe Gly Glu Leu Gln Lys Gln Ile Asp Tyr Ile Ala

115 120 125

Gly Asn Thr Gln Phe Asn Asp Lys

130 135

<210>163

<211>86

<212>PRT/Protein

<213>Bacillus cereus

<400>163

Asp Lys Ile Asp Glu Ala Leu Lys Thr Ile Ala Asp Asn Arg Ala Thr

1 5 10 15

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

20 25 30

Ser Gln Ser Ala Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

35 40 45

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

50 55 60

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

65 70 75 80

Val Ser Lys Leu Leu Gln

85

<210>164

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>164

Trp Gly Phe Leu Ile Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln

100 105 110

Ala Ala Leu Asn Lys Glu Phe Asp Ala Leu Lys Glu Gln Ile Asn Tyr

115 120 125

Ile Ser Thr Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>165

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>165

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn

1 5 10 15

Asn Leu Lys Ser Gln Gln Ser Ser Met Ala Ser Ala Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>166

<211>141

<212>PRT/Protein

<213>Bacillus cereus

<400>166

Trp Gly Phe Phe Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ser Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys

100 105 110

Ala Ala Met Gln Lys Glu Phe Gly Glu Leu Lys Glu Gln Ile Lys Tyr

115 120 125

Ile Ala Glu Asn Thr Gln Phe Asn Asp Gln His Leu Leu

130 135 140

<210>167

<211>78

<212>PRT/Protein

<213>Bacillus cereus

<400>167

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Met Ala Ala

20 25 30

Ala Ala Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

35 40 45

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

50 55 60

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>168

<211>141

<212>PRT/Protein

<213>Bacillus cereus

<400>168

Trp Gly Phe Phe Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ser Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys

100 105 110

Ala Ala Met Gln Lys Glu Phe Gly Glu Leu Lys Glu Gln Ile Lys Tyr

115 120 125

Ile Ala Glu Asn Thr Gln Phe Asn Asp Gln His Leu Leu

130 135 140

<210>169

<211>78

<212>PRT/Protein

<213>Bacillus cereus

<400>169

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Met Ala Ala

20 25 30

Ala Ala Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

35 40 45

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

50 55 60

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>170

<211>140

<212>PRT/Protein

<213>Bacillus cereus

<400>170

Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Leu Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ser Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Asn

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Gly Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Ala

100 105 110

Ala Met Gln Lys Glu Phe Ala Glu Leu Gln Lys Gln Ile Thr Tyr Ile

115 120 125

Ala Asp Asn Thr Gln Phe Asn Asp Lys Asn Leu Leu

130 135 140

<210>171

<211>84

<212>PRT/Protein

<213>Bacillus cereus

<400>171

Ile Asp Ala Ala Leu Lys Thr Val Ala Asp Asn Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln

20 25 30

Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>172

<211>141

<212>PRT/Protein

<213>Bacillus cereus

<400>172

Trp Gly Phe Phe Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ser Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys

100 105 110

Ala Ala Met Gln Lys Glu Phe Gly Glu Leu Lys Glu Gln Ile Lys Tyr

115 120 125

Ile Ala Glu Asn Thr Gln Phe Asn Asp Gln His Leu Leu

130 135 140

<210>173

<211>78

<212>PRT/Protein

<213>Bacillus cereus

<400>173

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Met Ala Ala

20 25 30

Ala Ala Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu

35 40 45

Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser

50 55 60

Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>174

<211>141

<212>PRT/Protein

<213>Bacillus cereus

<400>174

Trp Gly Phe Phe Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ser Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys

100 105 110

Ala Ala Met Gln Lys Glu Phe Gly Glu Leu Lys Glu Gln Ile Lys Tyr

115 120 125

Ile Ala Glu Asn Thr Gln Phe Asn Asp Gln His Leu Leu

130 135 140

<210>175

<211>77

<212>PRT/Protein

<213>Bacillus cereus

<400>175

Thr Val Ala Asp Asn Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu

1 5 10 15

Asp Phe Asn Val Asn Asn Leu Lys Ser Gln Ala Ser Ser Ala Ala Ala

20 25 30

Ala Ser Gln Val Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met

35 40 45

Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln

50 55 60

Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu Gln

65 70 75

<210>176

<211>140

<212>PRT/Protein

<213>Bacillus cereus

<400>176

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>177

<211>70

<212>PRT/Protein

<213>Bacillus cereus

<400>177

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>178

<211>128

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>178

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Ala Arg Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Ser Glu Thr Asn Thr Ser Lys Asn Gln Ala

100 105 110

Ala Met Gln Lys Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile

115 120 125

<210>179

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>179

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Thr

1 5 10 15

Asn Leu Lys Ser Gln Glu Asn Ser Met Ala Ala Ser Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>180

<211>128

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>180

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Thr Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ser Arg Glu Gly Gly Leu Asn

50 55 60

Val Ala Ala Arg Asn Thr Glu Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Leu Ala Asn Gln Ser Ala Ser Glu Thr Asn Thr Ser Lys Asn Gln Ala

100 105 110

Ala Met Gln Lys Glu Phe Asp Gln Leu Lys Glu Gln Ile Gln Tyr Ile

115 120 125

<210>181

<211>73

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>181

Arg Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Thr

1 5 10 15

Asn Leu Lys Ser Gln Glu Asn Ser Met Ala Ala Ser Ala Ser Gln Ile

20 25 30

Glu Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys

35 40 45

Ile Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr

50 55 60

Pro Gln Met Val Ser Lys Leu Leu Gln

65 70

<210>182

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>182

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Thr Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

100 105 110

Gly Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>183

<211>88

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>183

Ala Ile Lys Ala Ile Asp Glu Ala Leu Glu Thr Ile Ala Ser Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Asn Gln Ala Ser Ser Met Ala Ser Ala Ala Ser Gln Val Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>184

<211>141

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>184

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Ser Glu Asn Gln

100 105 110

Ala Ala Leu Asp Lys Glu Phe Gly Ala Leu Lys Glu Gln Ile Asn Tyr

115 120 125

Ile Ser Thr Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>185

<211>85

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>185

Ala Ile Asp Ser Ala Leu Glu Asn Ile Ala Ser Asn Arg Ala Thr Leu

1 5 10 15

Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser

20 25 30

Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp

35 40 45

Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu

50 55 60

Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

65 70 75 80

Ser Lys Leu Leu Gln

85

<210>186

<211>141

<212>PRT/Protein

<213>Bacillus cereus

<400>186

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Thr Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

100 105 110

Gly Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>187

<211>70

<212>PRT/Protein

<213>Bacillus cereus

<400>187

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Asn Gln Ala Ser Ser Met Ala Ser Ala Ala Ser Gln Val Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>188

<211>141

<212>PRT/Protein

<213>Bacillus cereus

<400>188

Met Gly Val Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Thr Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

100 105 110

Gly Ala Leu Asp Lys Glu Phe Ala Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu Leu

130 135 140

<210>189

<211>68

<212>PRT/Protein

<213>Bacillus cereus

<400>189

Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Asn Gln

1 5 10 15

Ala Ser Ser Met Ala Ser Ala Ala Ser Gln Val Glu Asp Ala Asp Met

20 25 30

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

35 40 45

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

50 55 60

Lys Leu Leu Gln

65

<210>190

<211>140

<212>PRT/Protein

<213>Bacillus cereus

<400>190

Trp Gly Phe Phe Tyr Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg

1 5 10 15

Thr Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Thr Ala Met

20 25 30

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

35 40 45

Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu

50 55 60

Gly Val Ala Ala Asn Asn Thr Gln Asp Gly Ile Ser Leu Ile Arg Thr

65 70 75 80

Ala Asp Ser Ala Met Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg

85 90 95

Asp Leu Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln

100 105 110

Ala Ala Leu Asp Lys Glu Phe Asn Ala Leu Lys Glu Gln Ile Asp Tyr

115 120 125

Ile Ser Lys Asn Thr Glu Phe Asn Asp Lys Lys Leu

130 135 140

<210>191

<211>88

<212>PRT/Protein

<213>Bacillus cereus

<400>191

Ala Ile Ala Ala Ile Asp Ala Ala Leu Thr Lys Val Ala Asp Asn Arg

1 5 10 15

Ala Thr Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn

20 25 30

Leu Lys Ser Gln Ala Ser Ser Met Ala Ser Ala Ala Ser Gln Val Glu

35 40 45

Asp Ala Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile

50 55 60

Leu Asn Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>192

<211>137

<212>PRT/Protein

<213>Bacillus cereus

<400>192

Trp Gly Phe Phe Tyr Met Arg Ile Gly Thr Asn Val Leu Ser Leu Asn

1 5 10 15

Ala Arg Gln Ser Leu Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met

20 25 30

Glu His Leu Ala Thr Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro

35 40 45

Ala Asn Ile Ala Ile Val Thr Arg Met His Ala Arg Ala Ser Gly Met

50 55 60

Arg Val Ala Ile Arg Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr

65 70 75 80

Ala Glu Ala Ala Leu Gln Thr Val Thr Asn Val Leu Gln Arg Met Arg

85 90 95

Asp Leu Ala Val Gln Ser Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg

100 105 110

Asp Ser Leu Asn Lys Glu Phe Gln Ser Leu Thr Glu Gln Ile Gly Tyr

115 120 125

Ile Asp Glu Thr Thr Glu Phe Asn Asn

130 135

<210>193

<211>88

<212>PRT/Protein

<213>Bacillus cereus

<400>193

Ala Ile Arg Lys Ile Glu Glu Ala Leu Gln Asn Val Ser Leu His Arg

1 5 10 15

Ala Asp Leu Gly Ala Met Ile Asn Arg Leu Gln Phe Asn Ile Glu Asn

20 25 30

Leu Asn Ser Gln Ser Thr Ala Leu Thr Asp Ala Ala Ser Arg Ile Glu

35 40 45

Asp Ala Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys Leu

50 55 60

Leu Thr Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Val Pro

65 70 75 80

Gln Met Val Ser Lys Leu Leu Gln

85

<210>194

<211>106

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>194

Leu Val Pro Phe Ala Val Trp Leu Ala Met Ser Arg Ile Arg Arg Arg

1 5 10 15

Ile Leu Asp Thr Asp Cys Lys Ala Glu Ser Ala Val Arg Ile Lys Glu

20 25 30

Ile Pro Ser Asp Val Leu Arg Ala Ala Thr Glu Arg Pro Leu Ser Cys

35 40 45

Ala Arg Ile Arg Val Ala Ile Ala Arg Pro Ala Ala Ser Ser Glu Ala

50 55 60

Leu Leu Ile Arg Leu Pro Leu Asp Lys Arg Ser Ile Ala Leu Leu Ile

65 70 75 80

Leu Ala Trp Phe Trp Arg Met Tyr Ser Cys Val Arg Met Leu Leu Met

85 90 95

Phe Val Leu Ile Leu Met Leu Arg Thr Pro

100 105

<210>195

<211>49

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>195

Met Ala Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu

1 5 10 15

Met Ser Glu Met Thr Lys Phe Lys Ile Leu Ser Glu Ala Gly Ile Ser

20 25 30

Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu

35 40 45

Gln

<210>196

<211>102

<212>PRT/Protein

<213>Bacillus cereus

<400>196

Ala Val Trp Leu Ala Met Ser Arg Ile Arg Arg Arg Ile Leu Asp Thr

1 5 10 15

Asp Cys Lys Ala Glu Ser Ala Val Arg Ile Lys Glu Ile Pro Ser Asp

20 25 30

Val Leu Arg Ala Ala Thr Glu Arg Pro Leu Ser Cys Ala Arg Ile Arg

35 40 45

Val Ala Ile Ala Arg Pro Ala Ala Ser Ser Glu Ala Leu Leu Ile Arg

50 55 60

Leu Pro Leu Asp Lys Arg Ser Ile Ala Leu Leu Ile Leu Ala Trp Phe

65 70 75 80

Trp Arg Met Tyr Ser Cys Val Arg Met Leu Leu Met Phe Val Leu Ile

85 90 95

Leu Met Leu Arg Thr Pro

100

<210>197

<211>50

<212>PRT/Protein

<213>Bacillus cereus

<400>197

Ser Met Ala Ala Ser Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys

1 5 10 15

Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Ser Glu Ala Gly Ile

20 25 30

Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu

35 40 45

Leu Gln

fifty

<210>198

<211>128

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>198

Gly Phe Leu Asn Met Arg Ile Gly Thr Asn Phe Leu Ser Met Asn Ala

1 5 10 15

Arg Gln Ser Leu Tyr Glu Asn Glu Lys Arg Met Asn Val Ala Met Glu

20 25 30

His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro Ala

35 40 45

Asn Ile Ala Ile Val Thr Arg Met His Ala Arg Ala Asn Gly Met Arg

50 55 60

Val Ala Ile Arg Asn Asn Glu Asp Ala Ile Ser Met Leu Arg Thr Ala

65 70 75 80

Glu Ala Ala Leu Gln Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp

85 90 95

Leu Ala Ile Gln Ser Ala Asn Ser Thr Asn Ser Asn Lys Asn Arg Asp

100 105 110

Ser Leu Asn Lys Glu Phe Gln Ser Leu Thr Glu Gln Ile Ser Tyr Ile

115 120 125

<210>199

<211>70

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>199

Leu Gly Ala Met Ile Asn Arg Leu His Phe Asn Ile Glu Asn Leu Asn

1 5 10 15

Ser Gln Ser Met Ala Leu Thr Asp Ala Ala Ser Arg Ile Glu Asp Ala

20 25 30

Asp Met Ala Gln Glu Met Ser Asp Phe Leu Lys Phe Lys Leu Leu Thr

35 40 45

Glu Val Ala Leu Ser Met Val Ser Gln Ala Asn Gln Ile Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>200

<211>128

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>200

Gly Phe Leu Asn Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr

1 5 10 15

Gln Glu Tyr Met Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp

20 25 30

Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala

35 40 45

Gly Leu Ala Ile Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly

50 55 60

Val Ala Ala Asn Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala

65 70 75 80

Asp Ser Ala Leu Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp

85 90 95

Ile Ala Asn Gln Ser Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys

100 105 110

Ala Leu Asp Lys Glu Phe Ser Ala Leu Lys Glu Gln Ile Asp Tyr Ile

115 120 125

<210>201

<211>70

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>201

Leu Gly Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys

1 5 10 15

Ser Gln Ser Ser Ser Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala

20 25 30

Asp Met Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn

35 40 45

Glu Ala Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met

50 55 60

Val Ser Lys Leu Leu Gln

65 70

<210>202

<211>154

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>202

Met Arg Ile Asn His Asn Ile Thr Ala Leu Asn Thr Tyr Arg Gln Phe

1 5 10 15

Asn Asn Ala Asn Asn Ala Gln Ala Lys Ser Met Glu Lys Leu Ser Ser

20 25 30

Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Asp Gln Ala Ser Arg

50 55 60

Asn Ala Gln Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala Leu

65 70 75 80

Asn Glu Thr His Asp Ile Leu Gln Arg Met Arg Glu Leu Val Val Gln

85 90 95

Ala Gly Asn Gly Thr Asn Lys Thr Glu Asp Leu Asp Ala Ile Gln Asp

100 105 110

Glu Ile Gly Ser Leu Ile Glu Glu Ile Gly Gly Glu Thr Asp Ser Lys

115 120 125

Gly Ile Ser Asp Arg Ala Gln Phe Asn Gly Arg Asn Leu Leu Asp Gly

130 135 140

Ser Leu Asp Ile Thr Leu Gln Val Gly Ala

145 150

<210>203

<211>52

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>203

Ile Asp Gly Ala Ile Asn Gln Val Ser Glu Gln Arg Ser Gly Leu Gly

1 5 10 15

Ala Thr Gln Asn Arg Leu Asp His Thr Ile Asn Asn Leu Ser Thr Ser

20 25 30

Ser Glu Asn Leu Thr Ala Ser Glu Ser Arg Ile Arg Asp Val Asp Tyr

35 40 45

Ala Leu Ala Ala

fifty

<210>204

<211>148

<212>PRT/Protein

<213>Bacillus manliponensis

<400>204

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Asp Lys Met Asn Thr Ser Met Asn Arg Leu Ser Ser

20 25 30

Gly Lys Gln Ile Asn Ser Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Lys Glu Gly Gly Leu Asn Val Gly Ala Lys

50 55 60

Asn Thr Gln Asp Gly Met Ser Ala Leu Arg Thr Met Asp Ser Ala Leu

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Thr Gln

85 90 95

Ser Ala Thr Gly Thr Asn Gln Gly Asn Asp Arg Glu Ser Leu Asp Leu

100 105 110

Glu Phe Gln Gln Leu Thr Glu Glu Ile Thr His Ile Ala Glu Lys Thr

115 120 125

Asn Phe Asn Gly Asn Ala Leu Leu Ser Gly Ser Gly Ser Ala Ile Asn

130 135 140

Val Gln Leu Ser

145

<210>205

<211>84

<212>PRT/Protein

<213>Bacillus manliponensis

<400>205

Ile Asp Gln Ala Ile Gln Asp Ile Ala Asp Asn Arg Ala Thr Tyr Gly

1 5 10 15

Ser Gln Leu Asn Arg Leu Asp His Asn Leu Asn Asn Val Asn Ser Gln

20 25 30

Ala Thr Asn Met Ala Ala Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Ser Glu Ala

50 55 60

Gly Val Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>206

<211>151

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>206

Met Arg Ile Gly Ser Trp Thr Ala Thr Gly Met Ser Ile Val Asn His

1 5 10 15

Met Asn Arg Asn Trp Asn Ala Ala Ser Lys Ser Met Leu Arg Leu Ser

20 25 30

Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala

35 40 45

Ile Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Thr Met Ala Ser

50 55 60

Lys Asn Ile Met Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala

65 70 75 80

Leu Asn Glu Thr His Ala Ile Val Gln Arg Met Arg Glu Leu Ala Val

85 90 95

Gln Ala Ala Thr Asp Thr Asn Thr Asp Asp Asp Arg Ala Lys Leu Asp

100 105 110

Leu Glu Phe Gln Glu Leu Lys Lys Glu Ile Asp Arg Ile Ser Thr Asp

115 120 125

Thr Glu Phe Asn Thr Arg Thr Leu Leu Asn Gly Asp Tyr Lys Asp Asn

130 135 140

Gly Leu Lys Ile Gln Val Gly

145 150

<210>207

<211>84

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>207

Leu Asp Glu Ala Thr Lys Asn Val Ser Met Glu Arg Ser Arg Leu Gly

1 5 10 15

Ala Tyr Gln Asn Arg Leu Glu His Ala Tyr Asn Val Ala Glu Asn Thr

20 25 30

Ala Ile Asn Leu Gln Asp Ala Glu Ser Arg Ile Arg Asp Val Asp Ile

35 40 45

Ala Lys Glu Met Met Asn Met Val Lys Ser Gln Ile Leu Ala Gln Val

50 55 60

Gly Gln Gln Val Leu Ala Met His Met Gln Gln Ala Gln Gly Ile Leu

65 70 75 80

Arg Leu Leu Gly

<210>208

<211>151

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>208

Met Lys Ile Gly Ser Trp Thr Ala Thr Gly Met Ser Ile Val Asn His

1 5 10 15

Met Asn Arg Asn Trp Asn Ala Ala Ser Lys Ser Met Leu Arg Leu Ser

20 25 30

Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala

35 40 45

Ile Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Thr Met Ala Ser

50 55 60

Lys Asn Ile Met Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala

65 70 75 80

Leu Asn Glu Thr His Ala Ile Val Gln Arg Met Arg Glu Leu Ala Val

85 90 95

Gln Ala Ala Thr Asp Thr Asn Thr Asp Asp Asp Arg Ala Lys Leu Asp

100 105 110

Leu Glu Phe Gln Glu Leu Lys Lys Glu Ile Asp Arg Ile Ser Thr Asp

115 120 125

Thr Ala Phe Asn Thr Arg Thr Leu Leu Asn Gly Asp Tyr Lys Asp Asn

130 135 140

Gly Leu Lys Ile Gln Val Gly

145 150

<210>209

<211>84

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>209

Leu Asp Glu Ala Thr Lys Asn Val Ser Met Glu Arg Ser Arg Leu Gly

1 5 10 15

Ala Tyr Gln Asn Arg Leu Glu His Ala Tyr Asn Val Ala Glu Asn Thr

20 25 30

Ala Ile Asn Leu Gln Asp Ala Glu Ser Arg Ile Arg Asp Val Asp Ile

35 40 45

Ala Lys Glu Met Met His Met Val Lys Ser Gln Ile Leu Ala Gln Val

50 55 60

Gly Gln Gln Val Leu Ala Met His Ile Gln Gln Ala Gln Gly Ile Leu

65 70 75 80

Arg Leu Leu Gly

<210>210

<211>148

<212>PRT/Protein

<213>Paenibacillus sp.

<400>210

Met Ile Ile Ser His Asn Leu Thr Ala Leu Asn Thr Met Asn Lys Leu

1 5 10 15

Lys Gln Lys Asp Leu Ala Val Ser Lys Ser Leu Gly Lys Leu Ser Ser

20 25 30

Gly Leu Arg Ile Asn Gly Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Asn Gln Ala Ser Arg

50 55 60

Asn Ile Gln Asp Gly Ile Ser Leu Ile Gln Val Ala Asp Gly Ala Met

65 70 75 80

Gln Glu Ile His Ser Met Leu Gln Arg Met Asn Glu Leu Ala Val Gln

85 90 95

Ala Ser Asn Gly Thr Tyr Ser Gly Ser Asp Arg Leu Asn Ile Gln Ser

100 105 110

Glu Val Glu Gln Leu Ile Glu Glu Ile Asp Glu Ile Ala Gly Asn Thr

115 120 125

Gly Phe Asn Gly Ile Lys Leu Leu Asn Gly Asn Asn Glu Lys Thr Glu

130 135 140

Lys Thr Glu Lys

145

<210>211

<211>84

<212>PRT/Protein

<213>Paenibacillus sp.

<400>211

Ile Ser Ala Ala Ile Asp Lys Val Ser Ala Glu Arg Ala Arg Met Gly

1 5 10 15

Ala Tyr Gln Asn Arg Leu Glu His Ser Arg Asn Asn Val Val Thr Tyr

20 25 30

Ala Glu Asn Leu Thr Ala Ala Glu Ser Arg Ile Arg Asp Val Asp Met

35 40 45

Ala Lys Glu Met Met Glu Leu Met Lys Asn Gln Ile Phe Thr Gln Ala

50 55 60

Gly Gln Ala Met Leu Leu Gln Thr Asn Thr Gln Pro Gln Ala Ile Leu

65 70 75 80

Gln Leu Leu Lys

<210>212

<211>148

<212>PRT/Protein

<213>Bacillus anthracis

<400>212

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Ala Lys Met Ser Asn Ala Met Asp Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Glu Ser Gly Leu Gly Val Ala Ala Asn

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Asp Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

85 90 95

Ser Ala Asn Gly Thr Asn Thr Lys Glu Asn Gln Asp Ala Leu Asp Lys

100 105 110

Glu Phe Gly Ala Leu Lys Glu Gln Ile Asp Tyr Ile Ser Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Lys Leu Leu Asn Gly Asp Asn Lys Ser Ile Ala

130 135 140

Ile Gln Thr Leu

145

<210>213

<211>84

<212>PRT/Protein

<213>Bacillus anthracis

<400>213

Ile Asp Ser Ala Leu Glu Thr Ile Ala Ser Asn Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Leu Asp Phe Asn Val Asn Asn Leu Lys Ser Gln

20 25 30

Ser Ser Ala Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>214

<211>172

<212>PRT/Protein

<213>Bacillus anthracis

<400>214

Met Gln Lys Ser Gln Tyr Lys Lys Met Gly Val Leu Lys Met Arg Ile

1 5 10 15

Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met Arg Gln Asn

20 25 30

Gln Asp Lys Met Asn Val Ser Met Asn Arg Leu Ser Ser Gly Lys Arg

35 40 45

Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile Ala Thr Arg

50 55 60

Met Arg Ala Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln Asn Thr Gln

65 70 75 80

Asp Gly Met Ser Leu Ile Arg Thr Ala Glu Ser Ala Met Asn Ser Val

85 90 95

Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser Ser Asn

100 105 110

Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys Glu Phe Ala

115 120 125

Glu Leu Gln Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr Glu Phe Asn

130 135 140

Asp Lys Asn Leu Leu Ala Gly Thr Gly Ala Val Thr Ile Gly Ser Thr

145 150 155 160

Ser Ile Ser Gly Ala Glu Ile Ser Ile Glu Thr Leu

165 170

<210>215

<211>81

<212>PRT/Protein

<213>Bacillus anthracis

<400>215

Ala Leu Asn Thr Val Ala Gly Asn Arg Ala Thr Leu Gly Ala Thr Leu

1 5 10 15

Asn Arg Leu Asp Arg Asn Val Glu Asn Leu Asn Asn Gln Ala Thr Asn

20 25 30

Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu

35 40 45

Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser

50 55 60

Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu

65 70 75 80

Gln

<210>216

<211>159

<212>PRT/Protein

<213>Bacillus anthracis

<400>216

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Asp Lys Met Asn Val Ser Met Asn Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Glu Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln

85 90 95

Ser Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys

100 105 110

Glu Phe Ala Glu Leu Gln Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Asn Leu Leu Ala Gly Thr Gly Ala Val Thr Ile

130 135 140

Gly Ser Thr Ser Ile Ser Gly Ala Glu Ile Ser Ile Glu Thr Leu

145 150 155

<210>217

<211>81

<212>PRT/Protein

<213>Bacillus anthracis

<400>217

Ala Leu Asn Thr Val Ala Gly Asn Arg Ala Thr Leu Gly Ala Thr Leu

1 5 10 15

Asn Arg Leu Asp Arg Asn Val Glu Asn Leu Asn Asn Gln Ala Thr Asn

20 25 30

Met Ala Ser Ala Ala Ser Gln Ile Lys Asp Ala Asp Lys Ala Lys Glu

35 40 45

Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser

50 55 60

Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser Lys Leu Leu

65 70 75 80

Gln

<210>218

<211>159

<212>PRT/Protein

<213>Bacillus anthracis

<400>218

Met Arg Ile Asn Thr Asn Ile Asn Ser Met Arg Thr Gln Glu Tyr Met

1 5 10 15

Arg Gln Asn Gln Asp Lys Met Asn Val Ser Met Asn Arg Leu Ser Ser

20 25 30

Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ala Thr Arg Met Arg Ala Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln

50 55 60

Asn Thr Gln Asp Gly Met Ser Leu Ile Arg Thr Ala Glu Ser Ala Met

65 70 75 80

Asn Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln

85 90 95

Ser Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys

100 105 110

Glu Phe Ala Glu Leu Gln Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr

115 120 125

Glu Phe Asn Asp Lys Asn Leu Leu Ala Gly Thr Gly Ala Val Thr Ile

130 135 140

Gly Ser Thr Ser Ile Ser Gly Ala Glu Ile Ser Ile Glu Thr Leu

145 150 155

<210>219

<211>76

<212>PRT/Protein

<213>Bacillus anthracis

<400>219

Ala Leu Asn Thr Val Ala Gly Asn Arg Ala Thr Leu Gly Ala Thr Leu

1 5 10 15

Asn Arg Leu Asp Arg Asn Val Glu Asn Leu Asn Asn Gln Ala Thr Asn

20 25 30

Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met Ala Lys Glu

35 40 45

Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala Gly Ile Ser

50 55 60

Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val

65 70 75

<210>220

<211>137

<212>PRT/Protein

<213>Bacillus anthracis

<400>220

Met Asn Val Ser Met Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser

1 5 10 15

Ala Ala Asp Asp Ala Ala Gly Leu Ala Ile Ala Thr Arg Met Arg Ala

20 25 30

Arg Gln Ser Gly Leu Glu Lys Ala Ser Gln Asn Thr Gln Asp Gly Met

35 40 45

Ser Leu Ile Arg Thr Ala Glu Ser Ala Met Asn Ser Val Ser Asn Ile

50 55 60

Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser Ser Asn Gly Thr Asn

65 70 75 80

Thr Ala Glu Asn Gln Ser Ala Leu Gln Lys Glu Phe Ala Glu Leu Gln

85 90 95

Glu Gln Ile Asp Tyr Ile Ala Lys Asn Thr Glu Phe Asn Asp Lys Asn

100 105 110

Leu Leu Ala Gly Thr Gly Ala Val Thr Ile Gly Ser Thr Ser Ile Ser

115 120 125

Gly Ala Glu Ile Ser Ile Glu Thr Leu

130 135

<210>221

<211>84

<212>PRT/Protein

<213>Bacillus anthracis

<400>221

Leu Asn Thr Ala Leu Asn Thr Val Ala Gly Asn Arg Ala Thr Leu Gly

1 5 10 15

Ala Thr Leu Asn Arg Leu Asp Arg Asn Val Glu Asn Leu Asn Asn Gln

20 25 30

Ala Thr Asn Met Ala Ser Ala Ala Ser Gln Ile Glu Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Ser Glu Met Thr Lys Phe Lys Ile Leu Asn Glu Ala

50 55 60

Gly Ile Ser Met Leu Ser Gln Ala Asn Gln Thr Pro Gln Met Val Ser

65 70 75 80

Lys Leu Leu Gln

<210>222

<211>154

<212>PRT/Protein

<213>Bacillus megaterium

<400>222

Met Arg Ile Asn His Asn Ile Thr Ala Leu Asn Thr Tyr Arg Gln Phe

1 5 10 15

Asn Asn Ala Asn Asn Ala Gln Ala Lys Ser Met Glu Lys Leu Ser Ser

20 25 30

Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Asp Gln Ala Ser Arg

50 55 60

Asn Ala Gln Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala Leu

65 70 75 80

Asn Glu Thr His Asp Ile Leu Gln Arg Met Arg Glu Leu Val Val Gln

85 90 95

Ala Gly Asn Gly Thr Asn Lys Thr Glu Asp Leu Asp Ala Ile Gln Asp

100 105 110

Glu Ile Gly Ser Leu Ile Glu Glu Ile Gly Gly Glu Ala Asp Ser Lys

115 120 125

Gly Ile Ser Asp Arg Ala Gln Phe Asn Gly Arg Asn Leu Leu Asp Gly

130 135 140

Ser Leu Asp Ile Thr Leu Gln Val Gly Ala

145 150

<210>223

<211>53

<212>PRT/Protein

<213>Bacillus megaterium

<400>223

Ile Ile Asp Gly Ala Ile Asn Gln Val Ser Glu Gln Arg Ser Gly Leu

1 5 10 15

Gly Ala Thr Gln Asn Arg Leu Asp His Thr Ile Asn Asn Leu Ser Thr

20 25 30

Ser Ser Glu Asn Leu Thr Ala Ser Glu Ser Arg Ile Arg Asp Val Asp

35 40 45

Tyr Ala Leu Ala Ala

fifty

<210>224

<211>148

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>224

Met Arg Ile Asn His Asn Leu Pro Ala Leu Asn Ala Tyr Arg Asn Leu

1 5 10 15

Ala Gln Asn Gln Ile Gly Thr Ser Lys Ile Leu Glu Arg Leu Ser Ser

20 25 30

Gly Tyr Arg Ile Asn Arg Ala Ser Asp Asp Ala Ala Gly Leu Ala Ile

35 40 45

Ser Glu Lys Met Arg Gly Gln Ile Arg Gly Leu Glu Gln Gly Gln Arg

50 55 60

Asn Thr Met Asp Gly Val Ser Leu Ile Gln Thr Ala Glu Gly Ala Leu

65 70 75 80

Gln Glu Ile His Glu Met Leu Gln Arg Met Arg Glu Leu Ala Val Gln

85 90 95

Ala Ala Asn Gly Thr Tyr Ser Asp Lys Asp Lys Lys Ala Ile Glu Asp

100 105 110

Glu Ile Asn Gln Leu Thr Ala Gln Ile Asp Gln Ile Ala Lys Thr Thr

115 120 125

Glu Phe Asn Gly Ile Gln Leu Ile Gly Asp Ser Asp Ser Thr Ser Leu

130 135 140

Gln Asp Val Lys

145

<210>225

<211>85

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>225

Phe Lys Ala Ala Ile Asp Gln Val Ser Arg Ile Arg Ser Tyr Phe Gly

1 5 10 15

Ala Ile Gln Asn Arg Leu Glu His Val Val Asn Asn Leu Ser Asn Tyr

20 25 30

Thr Glu Asn Leu Thr Gly Ala Glu Ser Arg Ile Arg Asp Ala Asp Met

35 40 45

Ala Lys Glu Met Thr Glu Phe Thr Arg Phe Asn Ile Ile Asn Gln Ser

50 55 60

Ala Thr Ala Met Leu Ala Gln Ala Asn Gln Leu Pro Gln Gly Val Leu

65 70 75 80

Gln Leu Leu Lys Gly

85

<210>226

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>226

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>227

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>227

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>228

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>228

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>229

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>229

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>230

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>230

Glu His Leu Ala Thr Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>231

<211>23

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>231

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala Thr

twenty

<210>232

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>232

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>233

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>233

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>234

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>234

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>235

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>235

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Val Ala Ile Val

twenty

<210>236

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>236

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>237

<211>22

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>237

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>238

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>238

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>239

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>239

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>240

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>240

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>241

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>241

Glu His Leu Ala Thr Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>242

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>242

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Val Ala Ile Val

twenty

<210>243

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>243

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>244

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>244

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>245

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>245

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>246

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>246

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>247

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>247

Glu His Phe Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Val Ala Ile Val

twenty

<210>248

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>248

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>249

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>249

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Val Ile Val

twenty

<210>250

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>250

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>251

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>251

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>252

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>252

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>253

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>253

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>254

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>254

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>255

<211>22

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>255

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>256

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>256

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>257

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>257

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Val Ala Ile Val

twenty

<210>258

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>258

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>259

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>259

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>260

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>260

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Val Ile Val

twenty

<210>261

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>261

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>262

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>262

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asn Asn Pro

1 5 10 15

Ala Asn Val Ala Ile Val

twenty

<210>263

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>263

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>264

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>264

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>265

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>265

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>266

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>266

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>267

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>267

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>268

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>268

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>269

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>269

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>270

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>270

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>271

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>271

Glu His Leu Ala Thr Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>272

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>272

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>273

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>273

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>274

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>274

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>275

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>275

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>276

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>276

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>277

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>277

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>278

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>278

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>279

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>279

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>280

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>280

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>281

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>281

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asn Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>282

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>282

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>283

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>283

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>284

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>284

Glu His Leu Ala Thr Gly Lys Lys Leu Asn Asn Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>285

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>285

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>286

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>286

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>287

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>287

Glu His Leu Ala Thr Gly Lys Lys Leu Asn His Ala Ser Asp Asn Pro

1 5 10 15

Ala Asn Ile Ala Ile Val

twenty

<210>288

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>288

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>289

<211>22

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>289

Glu Lys Leu Ser Ser Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>290

<211>22

<212>PRT/Protein

<213>Bacillus manliponensis

<400>290

Asn Arg Leu Ser Ser Gly Lys Gln Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>291

<211>22

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>291

Leu Arg Leu Ser Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>292

<211>22

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>292

Leu Arg Leu Ser Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>293

<211>22

<212>PRT/Protein

<213>Paenibacillus sp.

<400>293

Gly Lys Leu Ser Ser Gly Leu Arg Ile Asn Gly Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>294

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>294

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Asn Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>295

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>295

Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>296

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>296

Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>297

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>297

Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>298

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>298

Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>299

<211>22

<212>PRT/Protein

<213>Bacillus megaterium

<400>299

Glu Lys Leu Ser Ser Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>300

<211>22

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>300

Glu Arg Leu Ser Ser Gly Tyr Arg Ile Asn Arg Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>301

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>301

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala Ser

20 25

<210>302

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>302

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala Ser

20 25

<210>303

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>303

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala Ser

20 25

<210>304

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>304

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Lys Gly Asn Gln Ala Ser

20 25

<210>305

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>305

Thr Val Thr Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg His Ser

20 25

<210>306

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>306

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Ile Thr Asn Thr Asn Glu Asn Lys Ser Ala

20 25

<210>307

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>307

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys Ala

20 25

<210>308

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>308

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Glu Asn Lys Ala Ala

20 25

<210>309

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>309

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Val Ala

20 25

<210>310

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>310

Thr Val Thr Asn Ile Leu Gln Arg Met Arg Asp Val Ala Val Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>311

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>311

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln Gln Ala

20 25

<210>312

<211>28

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>312

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala

20 25

<210>313

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>313

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala

20 25

<210>314

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>314

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Ser Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala

20 25

<210>315

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>315

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>316

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>316

Thr Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser Ala Asn

1 5 10 15

Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser Leu Asn

20 25

<210>317

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>317

Thr Asn Val Leu Gln Arg Met Arg Asp Val Ala Val Gln Ser Ala Asn

1 5 10 15

Gly Thr Asn Leu Asn Lys Asn Arg Asp Ser Leu Asn

20 25

<210>318

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>318

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Ser Asn Lys Ser Ala

20 25

<210>319

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>319

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ala Glu Asn Lys Ala Ala

20 25

<210>320

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>320

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Lys Ala

20 25

<210>321

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>321

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln Gln Ala

20 25

<210>322

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>322

Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>323

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>323

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ala Asp Asn Gln Gln Ala

20 25

<210>324

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>324

Thr Val Thr Asn Ile Leu Gln His Met Arg Asp Phe Ala Ile Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Asn Thr Asn Arg Asp Ser

20 25

<210>325

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>325

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala

20 25

<210>326

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>326

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala

20 25

<210>327

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>327

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala

20 25

<210>328

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>328

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala Ala

20 25

<210>329

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>329

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala Ala

20 25

<210>330

<211>28

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>330

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ser Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Glu Asn Gln Gln Ala

20 25

<210>331

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>331

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>332

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>332

Thr Val Ala Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser

1 5 10 15

Ser Asn Asp Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>333

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>333

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys Ala

20 25

<210>334

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>334

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Asp Asn Gln Lys Ala

20 25

<210>335

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>335

Thr Val Thr Asn Ile Leu Gln His Met Arg Asp Phe Ala Ile Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Asn Thr Asn Arg Asp Ser

20 25

<210>336

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>336

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ser Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ser Ala

20 25

<210>337

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>337

Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Val Ala Val Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Ser Lys Asn Arg Asp Ser

20 25

<210>338

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>338

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Val Ala

20 25

<210>339

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>339

Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Ile Gln Ser

1 5 10 15

Ala Asn Ser Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>340

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>340

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Lys Ala

20 25

<210>341

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>341

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>342

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>342

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>343

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>343

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Gly Asn Gln Ala Ala

20 25

<210>344

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>344

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala

20 25

<210>345

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>345

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Glu Asn Gln Ala Ala

20 25

<210>346

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>346

Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser

1 5 10 15

Ala Asn Asp Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>347

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>347

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys Ala Ala

20 25

<210>348

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>348

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ser Asp Asn Gln Ala Ala

20 25

<210>349

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>349

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys Ala Ala

20 25

<210>350

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>350

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asn Glu Asn Lys Ala Ala

20 25

<210>351

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>351

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>352

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>352

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Ser Glu Thr Asn Thr Ser Lys Asn Gln Ala Ala

20 25

<210>353

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>353

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Ser Glu Thr Asn Thr Ser Lys Asn Gln Ala Ala

20 25

<210>354

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>354

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>355

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>355

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Ser Glu Asn Gln Ala Ala

20 25

<210>356

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>356

Thr Val Thr Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser

1 5 10 15

Ala Asn Val Thr Asn Ser Asn Lys Asn Arg Asn Ser

20 25

<210>357

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>357

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Gly Ala

20 25

<210>358

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>358

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Asp Lys Asn Gln Ala Ala

20 25

<210>359

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>359

Thr Val Thr Asn Val Leu Gln Arg Met Arg Asp Leu Ala Val Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>360

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>360

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Thr

1 5 10 15

Ala Asn Gly Thr Asn Lys Asp Thr Asp Ile Glu Ala

20 25

<210>361

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>361

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Thr

1 5 10 15

Ala Asn Gly Thr Asn Lys Asp Thr Asp Ile Glu Ala

20 25

<210>362

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>362

Thr Val Met Asn Ile Leu Gln Arg Met Arg Asp Leu Ala Ile Gln Ser

1 5 10 15

Ala Asn Ser Thr Asn Ser Asn Lys Asn Arg Asp Ser

20 25

<210>363

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>363

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Ile Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Gly Asp Asn Gln Lys Ala

20 25

<210>364

<211>28

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>364

Glu Thr His Asp Ile Leu Gln Arg Met Arg Glu Leu Val Val Gln Ala

1 5 10 15

Gly Asn Gly Thr Asn Lys Thr Glu Asp Leu Asp Ala

20 25

<210>365

<211>28

<212>PRT/Protein

<213>Bacillus manliponensis

<400>365

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Thr Gln Ser

1 5 10 15

Ala Thr Gly Thr Asn Gln Gly Asn Asp Arg Glu Ser

20 25

<210>366

<211>28

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>366

Glu Thr His Ala Ile Val Gln Arg Met Arg Glu Leu Ala Val Gln Ala

1 5 10 15

Ala Thr Asp Thr Asn Thr Asp Asp Asp Arg Ala Lys

20 25

<210>367

<211>28

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>367

Glu Thr His Ala Ile Val Gln Arg Met Arg Glu Leu Ala Val Gln Ala

1 5 10 15

Ala Thr Asp Thr Asn Thr Asp Asp Asp Arg Ala Lys

20 25

<210>368

<211>28

<212>PRT/Protein

<213>Paenibacillus sp.

<400>368

Glu Ile His Ser Met Leu Gln Arg Met Asn Glu Leu Ala Val Gln Ala

1 5 10 15

Ser Asn Gly Thr Tyr Ser Gly Ser Asp Arg Leu Asn

20 25

<210>369

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>369

Ser Val Ser Asn Ile Leu Leu Arg Met Arg Asp Leu Ala Asn Gln Ser

1 5 10 15

Ala Asn Gly Thr Asn Thr Lys Glu Asn Gln Asp Ala

20 25

<210>370

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>370

Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser

1 5 10 15

Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala

20 25

<210>371

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>371

Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser

1 5 10 15

Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala

20 25

<210>372

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>372

Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser

1 5 10 15

Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala

20 25

<210>373

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>373

Ser Val Ser Asn Ile Leu Thr Arg Met Arg Asp Ile Ala Val Gln Ser

1 5 10 15

Ser Asn Gly Thr Asn Thr Ala Glu Asn Gln Ser Ala

20 25

<210>374

<211>28

<212>PRT/Protein

<213>Bacillus megaterium

<400>374

Glu Thr His Asp Ile Leu Gln Arg Met Arg Glu Leu Val Val Gln Ala

1 5 10 15

Gly Asn Gly Thr Asn Lys Thr Glu Asp Leu Asp Ala

20 25

<210>375

<211>28

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>375

Glu Ile His Glu Met Leu Gln Arg Met Arg Glu Leu Ala Val Gln Ala

1 5 10 15

Ala Asn Gly Thr Tyr Ser Asp Lys Asp Lys Lys Ala

20 25

<210>376

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>376

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>377

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>377

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>378

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>378

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Ser Asn Ile Arg Lys Gly

1 5 10 15

Ser Ser Leu Arg Asp

twenty

<210>379

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>379

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>380

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>380

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala Asn Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Leu His Glu

twenty

<210>381

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>381

Thr Ala Ile Ala Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>382

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>382

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>383

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>383

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>384

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>384

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>385

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>385

Val Ile Ala Val Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>386

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>386

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>387

<211>22

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>387

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>388

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>388

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>389

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>389

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>390

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>390

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>391

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>391

Val Ile Ala Ile Asn Ala Pro Asn Asp Ala Ser Asn Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>392

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>392

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Leu His Glu

twenty

<210>393

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>393

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>394

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>394

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>395

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>395

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>396

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>396

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>397

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>397

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Phe His Glu

twenty

<210>398

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>398

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Arg Lys Gly

1 5 10 15

Ser Ser Leu Arg Asp

twenty

<210>399

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>399

Val Ile Val Ile Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>400

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>400

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>401

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>401

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>402

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>402

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>403

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>403

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>404

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>404

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>405

<211>22

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>405

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>406

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>406

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>407

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>407

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Leu His Glu

twenty

<210>408

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>408

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>409

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>409

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>410

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>410

Val Ile Val Ile Asn Ala Pro Asn Asp Ala Ser His Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>411

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>411

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>412

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>412

Val Ile Ala Val Ala Asn Pro Asn Asn Ser Ala His Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>413

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>413

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>414

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>414

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Leu His Glu

twenty

<210>415

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>415

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>416

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>416

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>417

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>417

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>418

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>418

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>419

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>419

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>420

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>420

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Ser Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>421

<211>21

<212>PRT/Protein

<213>Bacillus cereus

<400>421

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala Asn Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Leu His Glu

twenty

<210>422

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>422

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>423

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>423

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>424

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>424

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>425

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>425

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>426

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>426

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>427

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>427

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>428

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>428

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Asn Asn Ile Arg Lys Gly

1 5 10 15

Ser Ser Leu Arg Asp

twenty

<210>429

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>429

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>430

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>430

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>431

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>431

Val Ile Ala Ile Asn Ala Pro Asn Asn Ser Ala His Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>432

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>432

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>433

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>433

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>434

<211>22

<212>PRT/Protein

<213>Bacillus cereus

<400>434

Val Ile Ala Ile Asn Ala Pro Asn Asp Ser Ala Asn Asn Leu Lys Lys

1 5 10 15

Gly Thr Ala Leu His Glu

twenty

<210>435

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>435

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>436

<211>21

<212>PRT/Protein

<213>Bacillus cereus

<400>436

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Asn Asn Ile Arg Lys Gly

1 5 10 15

Ser Ser Leu Arg Asp

twenty

<210>437

<211>21

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>437

Val Ile Ala Asn Ala Pro Asn Asp Ser Ala His Asn Leu Lys Lys Gly

1 5 10 15

Thr Ala Leu His Glu

twenty

<210>438

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>438

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>439

<211>22

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>439

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Ser Asn Ile Arg Gln

1 5 10 15

Gly Ser Ser Leu Lys Glu

twenty

<210>440

<211>22

<212>PRT/Protein

<213>Bacillus manliponensis

<400>440

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Ser Asn Ile Gln Lys

1 5 10 15

Gly Ser Ser Leu Arg Asn

twenty

<210>441

<211>22

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>441

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Tyr

1 5 10 15

Gly Ser Ser Leu Arg Leu

twenty

<210>442

<211>22

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>442

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Tyr

1 5 10 15

Gly Ser Ser Leu Arg Leu

twenty

<210>443

<211>22

<212>PRT/Protein

<213>Paenibacillus sp.

<400>443

Ser Ile Ala Gly Leu Ala Ala Asp Asp Ser Ala Gly Asn Ile Arg Leu

1 5 10 15

Gly Ser Ser Leu Lys Gly

twenty

<210>444

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>444

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Asn Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asp

twenty

<210>445

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>445

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asn

twenty

<210>446

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>446

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asn

twenty

<210>447

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>447

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asn

twenty

<210>448

<211>22

<212>PRT/Protein

<213>Bacillus anthracis

<400>448

Ala Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asn

twenty

<210>449

<211>22

<212>PRT/Protein

<213>Bacillus megaterium

<400>449

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Ser Asn Ile Arg Gln

1 5 10 15

Gly Ser Ser Leu Lys Glu

twenty

<210>450

<211>22

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>450

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ser Ala Arg Asn Ile Arg Tyr

1 5 10 15

Gly Ser Ser Leu Arg Glu

twenty

<210>451

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>451

Ser Ala Gln Asn Gly Lys Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>452

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>452

Ser Ala Gln Asn Gly Lys Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>453

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>453

Ser Ala Gln Asn Gly Lys Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>454

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>454

Ser Ala Gln Asn Gly Lys Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>455

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>455

Ser His Arg Asn Lys Asn Ser Asn Thr Gly Asn Ala Ser Gln Val Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Ile Asn Thr Val Thr

20 25

<210>456

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>456

Ala Ser Lys Asn Glu Asn Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>457

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>457

Ala Lys Gln Asn Asp Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>458

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>458

Ala Ala Lys Asn Glu Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>459

<211>29

<212>PRT/Protein

<213>Bacillus cereus

<400>459

Leu Ala Val Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn

1 5 10 15

Ala Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>460

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>460

Ser Asp Arg Asn Lys Asn Ser Asn Thr Gly Asn Ala Ser Gln Val Ala

1 5 10 15

Val Asp Arg Met Arg Gln Leu Ile Asn Thr Val Thr

20 25

<210>461

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>461

Ala Gln Gln Asn Asp Ala Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>462

<211>28

<212>PRT/Protein

<213>Bacillus bombysepticus

<400>462

Ala Ala Gln Asn Lys Asp Thr Asn Thr Gly Ser Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>463

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>463

Ala Ala Gln Asn Lys Asp Thr Asn Thr Gly Ser Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>464

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>464

Ala Ala Gln Asn Lys Asp Thr Asn Thr Gly Ser Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>465

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>465

Ala Lys Gln Asn Asp Gly Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>466

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>466

Asn Leu Ser Asp Arg Asn Lys Asn Ser Asn Thr Gly Asn Ala Ser Gln

1 5 10 15

Val Ala Leu Asp Arg Met Arg Gln Leu Ile Asn Thr

20 25

<210>467

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>467

Asn Leu Ser Asp Arg Asn Lys Asn Leu Asn Thr Gly Asn Ala Ser Gln

1 5 10 15

Val Ala Val Asp Arg Met Arg Gln Leu Val Asn Thr

20 25

<210>468

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>468

Ala Ser Lys Asn Ser Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>469

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>469

Ala Ala Lys Asn Glu Ala Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>470

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>470

Ala Lys Gln Asn Asp Ser Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>471

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>471

Ala Gln Gln Asn Asp Ala Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>472

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>472

Ser Asp Arg Asn Lys Asn Ser Asn Thr Gly Asn Ala Ser Gln Val Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Ile Asn Met Val Thr

20 25

<210>473

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>473

Ala Gln Gln Asn Asp Ala Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>474

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>474

Ser Asp Arg Asn Thr Asn Ser Asn Thr Gly Asn Ala Ser Gln Ile Ala

1 5 10 15

Phe Asp Arg Met His Gln Leu Ile Asn Thr Val Thr

20 25

<210>475

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>475

Ala Ser Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ser

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>476

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>476

Ala Ser Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ser

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>477

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>477

Ala Ser Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ser

1 5 10 15

Ile Ser Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>478

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>478

Ala Ala Gln Asn Glu Asn Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>479

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>479

Ala Gln Gln Asn Glu Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ser

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>480

<211>28

<212>PRT/Protein

<213>Bacillus weihenstephanensis

<400>480

Ala Gln Gln Asn Glu Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ser

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>481

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>481

Ala Lys Gln Asn Asp Gly Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>482

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>482

Ser Asp Arg Asn Lys Asn Ser Asn Thr Asp Asn Ser Ser Gln Val Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Ile Asn Ala Val Thr

20 25

<210>483

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>483

Ala Lys Gln Asn Asp Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>484

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>484

Ala Lys Gln Asn Asp Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>485

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>485

Ser Asp Arg Asn Thr Asn Ser Asn Thr Gly Asn Ala Ser Gln Ile Ala

1 5 10 15

Phe Asp Arg Met His Gln Leu Ile Asn Thr Val Thr

20 25

<210>486

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>486

Ala Ser Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ser

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>487

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>487

Ser Asp Arg Asn Lys Ser Ser Asn Thr Gly Asn Ala Ser Gln Val Ala

1 5 10 15

Val Asp Arg Met Arg Gln Leu Val Asn Thr Val Thr

20 25

<210>488

<211>27

<212>PRT/Protein

<213>Bacillus cereus

<400>488

Ala Val Gln Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala Ile

1 5 10 15

Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>489

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>489

Ser Asp Arg Asn Lys Asn Ser Asn Thr Ser Asn Ala Ser Gln Ile Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Ile Asn Met Val Thr

20 25

<210>490

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>490

Ala Lys Gln Asn Asp Ser Thr Asn Ile Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>491

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>491

Ala Lys Gln Asn Asp Gly Thr Asn Thr Phe Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>492

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>492

Ala Lys Gln Asn Asp Gly Thr Asn Thr Phe Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>493

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>493

Ala Ala Gln Asn Gly Asn Thr Asn Thr Phe Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>494

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>494

Ala Ala Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>495

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>495

Ala Ala Gln Asn Glu Asn Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>496

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>496

Ser Asp Arg Asn Lys Asn Ser Asn Thr Asp Asn Ala Ser Gln Val Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Val Asn Thr Val Thr

20 25

<210>497

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>497

Ala Ala Lys Asn Glu Asn Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>498

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>498

Ala Ala Gln Asn Asp Ser Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>499

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>499

Ala Ala Lys Asn Glu Asn Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>500

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>500

Ala Ala Lys Asn Glu Asn Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>501

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>501

Ala Lys Gln Asn Asp Gly Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>502

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>502

Ala Ala Gln Asn Lys Ser Thr Asn Thr Glu Ser Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>503

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>503

Ala Ala Gln Asn Lys Ser Thr Asn Thr Glu Ser Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>504

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>504

Ala Lys Gln Asn Asp Gly Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>505

<211>27

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>505

Ala Ala Gln Asn Glu Ser Thr Asn Thr Gly Asn Ala Gln Asn Ala Leu

1 5 10 15

Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>506

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>506

Ser Asn Arg Asn Lys Asn Ser Asn Thr Val Asn Ala Ser Gln Val Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Ile Asn Thr Val Thr

20 25

<210>507

<211>27

<212>PRT/Protein

<213>Bacillus cereus

<400>507

Ala Gly Gln Asn Lys Asp Thr Asn Thr Asn Ala Ser Gln Asn Ala Leu

1 5 10 15

Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>508

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>508

Ala Ala Gln Asn Lys Asp Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>509

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>509

Ser Asp Arg Asn Lys Asn Ser Asn Thr Gly Asn Ala Ser Gln Val Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Val Asn Thr Val Thr

20 25

<210>510

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>510

Ala Glu Ile Asp Thr Asp Lys Asn Thr Gly Asn Ala Thr Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>511

<211>28

<212>PRT/Protein

<213>Bacillus cereus

<400>511

Ala Glu Ile Asp Thr Asp Lys Asn Thr Gly Asn Ala Thr Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>512

<211>27

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>512

Ser Asp Arg Asn Lys Asn Ser Asn Thr Ser Asn Ala Ser Gln Ile Ala

1 5 10 15

Leu Asp Arg Met Arg Gln Leu Ile Asn Met Thr

20 25

<210>513

<211>28

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>513

Ala Lys Gln Asn Asp Gly Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Ile Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>514

<211>28

<212>PRT/Protein

<213>Bacillus aryabhattai

<400>514

Ala Asp Leu Asp Glu Thr Lys Asn Thr Gly Asn Gly Ala Gln Val Val

1 5 10 15

Leu Glu Arg Met Arg Gln Leu Ile Asp His Thr Glu

20 25

<210>515

<211>27

<212>PRT/Protein

<213>Bacillus manliponensis

<400>515

Ser Glu Arg Asp Asn Gly Gln Asn Thr Gly Thr Ala Gln Thr Ala Leu

1 5 10 15

Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>516

<211>28

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>516

Lys Ala Arg Asp Asp Asp Thr Asn Thr Asp Thr Ala Ala Gln Val Ala

1 5 10 15

Leu Glu Arg Met Arg Gln Val Ile Ala His Thr Glu

20 25

<210>517

<211>28

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>517

Lys Ala Arg Asp Asp Asp Thr Asn Thr Asp Thr Ala Ala Gln Val Ala

1 5 10 15

Leu Glu Arg Met Arg Gln Val Ile Ala His Thr Glu

20 25

<210>518

<211>28

<212>PRT/Protein

<213>Paenibacillus sp.

<400>518

Asn Leu Arg Asp Ser Gly Ser Tyr Thr Gly Asn Ser Ala Gln Val Ala

1 5 10 15

Leu Glu Asn Met Arg Gln Leu Met Ser His Ile Glu

20 25

<210>519

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>519

Ala Asp Gln Asn Glu Lys Thr Asn Thr Gly Asn Ala Ser Gln Asn Ala

1 5 10 15

Leu Asp Arg Met Arg Leu Leu Ile Asn Ser Val Ser

20 25

<210>520

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>520

Ala Ser Gln Asn Glu Ala Thr Asn Thr Gly Asn Ser Ser Gln Val Ala

1 5 10 15

Ile Asp Arg Met Arg Thr Leu Ile Asn Ser Val Ser

20 25

<210>521

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>521

Ala Ser Gln Asn Glu Ala Thr Asn Thr Gly Asn Ser Ser Gln Val Ala

1 5 10 15

Ile Asp Arg Met Arg Thr Leu Ile Asn Ser Val Ser

20 25

<210>522

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>522

Ala Ser Gln Asn Glu Ala Thr Asn Thr Gly Asn Ser Ser Gln Val Ala

1 5 10 15

Ile Asp Arg Met Arg Thr Leu Ile Asn Ser Val Ser

20 25

<210>523

<211>28

<212>PRT/Protein

<213>Bacillus anthracis

<400>523

Ala Ser Gln Asn Glu Ala Thr Asn Thr Gly Asn Ser Ser Gln Val Ile

1 5 10 15

Ala Asp Arg Met Arg Thr Leu Ile Asn Ser Val Ser

20 25

<210>524

<211>28

<212>PRT/Protein

<213>Bacillus megaterium

<400>524

Ala Asp Leu Asp Glu Thr Lys Asn Thr Gly Asn Gly Ala Gln Val Val

1 5 10 15

Leu Glu Arg Met Arg Gln Leu Ile Asp His Thr Glu

20 25

<210>525

<211>27

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>525

Ala Lys Lys Asp Lys Ser Tyr Thr Gly Asn Ala Ala Gln Val Ala Leu

1 5 10 15

Glu Arg Met Arg Gln Leu Met Glu His Ile Glu

20 25

<210>526

<211>22

<212>PRT/Protein

<213>Escherichia coli

<400>526

Glu Arg Leu Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Gln Ala Ile Ala

twenty

<210>527

<211>22

<212>PRT/Protein

<213>Escherichia coli

<400>527

Ala Ile Ala Gln Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Arg Leu

1 5 10 15

Gly Ser Ser Leu Arg Glu

twenty

<210>528

<211>15

<212>PRT/Protein

<213>Escherichia coli

<400>528

Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Gln Ala Ile Ala

1 5 10 15

<210>529

<211>15

<212>PRT/Protein

<213>Escherichia coli

<400>529

Ala Ile Ala Gln Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Arg

1 5 10 15

<210>530

<211>22

<212>PRT/Protein

<213>Pseudomonas aeruginosa

<400>530

Gln Arg Leu Ser Thr Gly Ser Arg Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Leu Gln Ile Ala

twenty

<210>531

<211>22

<212>PRT/Protein

<213>Pseudomonas aeruginosa

<400>531

Ala Ile Gln Leu Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Arg Ser

1 5 10 15

Gly Thr Ser Leu Arg Gln

twenty

<210>532

<211>22

<212>PRT/Protein

<213>Xanthomonas spp.

<400>532

Gln Arg Leu Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>533

<211>22

<212>PRT/Protein

<213>Xanthomonas spp.

<400>533

Ser Ile Ala Leu Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Arg Leu

1 5 10 15

Gly Ser Ser Leu Arg Gln

twenty

<210>534

<211>22

<212>PRT/Protein

<213>Erwinia amylovora

<400>534

Gln Arg Leu Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Gln Ala Ile Ser

twenty

<210>535

<211>22

<212>PRT/Protein

<213>Erwinia amylovora

<400>535

Ser Ile Ala Gln Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Arg Leu

1 5 10 15

Gly Ser Ser Leu Arg Gln

twenty

<210>536

<211>22

<212>PRT/Protein

<213>Burkholderia phytofirmans

<400>536

Thr Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>537

<211>22

<212>PRT/Protein

<213>Burkholderia phytofirmans

<400>537

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Ser Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Thr

twenty

<210>538

<211>22

<212>PRT/Protein

<213>Burkholderia ubonensis

<400>538

Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Thr Ala Ala Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>539

<211>22

<212>PRT/Protein

<213>Burkholderia ubonensis

<400>539

Ser Ile Ala Leu Gly Ala Ala Asp Asp Ala Ala Thr Asn Ile Arg Lys

1 5 10 15

Gly Ser Ser Leu Arg Asn

twenty

<210>540

<211>22

<212>PRT/Protein

<213>Pseudomonas syringae

<400>540

Thr Arg Leu Ser Ser Gly Leu Lys Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Leu Gln Ile Ala

twenty

<210>541

<211>22

<212>PRT/Protein

<213>Pseudomonas syringae

<400>541

Ala Ile Gln Leu Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Lys Leu

1 5 10 15

Gly Ser Ser Leu Arg Thr

twenty

<210>542

<211>4

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>542

Gly Phe Leu Asn

one

<210>543

<211>5

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>543

Trp Gly Phe Leu Ile

fifteen

<210>544

<211>5

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>544

Met Gly Val Leu Asn

fifteen

<210>545

<211>4

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>545

Gly Val Leu Asn

one

<210>546

<211>5

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>546

Trp Gly Phe Phe Tyr

fifteen

<210>547

<211>9

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>547

Leu Val Pro Phe Ala Val Trp Leu Ala

fifteen

<210>548

<211>5

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>548

Ala Val Trp Leu Ala

fifteen

<210>549

<211>12

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>549

Leu Leu Gly Thr Ala Asp Lys Lys Ile Lys Ile Gln

1 5 10

<210>550

<211>11

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>550

Leu Leu Lys Ser Thr Gln Glu Ile Lys Ile Gln

1 5 10

<210>551

<211>11

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>551

Leu Leu Asn Glu Asp Ser Glu Val Lys Ile Gln

1 5 10

<210>552

<211>9

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>552

Leu Gly Val Ala Ala Asn Asn Thr Gln

fifteen

<210>553

<211>10

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>553

Leu Leu Arg Met Arg Asp Leu Ala Asn Gln

1 5 10

<210>554

<211>10

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>554

Leu Gln Arg Met Arg Asp Val Ala Val Gln

1 5 10

<210>555

<211>10

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>555

Leu Leu Arg Met Arg Asp Ile Ser Asn Gln

1 5 10

<210>556

<211>10

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>556

Leu Leu Arg Met Arg Asp Ile Ala Asn Gln

1 5 10

<210>557

<211>13

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>557

Leu Gln Lys Gln Ile Asp Tyr Ile Ala Gly Asn Thr Gln

1 5 10

<210>558

<211>8

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>558

Leu Leu Ile Arg Leu Pro Leu Asp

fifteen

<210>559

<211>9

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>559

Gln Arg Met Arg Glu Leu Ala Val Gln

fifteen

<210>560

<211>9

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>560

Thr Arg Met Arg Asp Ile Ala Val Gln

fifteen

<210>561

<211>9

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>561

Thr Arg Met Arg Asp Ile Ala Val Gln

fifteen

<210>562

<211>9

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>562

Gln Arg Met Arg Glu Leu Val Val Gln

fifteen

<210>563

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>563

Leu Gly Ala Thr Leu Asn

fifteen

<210>564

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>564

Leu Gly Ala Thr Gln Asn

fifteen

<210>565

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>565

Leu Ala Gln Ala Asn Gln

fifteen

<210>566

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>566

Leu Gly Ala Met Ile Asn

fifteen

<210>567

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>567

Leu Gly Ser Met Ile Asn

fifteen

<210>568

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>568

Met Gly Ala Tyr Gln Asn

fifteen

<210>569

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>569

Leu Gly Ala Tyr Gln Asn

fifteen

<210>570

<211>6

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>570

Tyr Gly Ser Gln Leu Asn

fifteen

<210>571

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>571

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>572

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>572

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Gln Ile Ala

twenty

<210>573

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>573

Gln Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>574

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>574

Asn Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>575

<211>22

<212>PRT/Protein

<213>Caballeronia megalochromosomata

<400>575

Thr Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>576

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>576

Asp Arg Leu Ser Ser Gly Tyr Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>577

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>577

Asp Arg Leu Ser Ser Gly Phe Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>578

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>578

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Asp Pro

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>579

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>579

Asp Arg Leu Ser Ser Gly Gln Arg Ile Asn Ser Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>580

<211>22

<212>PRT/Protein

<213>Lysinibacillus spp.

<400>580

Glu Lys Leu Ser Ser Gly Leu Arg Ile Asn Arg Ala Gly Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>581

<211>22

<212>PRT/Protein

<213>Lysinibacillus spp.

<400>581

Glu Lys Leu Ser Ser Gly Tyr Lys Ile Asn Arg Ala Ser Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>582

<211>22

<212>PRT/Protein

<213>Lysinibacillus spp.

<400>582

Leu Arg Ile Ser Ser Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Pro

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>583

<211>22

<212>PRT/Protein

<213>Lysinibacillus fusiformis

<400>583

Leu Arg Ile Ser Thr Gly Tyr Arg Ile Asn Ser Ala Ala Asp Asp Pro

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>584

<211>22

<212>PRT/Protein

<213>Lysinibacillus macroides

<400>584

Glu Lys Leu Ser Ser Gly Phe Arg Ile Asn Arg Ala Gly Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>585

<211>22

<212>PRT/Protein

<213>Lysinibacillus xylanilyticus

<400>585

Glu Lys Leu Ser Ser Gly Tyr Lys Ile Asn Arg Ala Gly Asp Asp Ala

1 5 10 15

Ala Gly Leu Ala Ile Ser

twenty

<210>586

<211>22

<212>PRT/Protein

<213>Escherichia coli

<400>586

Glu Arg Leu Ser Ser Gly Leu Arg Ile Asn Ser Ala Lys Asp Asp Ala

1 5 10 15

Ala Gly Gln Ala Ile Ala

twenty

<210>587

<211>23

<212>PRT/Protein

<213>Xanthomonas species

<400>587

Asn Gln Gly Ile Ser Glu Lys Gln Leu Asp Gln Leu Leu Thr Gln Leu

1 5 10 15

Ile Met Ala Leu Leu Gln Gln

twenty

<210>588

<211>23

<212>PRT/Protein

<213>Xanthomonas species

<400>588

Gln Gln Leu Leu Ala Met Ile Leu Gln Thr Leu Leu Gln Asp Leu Gln

1 5 10 15

Lys Glu Ser Ile Gly Gln Asn

twenty

<210>589

<211>12

<212>PRT/Protein

<213>Xanthomonas species

<400>589

Leu Asp Gln Leu Leu Thr Gln Leu Ile Met Ala Leu

1 5 10

<210>590

<211>12

<212>PRT/Protein

<213>Xanthomonas species

<400>590

Leu Ala Met Ile Leu Gln Thr Leu Leu Gln Asp Leu

1 5 10

<210>591

<211>19

<212>PRT/Protein

<213>Xanthomonas species

<400>591

Ser Glu Lys Gln Leu Asp Gln Leu Leu Thr Gln Leu Ile Met Ala Leu

1 5 10 15

Leu Gln Gln

<210>592

<211>19

<212>PRT/Protein

<213>Xanthomonas species

<400>592

Gln Gln Leu Leu Ala Met Ile Leu Gln Thr Leu Leu Gln Asp Leu Gln

1 5 10 15

Lys Glu Ser

<210>593

<211>143

<212>PRT/Protein

<213>Xanthamonas citri

<400>593

Met Met Asn Ser Leu Asn Thr Gln Leu Gly Ala Asn Ser Ser Phe Phe

1 5 10 15

Gln Val Asp Pro Ser Gln Asn Thr Gln Ser Gly Ser Asn Gln Gly Asn

20 25 30

Gln Gly Ile Ser Glu Lys Gln Leu Asp Gln Leu Leu Thr Gln Leu Ile

35 40 45

Met Ala Leu Leu Gln Gln Ser Asn Asn Ala Glu Gln Gly Gln Gly Gln

50 55 60

Gly Gln Gly Gly Asp Ser Gly Gly Gln Gly Gly Asn Arg Gln Gln Ala

65 70 75 80

Gly Gln Ser Asn Gly Ser Pro Ser Gln Tyr Thr Gln Met Leu Met Asn

85 90 95

Ile Val Gly Asp Ile Leu Gln Ala Gln Asn Gly Gly Gly Phe Gly Gly

100 105 110

Gly Phe Gly Gly Gly Phe Gly Gly Gly Gly Leu Gly Thr Ser Leu Gly

115 120 125

Thr Ser Leu Gly Thr Ser Leu Ala Ser Asp Thr Gly Ser Met Gln

130 135 140

<210>594

<211>19

<212>PRT/Protein

<213>Pantoea sesami

<400>594

Gln Leu Glu Gln Leu Met Thr Gln Leu Arg Ala Arg Leu Cys Arg Leu

1 5 10 15

Met Ala Met

<210>595

<211>19

<212>PRT/Protein

<213>Erwinia gerudensis

<400>595

Gln Leu Glu Gln Leu Met Thr Gln Leu Arg Ala Arg Leu Lys Arg Leu

1 5 10 15

Met Ala Met

<210>596

<211>19

<212>PRT/Protein

<213>Pantoea sesami

<400>596

Met Ala Met Leu Arg Cys Leu Arg Ala Arg Leu Gln Thr Met Leu Gln

1 5 10 15

Glu Leu Gln

<210>597

<211>19

<212>PRT/Protein

<213>Erwinia gerudensis

<400>597

Met Ala Met Leu Arg Lys Leu Arg Ala Arg Leu Gln Thr Met Leu Gln

1 5 10 15

Glu Leu Gln

<210>598

<211>5

<212>PRT/Protein

<213>Arabidopsis thaliana

<220>

<221>MISC_FEATURE/Other features

<222>(1)..(1)

<223>Xaa=sulfonated tyrosine

<220>

<221>MISC_FEATURE/Other features

<222>(3)..(3)

<223>Xaa=sulfonated tyrosine

<400>598

Xaa Ile Xaa Thr Gln

fifteen

<210>599

<211>5

<212>PRT/Protein

<213>Arabidopsis thaliana

<220>

<221>MISC_FEATURE/Other features

<222>(3)..(3)

<223>Xaa=sulfonated tyrosine

<220>

<221>MISC_FEATURE/Other features

<222>(5)..(5)

<223>Xaa=sulphonated tyrosine

<400>599

Gln Thr Xaa Ile Xaa

fifteen

<210>600

<211>12

<212>PRT/Protein

<213>Glycine max

<400>600

Gly Gly Ile Arg Ala Ala Pro Thr Gly Asn Glu Arg

1 5 10

<210>601

<211>12

<212>PRT/Protein

<213>Glycine max

<400>601

Arg Glu Asn Gly Thr Pro Ala Ala Arg Ile Gly Gly

1 5 10

<210>602

<211>217

<212>PRT/Protein

<213>Glycine max

<400>602

Met Lys Ser Thr Ile Phe Phe Ala Leu Phe Leu Phe Cys Ala Phe Thr

1 5 10 15

Thr Ser Tyr Leu Pro Ser Ala Ile Ala Asp Phe Val Leu Asp Asn Glu

20 25 30

Gly Asn Pro Leu Glu Asn Gly Gly Thr Tyr Tyr Ile Leu Ser Asp Ile

35 40 45

Thr Ala Phe Gly Gly Ile Arg Ala Ala Pro Thr Gly Asn Glu Arg Cys

50 55 60

Pro Leu Thr Val Val Gln Ser Arg Asn Glu Leu Asp Lys Gly Ile Glu

65 70 75 80

Thr Ile Ile Ser Ser Pro Tyr Arg Ile Arg Phe Ile Ala Glu Gly His

85 90 95

Pro Leu Ser Leu Lys Phe Asp Ser Phe Ala Val Ile Met Leu Cys Val

100 105 110

Gly Ile Pro Thr Glu Trp Ser Val Val Glu Asp Leu Pro Glu Gly Pro

115 120 125

Ala Val Lys Ile Gly Glu Asn Lys Asp Ala Met Asp Gly Trp Phe Arg

130 135 140

Leu Glu Arg Val Ser Asp Asp Glu Phe Asn Asn Tyr Lys Leu Val Phe

145 150 155 160

Cys Pro Gln Gln Ala Glu Asp Asp Lys Cys Gly Asp Ile Gly Ile Ser

165 170 175

Ile Asp His Asp Asp Gly Thr Arg Arg Leu Val Val Ser Lys Asn Lys

180 185 190

Pro Leu Val Val Gln Phe Gln Lys Leu Asp Lys Glu Ser Leu Ala Lys

195 200 205

Lys Asn His Gly Leu Ser Arg Ser Glu

210 215

<210>603

<211>12

<212>PRT/Protein

<213>Glycine max

<400>603

Gly Gly Ile Arg Ala Thr Pro Thr Glu Asn Glu Arg

1 5 10

<210>604

<211>12

<212>PRT/Protein

<213>Glycine max

<400>604

Gly Gly Ile Arg Val Ala Ala Thr Gly Lys Glu Arg

1 5 10

<210>605

<211>12

<212>PRT/Protein

<213>Glycine max

<400>605

Arg Glu Asn Glu Thr Pro Thr Ala Arg Ile Gly Gly

1 5 10

<210>606

<211>12

<212>PRT/Protein

<213>Glycine max

<400>606

Arg Glu Lys Gly Thr Ala Ala Val Arg Ile Gly Gly

1 5 10

<210>607

<211>18

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>607

Ala Arg Gly Lys Phe Glu Arg Lys Lys Pro His Val Asn Ile Gly Thr

1 5 10 15

Ile Gly

<210>608

<211>26

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>608

Ala Arg Gly Lys Phe Glu Arg Lys Lys Pro His Val Asn Ile Gly Thr

1 5 10 15

Ile Gly His Val Asp His Gly Lys Thr Thr

20 25

<210>609

<211>50

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>609

Glu Lys Pro Asn Val Lys Arg Gly Glu Asn Lys Trp Val Asp Lys Ile

1 5 10 15

Tyr Glu Leu Met Asp Ser Val Asp Ser Tyr Ile Pro Ile Pro Thr Arg

20 25 30

Gln Thr Glu Leu Pro Phe Leu Leu Ala Val Glu Asp Val Phe Ser Ile

35 40 45

Thr Gly

fifty

<210>610

<211>18

<212>PRT/Protein

<213>Euglena gracilis

<400>610

Ala Arg Gln Lys Phe Glu Arg Thr Lys Pro His Ile Asn Ile Gly Thr

1 5 10 15

Ile Gly

<210>611

<211>26

<212>PRT/Protein

<213>Euglena gracilis

<400>611

Ala Arg Gln Lys Phe Glu Arg Thr Lys Pro His Ile Asn Ile Gly Thr

1 5 10 15

Ile Gly His Val Asp His Gly Lys Thr Thr

20 25

<210>612

<211>50

<212>PRT/Protein

<213>Euglena gracilis

<400>612

Lys Asn Pro Lys Ile Thr Lys Gly Glu Asn Lys Trp Val Asp Lys Ile

1 5 10 15

Leu Asn Leu Met Asp Gln Val Asp Ser Tyr Ile Pro Thr Pro Thr Arg

20 25 30

Asp Thr Glu Lys Asp Phe Leu Met Ala Ile Glu Asp Val Leu Ser Ile

35 40 45

Thr Gly

fifty

<210>613

<211>18

<212>PRT/Protein

<213>Acidovorax avenae

<400>613

Ala Lys Gly Lys Phe Glu Arg Thr Lys Pro His Val Asn Val Gly Thr

1 5 10 15

Ile Gly

<210>614

<211>26

<212>PRT/Protein

<213>Acidovorax avenae

<400>614

Ala Lys Gly Lys Phe Glu Arg Thr Lys Pro His Val Asn Val Gly Thr

1 5 10 15

Ile Gly His Val Asp His Gly Lys Thr Thr

20 25

<210>615

<211>50

<212>PRT/Protein

<213>Acidovorax spp.

<400>615

Lys Leu Ala Leu Glu Gly Asp Lys Gly Pro Leu Gly Glu Gln Ala Ile

1 5 10 15

Asp Lys Leu Ala Glu Ala Leu Asp Thr Tyr Ile Pro Thr Pro Glu Arg

20 25 30

Ala Val Asp Gly Ala Phe Leu Met Pro Val Glu Asp Val Phe Ser Ile

35 40 45

Ser Gly

fifty

<210>616

<211>18

<212>PRT/Protein

<213>Bacillus cereus

<400>616

Ala Lys Ala Lys Phe Glu Arg Ser Lys Pro His Val Asn Ile Gly Thr

1 5 10 15

Ile Gly

<210>617

<211>26

<212>PRT/Protein

<213>Bacillus cereus

<400>617

Ala Lys Ala Lys Phe Glu Arg Ser Lys Pro His Val Asn Ile Gly Thr

1 5 10 15

Ile Gly His Val Asp His Gly Lys Thr Thr

20 25

<210>618

<211>50

<212>PRT/Protein

<213>Bacillus cereus

<400>618

Ser Ala Leu Lys Ala Leu Gln Gly Glu Ala Glu Trp Glu Glu Lys Ile

1 5 10 15

Ile Glu Leu Met Ala Glu Val Asp Ala Tyr Ile Pro Thr Pro Glu Arg

20 25 30

Glu Thr Asp Lys Pro Phe Leu Met Pro Ile Glu Asp Val Phe Ser Ile

35 40 45

Thr Gly

fifty

<210>619

<211>26

<212>PRT/Protein

<213>Burkholderia spp.

<400>619

Ala Lys Gly Lys Phe Glu Arg Thr Lys Pro His Val Asn Val Gly Thr

1 5 10 15

Ile Gly His Val Asp His Gly Lys Thr Thr

20 25

<210>620

<211>50

<212>PRT/Protein

<213>Burkholderia spp.

<400>620

Lys Leu Ala Leu Glu Gly Asp Thr Gly Glu Leu Gly Glu Val Ala Ile

1 5 10 15

Met Asn Leu Ala Asp Ala Leu Asp Thr Tyr Ile Pro Thr Pro Glu Arg

20 25 30

Ala Val Asp Gly Ala Phe Leu Met Pro Val Glu Asp Val Phe Ser Ile

35 40 45

Ser Gly

fifty

<210>621

<211>50

<212>PRT/Protein

<213>Xanthomonas campestris

<400>621

Arg Leu Ala Leu Asp Gly Asp Gln Ser Glu Ile Gly Val Pro Ala Ile

1 5 10 15

Leu Lys Leu Val Asp Ala Leu Asp Thr Phe Ile Pro Glu Pro Thr Arg

20 25 30

Asp Val Asp Arg Pro Phe Leu Met Pro Val Glu Asp Val Phe Ser Ile

35 40 45

Ser Gly

fifty

<210>622

<211>26

<212>PRT/Protein

<213>Pseudomonas spp.

<400>622

Ala Lys Glu Lys Phe Glu Arg Ser Lys Pro His Val Asn Val Gly Thr

1 5 10 15

Ile Gly His Val Asp His Gly Lys Thr Thr

20 25

<210>623

<211>50

<212>PRT/Protein

<213>Pseudomonas spp.

<400>623

Met Ala Leu Glu Gly Lys Asp Asp Asn Glu Met Gly Thr Thr Ala Val

1 5 10 15

Lys Lys Leu Val Glu Thr Leu Asp Ser Tyr Ile Pro Glu Pro Glu Arg

20 25 30

Ala Ile Asp Lys Pro Phe Leu Met Pro Ile Glu Asp Val Phe Ser Ile

35 40 45

SerGly

fifty

<210>624

<211>18

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>624

Gly Ile Thr Gly Ile Asn Val His Pro Lys Lys Arg Glu Phe Lys Gly

1 5 10 15

Arg Ala

<210>625

<211>26

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>625

Thr Thr Lys Gly His Asp Val His Gly Ile Thr Gly Ile Asn Val His

1 5 10 15

Pro Lys Lys Arg Glu Phe Lys Gly Arg Ala

20 25

<210>626

<211>50

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>626

Gly Thr Ile Ser Phe Val Asp Glu Val Ala Leu Leu Phe Pro Leu Glu

1 5 10 15

Thr Gln Arg Thr Pro Ile Pro Ile Tyr Ser Asp Val Ser Asp Met Leu

20 25 30

Glu Tyr Ile Lys Asp Val Trp Lys Asn Glu Gly Arg Lys Val Asn Pro

35 40 45

Lys Glu

fifty

<210>627

<211>18

<212>PRT/Protein

<213>Euglena gracilis

<400>627

Gly Ile Thr Gly Ile Asn Ile His Pro Lys Thr Arg Glu Phe Lys Gln

1 5 10 15

Arg Ala

<210>628

<211>26

<212>PRT/Protein

<213>Euglena gracilis

<400>628

Thr Thr Lys Gly His Asp Val His Gly Ile Thr Gly Ile Asn Ile His

1 5 10 15

Pro Lys Thr Arg Glu Phe Lys Gln Arg Ala

20 25

<210>629

<211>50

<212>PRT/Protein

<213>Euglena gracilis

<400>629

Gly Thr Ile Ser Leu Val Asp Glu Ile Ala Met Leu Phe Asp Lys Glu

1 5 10 15

Thr Asp Arg Thr Pro Thr Pro Ile Tyr Ser Asp Val Gln Asp Met Leu

20 25 30

Asn Leu Ile Lys Asp Val Trp Lys Asn Glu Gly Lys Thr Ile Lys Pro

35 40 45

Asn Lys

fifty

<210>630

<211>18

<212>PRT/Protein

<213>Acidovorax avenae

<400>630

Gly Ile Thr Gly Val Asn Val His Pro Lys Thr Arg Glu Phe Lys Gly

1 5 10 15

Lys Ala

<210>631

<211>26

<212>PRT/Protein

<213>Acidovorax avenae

<400>631

Thr Thr Lys Gly His Asp Val His Gly Ile Thr Gly Val Asn Val His

1 5 10 15

Pro Lys Thr Arg Glu Phe Lys Gly Lys Ala

20 25

<210>632

<211>50

<212>PRT/Protein

<213>Acidovorax spp.

<400>632

Gly Ser Ile Ser Phe Val Asp Glu Val Pro Met Leu Phe Ala Gly Asp

1 5 10 15

Val Ala Arg Glu Pro Thr Pro Ile Tyr Thr Asp Leu Ala Glu Ala Leu

20 25 30

Lys Asp Ile Ala Gln Glu Gly Leu Pro Gly Lys Asp Gly Glu Leu Ala

35 40 45

Leu Lys

fifty

<210>633

<211>18

<212>PRT/Protein

<213>Bacillus cereus

<400>633

Gly Ile Thr Gly Ile Asn Val His Pro Lys Ser Arg Glu Phe Lys Ala

1 5 10 15

Lys Ala

<210>634

<211>26

<212>PRT/Protein

<213>Bacillus cereus

<400>634

Thr Thr Lys Gly His Asp Val His Gly Ile Thr Gly Ile Asn Val His

1 5 10 15

Pro Lys Ser Arg Glu Phe Lys Ala Lys Ala

20 25

<210>635

<211>50

<212>PRT/Protein

<213>Bacillus cereus

<400>635

Gly Ile Thr Ser Phe Val Asp Glu Ile Pro Met Leu Phe Pro Lys Asp

1 5 10 15

Thr Glu Arg Glu Pro Thr Pro Ile Tyr Ala Asp Val Glu Ala Met Leu

20 25 30

Glu Ile Ile Lys Glu Glu Trp Glu Ala Glu Gly Gln Leu Ala Lys Leu

35 40 45

Ala Ser

fifty

<210>636

<211>26

<212>PRT/Protein

<213>Burkholderia spp.

<400>636

Thr Thr Lys Gly His Asp Val His Gly Ile Thr Gly Val Asn Val His

1 5 10 15

Pro Lys Thr Arg Glu Phe Lys Gly Lys Ala

20 25

<210>637

<211>50

<212>PRT/Protein

<213>Burkholderia spp.

<400>637

Gly Ser Ile Ser Phe Val Asp Glu Val Pro Met Leu Phe Ala Gly Asp

1 5 10 15

Val Ala Arg Glu Pro Thr Pro Ile Tyr Thr Asp Leu Ala Asp Ala Leu

20 25 30

Asn Met Ile Ala Val Glu Gly Leu Glu Gly Thr Asp Gly Glu Leu Ala

35 40 45

Leu Lys

fifty

<210>638

<211>50

<212>PRT/Protein

<213>Xanthomonas campestris

<400>638

Gly Ser Ile Ser Phe Val Asp Glu Val Pro Met Leu Phe Pro Arg Asp

1 5 10 15

Val Asp Arg Thr Pro Glu Pro Ile Phe Thr Asp Leu Ala Asp Val Leu

20 25 30

Lys Leu Ile Ala Pro Val Gly Ile Glu Ser Gln Asp Gly Asp Leu Ala

35 40 45

Leu Arg

fifty

<210>639

<211>26

<212>PRT/Protein

<213>Pseudomonas spp.

<400>639

Thr Thr Lys Gly His Asp Val His Gly Ile Thr Gly Val Asn Val His

1 5 10 15

Pro Lys Ser Arg Glu Phe Lys Glu Lys Ala

20 25

<210>640

<211>50

<212>PRT/Protein

<213>Pseudomonas spp.

<400>640

Gly Ser Ile Ser Phe Val Asp Glu Ile Pro Met Leu Phe Pro Lys Asp

1 5 10 15

Ile Ala Arg Glu Pro Glu Pro Ile Tyr Ser Asp Leu Thr Glu Val Leu

20 25 30

Lys Lys Val Ala Thr Thr Gly Met Glu Asn Asp Asp Lys Gly Glu Leu

35 40 45

Ala Met

fifty

<210>641

<211>54

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>641

Met Ser Thr Ala Thr Phe Val Asp Ile Ile Ile Ala Ile Leu Leu Pro

1 5 10 15

Pro Leu Gly Val Phe Leu Arg Phe Gly Cys Gly Val Glu Phe Trp Ile

20 25 30

Cys Leu Val Leu Thr Leu Leu Gly Tyr Ile Pro Gly Ile Ile Tyr Ala

35 40 45

Ile Tyr Val Leu Thr Lys

fifty

<210>642

<211>54

<212>PRT/Protein

<213>Citrus clementina

<400>642

Met Gly Ser Glu Thr Phe Leu Glu Val Ile Leu Ala Ile Leu Leu Pro

1 5 10 15

Pro Val Gly Val Phe Leu Arg Tyr Gly Cys Gly Val Glu Phe Trp Ile

20 25 30

Cys Leu Leu Leu Thr Val Leu Gly Tyr Ile Pro Gly Ile Ile Tyr Ala

35 40 45

Ile Tyr Val Leu Val Gly

fifty

<210>643

<211>54

<212>PRT/Protein

<213>Citrus trifoliata

<400>643

Met Gly Thr Ala Thr Cys Val Asp Ile Ile Leu Ala Val Ile Leu Pro

1 5 10 15

Pro Leu Gly Val Phe Leu Lys Phe Gly Cys Lys Ala Glu Phe Trp Ile

20 25 30

Cys Leu Leu Leu Thr Ile Leu Gly Tyr Ile Pro Gly Ile Ile Tyr Ala

35 40 45

Val Tyr Val Ile Thr Lys

fifty

<210>644

<211>58

<212>PRT/Protein

<213>Citrus sinensis

<400>644

Met Ala Asp Glu Gly Thr Ala Thr Cys Ile Asp Ile Ile Leu Ala Ile

1 5 10 15

Ile Leu Pro Pro Leu Gly Val Phe Leu Lys Phe Gly Cys Lys Val Glu

20 25 30

Phe Trp Ile Cys Leu Leu Leu Thr Ile Phe Gly Tyr Ile Pro Gly Ile

35 40 45

Ile Tyr Ala Val Tyr Ala Ile Thr Lys Asn

50 55

<210>645

<211>58

<212>PRT/Protein

<213>Citrus sinensis

<400>645

Met Ala Asp Gly Ser Thr Ala Thr Cys Val Asp Ile Leu Leu Ala Val

1 5 10 15

Ile Leu Pro Pro Leu Gly Val Phe Leu Lys Phe Gly Cys Lys Ala Glu

20 25 30

Phe Trp Ile Cys Leu Leu Leu Thr Ile Leu Gly Tyr Ile Pro Gly Ile

35 40 45

Ile Tyr Ala Val Tyr Ala Ile Thr Lys Lys

50 55

<210>646

<211>104

<212>PRT/Protein

<213>Citrus clementina

<400>646

Phe Tyr Lys Gln Lys Tyr Gln Val Gln Ile Thr Lys Ala Val Thr Gln

1 5 10 15

Asn Pro Lys His Phe Phe Asn Gln Ser Ser Cys Phe Leu Thr Leu Asn

20 25 30

Phe Ile Leu Phe His Phe Thr Leu Phe Lys Asn Gln Ser Lys Met Ala

35 40 45

Asp Gly Ser Thr Ala Thr Cys Val Asp Ile Leu Leu Ala Val Ile Leu

50 55 60

Pro Pro Leu Gly Val Phe Leu Lys Phe Gly Cys Lys Ala Glu Phe Trp

65 70 75 80

Ile Cys Leu Leu Leu Thr Ile Leu Gly Tyr Ile Pro Gly Ile Ile Tyr

85 90 95

Ala Val Tyr Ala Ile Thr Lys Lys

100

<210>647

<211>54

<212>PRT/Protein

<213>Arabidopsis thaliana

<400>647

Met Ser Thr Ala Thr Phe Val Asp Ile Ile Ile Ala Ile Leu Leu Pro

1 5 10 15

Pro Leu Gly Val Phe Leu Arg Phe Gly Cys Gly Val Glu Phe Trp Ile

20 25 30

Cys Leu Val Leu Thr Leu Leu Gly Tyr Ile Pro Gly Ile Ile Tyr Ala

35 40 45

Ile Tyr Val Leu Thr Lys

fifty

<210>648

<211>54

<212>PRT/Protein

<213>Camelina sativa

<400>648

Met Ser Thr Ala Thr Phe Val Asp Ile Ile Ile Ala Val Leu Leu Pro

1 5 10 15

Pro Leu Gly Val Phe Leu Arg Phe Gly Cys Gly Val Glu Phe Trp Ile

20 25 30

Cys Leu Val Leu Thr Leu Leu Gly Tyr Ile Pro Gly Ile Ile Tyr Ala

35 40 45

Ile Tyr Val Leu Thr Lys

fifty

<210>649

<211>54

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>649

Met Gly Thr Ala Thr Cys Val Asp Ile Ile Ile Ala Ile Leu Leu Pro

1 5 10 15

Pro Leu Gly Val Phe Leu Arg Phe Gly Cys Gly Val Glu Phe Trp Ile

20 25 30

Cys Leu Val Leu Thr Leu Leu Gly Tyr Ile Pro Gly Ile Leu Tyr Ala

35 40 45

Leu Tyr Val Leu Thr Lys

fifty

<210>650

<211>52

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>650

Arg Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg

1 5 10 15

Asp Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly

20 25 30

Asp Cys Arg Gly Phe Arg Arg Arg Cys Arg Cys Thr Arg Pro Cys Val

35 40 45

Phe Asp Glu Lys

fifty

<210>651

<211>47

<212>PRT/Protein

<213>Citrus sinensis

<400>651

Arg Val Cys Gln Ser Gln Ser His His Phe His Gly Ala Cys Phe Ser

1 5 10 15

His His Asn Cys Ala Phe Val Cys Arg Asn Glu Gly Phe Ser Gly Gly

20 25 30

Lys Cys Arg Gly Val Arg Arg Arg Cys Phe Cys Ser Lys Leu Cys

35 40 45

<210>652

<211>46

<212>PRT/Protein

<213>Avena sativa

<400>652

Lys Ser Cys Cys Lys Asp Ile Met Ala Arg Asn Cys Tyr Asn Val Cys

1 5 10 15

Arg Ile Pro Gly Thr Pro Arg Pro Val Cys Ala Thr Thr Cys Arg Cys

20 25 30

Lys Ile Ile Ser Gly Asn Lys Cys Pro Lys Asp Tyr Pro Lys

35 40 45

<210>653

<211>52

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>653

Arg Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg

1 5 10 15

Asp Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly

20 25 30

Asp Cys Arg Gly Phe Arg Arg Arg Cys Arg Cys Thr Arg Pro Cys Val

35 40 45

Phe Asp Glu Lys

fifty

<210>654

<211>75

<212>PRT/Protein

<213>Citrus sinensis

<400>654

Met Asp Ser Arg Ser Phe Gly Leu Leu Pro Leu Leu Leu Leu Ile Leu

1 5 10 15

Leu Thr Ser Gln Met Thr Val Leu Gln Thr Glu Ala Arg Leu Cys Glu

20 25 30

Ser Gln Ser His Arg Phe His Gly Thr Cys Val Arg Ser His Asn Cys

35 40 45

Asp Leu Val Cys Arg Thr Glu Gly Phe Thr Gly Gly Arg Cys Arg Gly

50 55 60

Phe Arg Arg Arg Cys Phe Cys Thr Arg Ile Cys

65 70 75

<210>655

<211>73

<212>PRT/Protein

<213>Citrus paradise

<400>655

Met Lys Ser Phe Phe Gly Ile Phe Leu Leu Leu Leu Ile Leu Phe Ala

1 5 10 15

Ser Gln Glu Ile Met Val Pro Ala Glu Gly Arg Val Cys Gln Ser Gln

20 25 30

Ser His His Phe His Gly Ala Cys Phe Ser His His Asn Cys Ala Phe

35 40 45

Val Cys Arg Asn Glu Gly Phe Ser Gly Gly Lys Cys Arg Gly Val Arg

50 55 60

Arg Arg Cys Phe Cys Ser Lys Leu Cys

65 70

<210>656

<211>72

<212>PRT/Protein

<213>Citrus clementina

<400>656

Met Lys Ser Phe Phe Gly Ile Phe Leu Leu Leu Leu Ile Leu Phe Ala

1 5 10 15

Ser Gln Met Met Val Pro Ala Glu Gly Arg Val Cys Gln Ser Gln Ser

20 25 30

His His Phe His Gly Ala Cys Phe Ser His His Asn Cys Ala Phe Val

35 40 45

Cys Arg Asn Glu Gly Phe Ser Gly Gly Lys Cys Arg Gly Ala Arg Arg

50 55 60

Arg Cys Phe Cys Ser Lys Leu Cys

65 70

<210>657

<211>73

<212>PRT/Protein

<213>Citrus clementina

<400>657

Met Lys Ser Phe Phe Gly Ile Phe Leu Leu Leu Leu Ile Leu Phe Ala

1 5 10 15

Ser Gln Glu Met Met Val Pro Ala Glu Gly Arg Val Cys Gln Ser Gln

20 25 30

Ser His His Phe His Gly Ala Cys Phe Ser His His Asn Cys Ala Phe

35 40 45

Val Cys Arg Asn Glu Gly Phe Ser Gly Gly Lys Cys Arg Gly Ala Arg

50 55 60

Arg Arg Cys Phe Cys Ser Lys Leu Cys

65 70

<210>658

<211>72

<212>PRT/Protein

<213>Citrus clementina

<400>658

Met Lys Ser Phe Phe Gly Ile Phe Leu Leu Leu Leu Ile Leu Phe Ala

1 5 10 15

Ser Gln Met Met Val Pro Ala Glu Gly Arg Val Cys Gln Ser Gln Ser

20 25 30

His His Phe His Gly Ala Cys Phe Ser His His Asn Cys Ala Phe Val

35 40 45

Cys Arg Asn Glu Gly Phe Ser Gly Gly Lys Cys Arg Gly Ala Arg Arg

50 55 60

Arg Cys Phe Cys Ser Lys Leu Cys

65 70

<210>659

<211>78

<212>PRT/Protein

<213>Nicotiana benthamiana

<400>659

Met Ala Asn Ser Met Arg Phe Phe Ala Thr Val Leu Leu Leu Ala Leu

1 5 10 15

Leu Val Met Ala Thr Glu Met Gly Pro Met Thr Ile Ala Glu Ala Arg

20 25 30

Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg Asp

35 40 45

Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly Asp

50 55 60

Cys Arg Gly Phe Arg Arg Arg Cys Phe Cys Thr Arg Pro Cys

65 70 75

<210>660

<211>78

<212>PRT/Protein

<213>Nicotiana sylvestris

<400>660

Met Ala Lys Ser Met Arg Phe Phe Ala Thr Val Leu Leu Leu Ala Leu

1 5 10 15

Leu Val Met Ala Thr Glu Met Gly Pro Thr Thr Ile Ala Glu Ala Arg

20 25 30

Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg Asp

35 40 45

Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly Asp

50 55 60

Cys Arg Gly Phe Arg Arg Arg Cys Phe Cys Thr Arg Pro Cys

65 70 75

<210>661

<211>78

<212>PRT/Protein

<213>Nicotiana tabacum

<400>661

Met Ala Asn Ser Met Arg Phe Phe Ala Thr Val Leu Leu Leu Thr Leu

1 5 10 15

Leu Val Met Ala Thr Glu Met Gly Pro Met Thr Ile Ala Glu Ala Arg

20 25 30

Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg Asp

35 40 45

Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly Asp

50 55 60

Cys Arg Gly Phe Arg Arg Arg Cys Phe Cys Thr Arg Pro Cys

65 70 75

<210>662

<211>78

<212>PRT/Protein

<213>Nicotiana tomentosiformis

<400>662

Met Ala Asn Ser Met Arg Phe Phe Ala Thr Val Leu Leu Ile Ala Leu

1 5 10 15

Leu Val Met Ala Thr Glu Met Gly Pro Met Thr Ile Ala Glu Ala Arg

20 25 30

Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg Asp

35 40 45

Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly Asp

50 55 60

Cys Arg Gly Phe Arg Arg Arg Cys Phe Cys Thr Arg Pro Cys

65 70 75

<210>663

<211>78

<212>PRT/Protein

<213>Nicotiana tabacum

<400>663

Met Ala Asn Ser Met Arg Phe Phe Ala Thr Val Leu Leu Ile Ala Leu

1 5 10 15

Leu Val Thr Ala Thr Glu Met Gly Pro Met Thr Ile Ala Glu Ala Arg

20 25 30

Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ser Arg Asp

35 40 45

Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly Asp

50 55 60

Cys Arg Gly Phe Arg Arg Arg Cys Phe Cys Thr Arg Pro Cys

65 70 75

<210>664

<211>78

<212>PRT/Protein

<213>Nicotiana alata

<400>664

Met Ala Asn Ser Met Arg Phe Phe Ala Thr Val Leu Leu Leu Thr Leu

1 5 10 15

Leu Phe Met Ala Thr Glu Met Gly Pro Met Thr Ile Ala Glu Ala Arg

20 25 30

Thr Cys Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Ala Arg Asp

35 40 45

Ser Asn Cys Ala Thr Val Cys Leu Thr Glu Gly Phe Ser Gly Gly Asp

50 55 60

Cys Arg Gly Phe Arg Arg Arg Cys Phe Cys Thr Arg Pro Cys

65 70 75

<210>665

<211>80

<212>PRT/Protein

<213>Avena sativa

<400>665

Met Gly Ser Ile Lys Gly Leu Lys Ser Val Val Ile Cys Val Leu Val

1 5 10 15

Leu Gly Ile Val Leu Glu Gln Val Gln Val Glu Gly Lys Ser Cys Cys

20 25 30

Lys Asp Ile Met Ala Arg Asn Cys Tyr Asn Val Cys Arg Ile Pro Gly

35 40 45

Thr Pro Arg Pro Val Cys Ala Thr Thr Cys Arg Cys Lys Ile Ile Ser

50 55 60

Gly Asn Lys Cys Pro Lys Asp Tyr Pro Lys Leu His Gly Asp Pro Asp

65 70 75 80

<210>666

<211>80

<212>PRT/Protein

<213>Avena sativa

<400>666

Met Gly Ser Ile Lys Gly Leu Lys Ser Val Val Ile Cys Val Leu Val

1 5 10 15

Leu Gly Ile Val Leu Glu His Val Gln Val Glu Gly Lys Ser Cys Cys

20 25 30

Lys Asp Thr Thr Ala Arg Asn Cys Tyr Asn Val Cys Arg Ile Pro Gly

35 40 45

Thr Pro Arg Pro Val Cys Ala Thr Thr Cys Arg Cys Lys Ile Ile Ser

50 55 60

Gly Asn Lys Cys Pro Lys Asp Tyr Pro Lys Leu His Gly Asp Leu Asp

65 70 75 80

<210>667

<211>112

<212>PRT/Protein

<213>Tulipa gesneriana

<400>667

Leu Gly Leu Val Val Ala Gln Thr Gln Val Asp Ala Lys Ser Cys Cys

1 5 10 15

Pro Ser Thr Ala Ala Arg Asn Cys Tyr Asn Val Cys Arg Phe Pro Gly

20 25 30

Thr Pro Arg Pro Val Cys Ala Ala Thr Cys Gly Cys Lys Ile Ile Thr

35 40 45

Gly Thr Lys Cys Pro Pro Asp Tyr Pro Lys Leu Gly Trp Ser Thr Phe

50 55 60

Gln Asn Ser Asp Val Ala Asp Lys Ala Leu Asp Val Val Asp Glu Ala

65 70 75 80

Leu His Val Ala Lys Glu Val Met Lys Glu Ala Val Glu Arg Cys Asn

85 90 95

Asn Ala Cys Ser Glu Val Cys Thr Lys Gly Ser Tyr Ala Val Thr Ala

100 105 110

<210>668

<211>75

<212>PRT/Protein

<213>Vitis vinifera

<400>668

Met Glu Arg Lys Ser Leu Gly Phe Phe Phe Phe Leu Leu Leu Ile Leu

1 5 10 15

Leu Ala Ser Gln Glu Met Val Val Pro Ser Glu Ala Arg Val Cys Glu

20 25 30

Ser Gln Ser His Lys Phe Glu Gly Ala Cys Met Gly Asp His Asn Cys

35 40 45

Ala Leu Val Cys Arg Asn Glu Gly Phe Ser Gly Gly Lys Cys Lys Gly

50 55 60

Leu Arg Arg Arg Cys Phe Cys Thr Lys Leu Cys

65 70 75

<210>669

<211>74

<212>PRT/Protein

<213>Vitis vinifera

<400>669

Met Glu Arg Lys Ser Leu Gly Phe Phe Phe Phe Leu Leu Leu Ile Leu

1 5 10 15

Leu Ala Ser Gln Met Val Val Pro Ser Glu Ala Arg Val Cys Glu Ser

20 25 30

Gln Ser His Lys Phe Glu Gly Ala Cys Met Gly Asp His Asn Cys Ala

35 40 45

Leu Val Cys Arg Asn Glu Gly Phe Ser Gly Gly Lys Cys Lys Gly Leu

50 55 60

Arg Arg Arg Cys Phe Cys Thr Lys Leu Cys

65 70

<210>670

<211>76

<212>PRT/Protein

<213>Citrus sinensis

<400>670

Met Glu Arg Ser Val Arg Leu Phe Ser Thr Val Leu Leu Val Leu Leu

1 5 10 15

Leu Leu Ala Ser Glu Met Gly Leu Arg Ala Ala Glu Ala Arg Ile Cys

20 25 30

Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Val Ser Lys Ser Asn

35 40 45

Cys Ala Ala Val Cys Gln Thr Glu Gly Phe His Gly Gly His Cys Arg

50 55 60

Gly Phe Arg Arg Arg Cys Phe Cys Thr Lys Arg Cys

65 70 75

<210>671

<211>50

<212>PRT/Protein

<213>Aesculus hippocastanum

<400>671

Leu Cys Asn Glu Arg Pro Ser Gln Thr Trp Ser Gly Asn Cys Gly Asn

1 5 10 15

Thr Ala His Cys Asp Lys Gln Cys Gln Asp Trp Glu Lys Ala Ser His

20 25 30

Gly Ala Cys His Lys Arg Glu Asn His Trp Lys Cys Phe Cys Tyr Phe

35 40 45

Asn Cys

fifty

<210>672

<211>81

<212>PRT/Protein

<213>Dacus carota

<400>672

Met Ala Lys Asn Ser Thr Ser Pro Val Ser Leu Phe Ala Ile Ser Leu

1 5 10 15

Ile Phe Phe Leu Leu Ala Asn Ser Gly Ser Ile Thr Glu Val Asp Gly

20 25 30

Lys Val Cys Glu Lys Pro Ser Leu Thr Trp Ser Gly Lys Cys Gly Asn

35 40 45

Thr Gln His Cys Asp Lys Gln Cys Gln Asp Trp Glu Gly Ala Lys His

50 55 60

Gly Ala Cys His Ser Arg Gly Gly Trp Lys Cys Phe Cys Tyr Phe Glu

65 70 75 80

Cys

<210>673

<211>49

<212>PRT/Protein

<213>Clitoria ternatea

<400>673

Asn Leu Cys Glu Arg Ala Ser Leu Thr Trp Thr Gly Asn Cys Gly Asn

1 5 10 15

Thr Gly His Cys Asp Thr Gln Cys Arg Asn Trp Glu Ser Ala Lys His

20 25 30

Gly Ala Cys His Lys Arg Gly Asn Trp Lys Cys Phe Cys Tyr Phe Asn

35 40 45

Cys

<210>674

<211>80

<212>PRT/Protein

<213>Dacus carota

<400>674

Met Ala Lys Lys Ser Ser Ser Phe Cys Leu Ser Ala Ile Phe Leu Val

1 5 10 15

Leu Leu Leu Val Ala Asn Thr Gly Met Val Arg Glu Val Asp Gly Ala

20 25 30

Leu Cys Glu Lys Pro Ser Leu Thr Trp Ser Gly Asn Cys Arg Asn Thr

35 40 45

Gln His Cys Asp Lys Gln Cys Gln Ser Trp Glu Gly Ala Lys His Gly

50 55 60

Ala Cys His Lys Arg Gly Asn Trp Lys Cys Phe Cys Tyr His Ala Cys

65 70 75 80

<210>675

<211>92

<212>PRT/Protein

<213>Bupleurum kaoi

<400>675

Met Ala Lys Lys Leu Asn Ala Val Thr Val Ser Ala Ile Phe Leu Val

1 5 10 15

Val Phe Leu Ile Ala Ser Tyr Ser Val Gly Ala Ala Lys Glu Ala Gly

20 25 30

Ala Glu Gly Glu Val Val Phe Pro Glu Gln Leu Cys Glu Arg Ala Ser

35 40 45

Gln Thr Trp Ser Gly Asp Cys Lys Asn Thr Lys Asn Cys Asp Asn Gln

50 55 60

Cys Ile Gln Trp Glu Lys Ala Arg His Gly Ala Cys His Lys Arg Gly

65 70 75 80

Gly Lys Trp Met Cys Phe Cys Tyr Phe Asp Lys Cys

85 90

<210>676

<211>50

<212>PRT/Protein

<213>Dahlia merckii

<400>676

Glu Leu Cys Glu Lys Ala Ser Lys Thr Trp Ser Gly Asn Cys Gly Asn

1 5 10 15

Thr Gly His Cys Asp Asn Gln Cys Lys Ser Trp Glu Gly Ala Ala His

20 25 30

Gly Ala Cys His Val Arg Asn Gly Lys His Met Cys Phe Cys Tyr Phe

35 40 45

Asn Cys

fifty

<210>677

<211>108

<212>PRT/Protein

<213>Helianthus annuus

<400>677

Met Ala Lys Ile Ser Val Ala Phe Asn Ala Phe Leu Leu Leu Leu Phe

1 5 10 15

Val Leu Ala Ile Ser Glu Ile Gly Ser Val Lys Gly Glu Leu Cys Glu

20 25 30

Lys Ala Ser Gln Thr Trp Ser Gly Thr Cys Gly Lys Thr Lys His Cys

35 40 45

Asp Asp Gln Cys Lys Ser Trp Glu Gly Ala Ala His Gly Ala Cys His

50 55 60

Val Arg Asp Gly Lys His Met Cys Phe Cys Tyr Phe Asn Cys Ser Lys

65 70 75 80

Ala Gln Lys Leu Ala Gln Asp Lys Leu Arg Ala Glu Glu Leu Ala Lys

85 90 95

Glu Lys Ile Glu Pro Glu Lys Ala Thr Ala Lys Pro

100 105

<210>678

<211>117

<212>PRT/Protein

<213>Cynara cardunculus

<400>678

Met Ala Lys Asn Ser Val Ala Phe Phe Ala Leu Leu Leu Leu Ile Cys

1 5 10 15

Ile Leu Thr Ile Ser Glu Phe Ala Val Val Lys Gly Glu Leu Cys Glu

20 25 30

Lys Ala Ser Lys Thr Trp Ser Gly Asn Cys Gly Asn Thr Arg His Cys

35 40 45

Asp Asp Gln Cys Lys Ala Trp Glu Gly Ala Ala His Gly Ala Cys His

50 55 60

Thr Arg Asn Lys Lys His Met Cys Phe Cys Tyr Phe Asn Cys Pro Lys

65 70 75 80

Ala Glu Lys Leu Ala Gln Asp Lys Leu Lys Ala Glu Glu Glu Leu Ala Arg

85 90 95

Asp Lys Val Glu Ala Lys Glu Val Pro His Phe Lys His Pro Ile Glu

100 105 110

Pro Ile His His Pro

115

<210>679

<211>117

<212>PRT/Protein

<213>Cynara cardunculus

<400>679

Met Ala Lys Gln Trp Val Ser Phe Phe Ala Leu Ala Phe Ile Val Phe

1 5 10 15

Val Leu Ala Ile Ser Glu Thr Gln Thr Val Lys Gly Glu Leu Cys Glu

20 25 30

Lys Ala Ser Lys Thr Trp Ser Gly Asn Cys Gly Asn Thr Lys His Cys

35 40 45

Asp Asp Gln Cys Lys Ser Trp Glu Gly Ala Ala His Gly Ala Cys His

50 55 60

Val Arg Asn Gly Lys His Met Cys Phe Cys Tyr Phe Asn Ser Cys Ala

65 70 75 80

Glu Ala Asp Lys Leu Ser Glu Asp Gln Ile Glu Ala Gly Lys Leu Ala

85 90 95

Phe Glu Lys Ala Glu Lys Leu Asp Arg Asp Val Lys Lys Ala Val Pro

100 105 110

Asn Val Asp His Pro

115

<210>680

<211>94

<212>PRT/Protein

<213>Daucus carota

<400>680

Met Ala Gln Lys Val Asn Ser Ala Leu Ile Phe Ser Ala Ile Phe Val

1 5 10 15

Leu Phe Leu Val Ala Ser Tyr Ser Val Thr Val Ala Glu Gly Ala Arg

20 25 30

Ala Gly Ala Glu Gly Glu Val Val Tyr Pro Glu Ala Leu Cys Glu Arg

35 40 45

Ala Ser Gln Thr Trp Thr Gly Lys Cys Gln His Thr Asp His Cys Asp

50 55 60

Asn Gln Cys Ile Gln Trp Glu Asn Ala Arg His Gly Ala Cys His Lys

65 70 75 80

Arg Gly Gly Asn Trp Lys Cys Phe Cys Tyr Phe Asp His Cys

85 90

<210>681

<211>78

<212>PRT/Protein

<213>Arabidopsis lyrata

<400>681

Met Ala Ser Ser Tyr Thr Leu Met Leu Phe Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Met Met Ala Val Glu Ala Arg Ile Cys Glu

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Ser Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>682

<211>80

<212>PRT/Protein

<213>Parthenium hysterophorus

<400>682

Met Ala Lys Ser Ser Thr Ser Tyr Leu Val Phe Leu Leu Leu Val Leu

1 5 10 15

Val Val Ala Ile Ser Glu Ile Ala Ser Val Asn Gly Lys Val Cys Glu

20 25 30

Lys Pro Ser Lys Thr Trp Phe Gly Asn Cys Lys Asp Thr Glu Lys Cys

35 40 45

Asp Lys Arg Cys Met Glu Trp Glu Gly Ala Lys His Gly Ala Cys His

50 55 60

Gln Arg Glu Ser Lys Tyr Met Cys Phe Cys Tyr Phe Asp Cys Asp Pro

65 70 75 80

<210>683

<211>78

<212>PRT/Protein

<213>Arabidopsis thaliana

<400>683

Met Ala Ser Ser Tyr Thr Leu Met Leu Phe Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Met Met Ala Val Glu Gly Arg Ile Cys Glu

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>684

<211>78

<212>PRT/Protein

<213>Eutrema salsugineum

<400>684

Met Ala Ser Ser Tyr Thr Leu Leu Leu Phe Val Cys Leu Ser Ile Phe

1 5 10 15

Phe Ile Ala Ser Thr Glu Met Met Met Val Glu Gly Arg Val Cys Glu

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>685

<211>82

<212>PRT/Protein

<213>Vitis vinifera

<400>685

Met Ala Lys Leu Leu Gly Tyr Leu Leu Ser Tyr Ala Leu Ser Phe Leu

1 5 10 15

Thr Leu Phe Ala Leu Leu Val Ser Thr Glu Met Val Met Leu Glu Ala

20 25 30

Lys Val Cys Gln Arg Pro Ser Lys Thr Trp Ser Gly Phe Cys Gly Ser

35 40 45

Ser Lys Asn Cys Asp Arg Gln Cys Lys Asn Trp Glu Gly Ala Lys His

50 55 60

Gly Ala Cys His Ala Lys Phe Pro Gly Val Ala Cys Phe Cys Tyr Phe

65 70 75 80

Asn Cys

<210>686

<211>82

<212>PRT/Protein

<213>Corchorus olitorius

<400>686

Met Ala Lys Ser Leu Ser Ser Phe Ala Thr Phe Leu Ala Leu Leu Cys

1 5 10 15

Leu Phe Phe Leu Leu Ser Thr Pro Asn Glu Met Lys Met Ala Glu Ala

20 25 30

Lys Ile Cys Glu Lys Arg Ser Gln Thr Trp Ser Gly Trp Cys Gly Asn

35 40 45

Ser Ser His Cys Asp Arg Gln Cys Lys Asn Trp Glu Asn Ala Arg His

50 55 60

Gly Ser Cys His Ala Asp Gly Leu Gly Trp Ala Cys Phe Cys Tyr Phe

65 70 75 80

Asn Cys

<210>687

<211>58

<212>PRT/Protein

<213>Corchorus olitorius

<400>687

Met Glu Met Lys Met Ala Glu Gly Lys Ile Cys Glu Lys Arg Ser Gln

1 5 10 15

Thr Trp Ser Gly Trp Cys Gly Asn Ser Ser His Cys Asp Arg Gln Cys

20 25 30

Lys Asn Trp Glu Asn Ala Arg His Gly Ser Cys His Ala Asp Gly Leu

35 40 45

Gly Trp Ala Cys Phe Cys Tyr Phe Asn Cys

50 55

<210>688

<211>78

<212>PRT/Protein

<213>Camelina sativa

<400>688

Met Ala Ser Ser Leu Lys Leu Met Leu Phe Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Met Met Thr Val Glu Gly Arg Thr Cys Glu

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Arg Ser Trp Glu Gly Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>689

<211>84

<212>PRT/Protein

<213>Cucumis sativus

<400>689

Met Ala Lys Val Val Gly Asn Ser Ala Lys Met Ile Val Ala Leu Leu

1 5 10 15

Phe Leu Leu Ala Leu Met Leu Ser Met Asn Glu Lys Gln Gly Val Val

20 25 30

Glu Ala Lys Val Cys Glu Arg Arg Ser Lys Thr Trp Ser Gly Trp Cys

35 40 45

Gly Asn Thr Lys His Cys Asp Arg Gln Cys Lys Asn Trp Glu Gly Ala

50 55 60

Thr His Gly Ala Cys His Ala Gln Phe Pro Gly Arg Ala Cys Phe Cys

65 70 75 80

Tyr Phe Asn Cys

<210>690

<211>80

<212>PRT/Protein

<213>Cynara cardunculus

<400>690

Met Ile Asp Ala Phe Asn Tyr Lys Gln Phe Ser Thr Val Lys Gly Lys

1 5 10 15

Ile Cys Glu Lys Pro Ser Lys Thr Trp Phe Gly Lys Cys Gln Asp Thr

20 25 30

Thr Lys Cys Asp Lys Gln Cys Ile Glu Trp Glu Asp Ala Lys His Gly

35 40 45

Ala Cys His Glu Arg Glu Ser Lys Leu Met Cys Phe Cys Tyr Tyr Asn

50 55 60

Cys Gly Pro Pro Lys Asn Thr Pro Pro Gly Thr Pro Pro Ser Pro Pro

65 70 75 80

<210>691

<211>78

<212>PRT/Protein

<213>Capsella rubella

<400>691

Met Ala Ser Ser Tyr Lys Leu Ile Leu Phe Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Phe Glu Met Met Ala Val Glu Gly Arg Ile Cys Gln

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>692

<211>56

<212>PRT/Protein

<213>Arabidopsis thaliana

<400>692

Met Met Ala Val Glu Gly Arg Ile Cys Glu Arg Arg Ser Lys Thr Trp

1 5 10 15

Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys Asp Ser Gln Cys Lys Arg

20 25 30

Trp Glu Arg Ala Ser His Gly Ala Cys His Ala Gln Phe Pro Gly Phe

35 40 45

Ala Cys Phe Cys Tyr Phe Asn Cys

50 55

<210>693

<211>78

<212>PRT/Protein

<213>Brassica napus

<400>693

Met Ala Ser Ser Tyr Thr Arg Leu Leu Leu Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Val Met Val Glu Gly Arg Val Cys Gln

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>694

<211>78

<212>PRT/Protein

<213>Brassica rapa

<400>694

Met Ala Ser Ser Tyr Ala Arg Leu Leu Leu Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Val Met Val Glu Gly Arg Val Cys Gln

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>695

<211>78

<212>PRT/Protein

<213>Camelina sativa

<400>695

Met Ala Ser Ser Leu Lys Leu Met Leu Phe Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Met Met Thr Val Glu Gly Arg Thr Cys Glu

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Arg Arg Trp Glu His Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>696

<211>77

<212>PRT/Protein

<213>Brassica napus

<400>696

Met Ala Ser Tyr Thr Arg Leu Leu Leu Leu Cys Leu Ser Ile Phe Leu

1 5 10 15

Ile Ala Ser Thr Glu Val Met Met Val Glu Gly Arg Val Cys Gln Arg

20 25 30

Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys Asp

35 40 45

Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His Ala

50 55 60

Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>697

<211>56

<212>PRT/Protein

<213>Vitis vinifera

<400>697

Met Val Met Leu Glu Ala Lys Val Cys Gln Arg Pro Ser Lys Thr Trp

1 5 10 15

Ser Gly Phe Cys Gly Ser Ser Lys Asn Cys Asp Arg Gln Cys Lys Asn

20 25 30

Trp Glu Gly Ala Lys His Gly Ala Cys His Ala Lys Phe Pro Gly Val

35 40 45

Ala Cys Phe Cys Tyr Phe Asn Cys

50 55

<210>698

<211>88

<212>PRT/Protein

<213>Brassica napus

<400>698

Met Thr Lys Ser Phe Ile Leu Val Ala Leu Leu Cys Ile Cys Phe Ile

1 5 10 15

Leu Leu Ser Pro Thr Glu Met Arg Leu Thr Leu Asn Ala Cys Leu Lys

20 25 30

Leu Ala Glu Ala Lys Ile Cys Glu Lys Tyr Ser Gln Thr Trp Ser Gly

35 40 45

Arg Cys Thr Lys Thr Ser His Cys Asp Arg Gln Cys Ile Asn Trp Glu

50 55 60

Asp Ala Arg His Gly Ala Cys His Gln Asp Lys His Gly Arg Ala Cys

65 70 75 80

Phe Cys Tyr Phe Asn Cys Lys Lys

85

<210>699

<211>78

<212>PRT/Protein

<213>Raphanus sativus

<400>699

Met Ala Ser Ser Tyr Thr Val Phe Leu Leu Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Ala Ser Thr Glu Val Met Val Glu Gly Arg Val Cys Gln

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu His Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>700

<211>78

<212>PRT/Protein

<213>Arabis alpine

<400>700

Met Ala Ser Ser Tyr Thr Leu Leu Leu Phe Leu Cys Leu Ser Ile Phe

1 5 10 15

Leu Ile Val Ser Thr Glu Met Met Met Val Glu Gly Arg Ile Cys Glu

20 25 30

Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Ala Asn Thr Arg Gly Cys

35 40 45

Asp Ser Gln Cys Lys Arg Trp Glu Arg Ala Ser His Gly Ala Cys His

50 55 60

Ala Gln Phe Pro Gly Val Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>701

<211>84

<212>PRT/Protein

<213>Cucumis melo

<400>701

Met Ala Lys Val Val Gly Asn Ser Ala Lys Met Ile Val Ala Phe Leu

1 5 10 15

Phe Leu Leu Ala Leu Thr Leu Ser Met Asn Glu Lys Gln Gly Val Val

20 25 30

Glu Ala Lys Val Cys Glu Arg Arg Ser Lys Thr Trp Ser Gly Trp Cys

35 40 45

Gly Asp Thr Lys His Cys Asp Arg Gln Cys Lys Asn Trp Glu Gly Ala

50 55 60

Lys His Gly Ala Cys His Ala Gln Phe Pro Gly Arg Ala Cys Phe Cys

65 70 75 80

Tyr Phe Asn Cys

<210>702

<211>82

<212>PRT/Protein

<213>Erythranthe guttate

<400>702

Met Ala Ala Ser Leu Val Tyr Arg Leu Ser Ser Val Ile Leu Ile Val

1 5 10 15

Leu Leu Leu Phe Ile Met Leu Asn Asn Glu Val Met Val Val Glu Ser

20 25 30

Arg Leu Cys Glu Arg Arg Ser Lys Thr Trp Thr Gly Phe Cys Gly Ser

35 40 45

Ser Asn Asn Cys Asn Asn Gln Cys Arg Asn Trp Glu Arg Ala Ser His

50 55 60

Gly Ala Cys His Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe

65 70 75 80

Asn Cys

<210>703

<211>76

<212>PRT/Protein

<213>Sesamum indicum

<400>703

Met Ala Lys Phe Gln Val Ser Thr Ile Phe Phe Ala Leu Phe Phe

1 5 10 15

Cys Phe Leu Leu Leu Ala Ser Asn Glu Ala Lys Ile Cys Gln Arg Met

20 25 30

Ser Lys Thr Trp Ser Gly Val Cys Leu Asn Ser Gly Asn Cys Asp Arg

35 40 45

Gln Cys Arg Asn Trp Glu Arg Ala Gln His Gly Ala Cys His Arg Arg

50 55 60

Gly Leu Gly Phe Ala Cys Leu Cys Tyr Phe Lys Cys

65 70 75

<210>704

<211>110

<212>PRT/Protein

<213>Eclipta prostrata

<400>704

Met Ala Lys Asn Ser Val Ala Phe Phe Ala Phe Leu Leu Ile Leu Phe

1 5 10 15

Val Leu Ala Ile Ser Glu Ile Gly Ser Val Lys Gly Glu Leu Cys Glu

20 25 30

Lys Ala Ser Gln Thr Trp Ser Gly Thr Cys Arg Ile Thr Ser His Cys

35 40 45

Asp Asn Gln Cys Lys Ser Trp Glu Gly Ala Ala His Gly Ala Cys His

50 55 60

Val Arg Gly Gly Lys His Met Cys Phe Cys Tyr Phe Ser His Cys Ala

65 70 75 80

Lys Ala Glu Lys Leu Thr Gln Asp Lys Leu Lys Ala Gly His Leu Val

85 90 95

Asn Glu Lys Ser Glu Ala Asp Gln Lys Val Pro Val Thr Pro

100 105 110

<210>705

<211>105

<212>PRT/Protein

<213>Cynara cardunculus

<400>705

Met Ala Lys Asn Thr Lys Val Ser Ala Phe Leu Phe Val Phe Leu Phe

1 5 10 15

Val Phe Phe Leu Val Val His Ser Val Thr Ala Phe Ala Ile Arg Phe

20 25 30

Lys Cys Phe Asp Thr Asp Met Leu Leu Lys Val Ile Ala Asp Met Val

35 40 45

Val Gly Met Lys Gly Ile Glu Lys Val Cys Arg Arg Arg Ser Lys Thr

50 55 60

Trp Ser Gly Tyr Cys Gly Asp Ser Lys His Cys Asp Gln Gln Cys Arg

65 70 75 80

Glu Trp Glu Gly Ala Glu His Gly Ala Cys His His Glu Gly Leu Gly

85 90 95

Arg Ala Cys Phe Cys Tyr Phe Asn Cys

100 105

<210>706

<211>110

<212>PRT/Protein

<213>Ambrosia artemisiifolia

<400>706

Met Ala Ala Gly Leu Leu Val Phe Val Leu Ala Ile Ser Glu Ile Ala

1 5 10 15

Ser Val Lys Gly Lys Leu Cys Glu Lys Pro Ser Val Thr Trp Ser Gly

20 25 30

Lys Cys Lys Val Lys Gln Thr Asp Lys Cys Asp Lys Arg Cys Ile Glu

35 40 45

Trp Glu Gly Ala Lys His Gly Ala Cys His Lys Arg Asp Ser Lys Ala

50 55 60

Ser Cys Phe Cys Tyr Phe Asp Cys Asp Pro Thr Lys Asn Pro Gly Pro

65 70 75 80

Pro Pro Gly Ala Pro Lys Gly Lys Ala Pro Ala Pro Ser Pro Pro Ser

85 90 95

Gly Gly Gly Gly Glu Gly Gly Gly Glu Gly Gly Gly Glu Arg

100 105 110

<210>707

<211>111

<212>PRT/Protein

<213>Ambrosia artemisiifolia

<400>707

Met Ala Ala Gly Leu Leu Val Phe Val Leu Ala Ile Ser Glu Ile Ala

1 5 10 15

Ser Val Lys Gly Lys Leu Cys Glu Lys Pro Ser Leu Thr Trp Ser Gly

20 25 30

Lys Cys Lys Val Lys Gln Thr Asp Lys Cys Asp Lys Arg Cys Ile Glu

35 40 45

Trp Glu Gly Ala Lys His Gly Ala Cys His Lys Arg Asp Ser Lys Ala

50 55 60

Thr Cys Phe Cys Tyr Phe Asp Cys Asp Pro Thr Lys Asn Pro Gly Pro

65 70 75 80

Pro Pro Gly Ala Pro Lys Gly Lys Ala Pro Ala Pro Ser Pro Pro Ser

85 90 95

Gly Gly Gly Ala Pro Pro Ser Gly Gly Glu Gly Gly Glu Arg

100 105 110

<210>708

<211>79

<212>PRT/Protein

<213>Jatropha curcas

<400>708

Met Ala Lys Leu His Ser Ser Ala Leu Cys Phe Leu Ile Ile Phe Leu

1 5 10 15

Phe Leu Leu Val Ser Lys Glu Met Ala Val Thr Glu Ala Lys Leu Cys

20 25 30

Gln Arg Arg Ser Lys Thr Trp Ser Gly Phe Cys Gly Asp Pro Gly Lys

35 40 45

Cys Asn Arg Gln Cys Arg Asn Trp Glu Gly Ala Ser His Gly Ala Cys

50 55 60

His Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Lys Cys

65 70 75

<210>709

<211>79

<212>PRT/Protein

<213>Nelumbo nucifera

<400>709

Met Ala Lys Ala Pro Lys Ser Val Ser Tyr Phe Ala Phe Phe Phe Ile

1 5 10 15

Leu Phe Leu Leu Ala Ser Ser Glu Ile Gln Lys Thr Lys Lys Leu Cys

20 25 30

Glu Arg Arg Ser Lys Thr Trp Ser Gly Arg Cys Thr Lys Thr Gln Asn

35 40 45

Cys Asp Lys Gln Cys Lys Asp Trp Glu Tyr Ala Lys His Gly Ala Cys

50 55 60

His Gly Ser Trp Phe Asn Lys Lys Cys Tyr Cys Tyr Phe Asp Cys

65 70 75

<210>710

<211>82

<212>PRT/Protein

<213>Pyrus x bretschneideri

<400>710

Met Ala Lys Leu Leu Ser Arg Leu Ser Ile Pro Leu Ile Val Phe Val

1 5 10 15

Phe Leu Leu Ile Leu Leu Ala Ser Thr Glu Val Ala Met Val Glu Ala

20 25 30

Arg Ile Cys Gln Arg Arg Ser Lys Thr Trp Ser Gly Phe Cys Ala Asn

35 40 45

Thr Gly Asn Cys Asn Arg Gln Cys Thr Asn Trp Glu Gly Ala Leu His

50 55 60

Gly Ala Cys His Ala Gln Phe Pro Gly Val Ala Cys Phe Cys Tyr Phe

65 70 75 80

Arg Cys

<210>711

<211>83

<212>PRT/Protein

<213>Ricinus communis

<400>711

Met Ala Lys Leu His Phe Pro Thr Leu Leu Cys Leu Phe Ile Phe Leu

1 5 10 15

Phe Leu Leu Val Ser Thr Glu Met Gln Val Thr Gln Ala Lys Val Cys

20 25 30

Gln Arg Arg Ser Lys Thr Trp Ser Gly Phe Cys Gly Ser Thr Lys Asn

35 40 45

Cys Asp Arg Gln Cys Lys Asn Trp Glu Gly Ala Leu His Gly Ala Cys

50 55 60

His Ala Gln Phe Pro Gly Val Ala Cys Phe Cys Tyr Phe Lys Cys Gly

65 70 75 80

Gly Glu Arg

<210>712

<211>91

<212>PRT/Protein

<213>Ambrosia artemisiifolia

<400>712

Lys Leu Cys Glu Lys Pro Ser Val Thr Trp Ser Gly Lys Cys Lys Val

1 5 10 15

Lys Gln Thr Asp Lys Cys Asp Lys Arg Cys Ile Glu Trp Glu Gly Ala

20 25 30

Lys His Gly Ala Cys His Lys Arg Asp Ser Lys Ala Ser Cys Phe Cys

35 40 45

Tyr Phe Asp Cys Asp Pro Thr Lys Asn Pro Gly Pro Pro Pro Gly Ala

50 55 60

Pro Lys Gly Lys Ala Pro Ala Pro Ser Pro Pro Ser Gly Gly Gly Ala

65 70 75 80

Pro Pro Pro Ser Gly Gly Glu Gly Gly Gly Asp

85 90

<210>713

<211>96

<212>PRT/Protein

<213>Ambrosia artemisiifolia

<400>713

Lys Leu Cys Glu Lys Pro Ser Val Thr Trp Ser Gly Asn Lys Val Lys

1 5 10 15

Gln Thr Asp Lys Cys Asp Lys Arg Cys Ile Glu Trp Glu Gly Ala Lys

20 25 30

His Gly Ala Cys His Lys Arg Asp Ser Lys Ala Ser Cys Phe Cys Tyr

35 40 45

Phe Asp Cys Asp Pro Thr Lys Asn Pro Gly Pro Pro Pro Gly Ala Pro

50 55 60

Lys Gly Lys Ala Pro Ala Pro Ser Pro Pro Ser Gly Gly Gly Ala Pro

65 70 75 80

Pro Pro Ser Gly Gly Glu Gly Gly Gly Asp Gly Gly Gly Gly Arg Arg

85 90 95

<210>714

<211>82

<212>PRT/Protein

<213>Prunus mume

<400>714

Met Ala Lys Leu Leu Ser His Leu Leu Phe Tyr Pro Ile Leu Phe Leu

1 5 10 15

Phe Leu Phe Ile Phe Leu Ala Ser Thr Glu Val Ala Ile Leu Glu Ala

20 25 30

Arg Ile Cys Gln Arg Arg Ser Lys Thr Trp Ser Gly Phe Cys Gly Asn

35 40 45

Thr Arg Asn Cys Asn Arg Gln Cys Arg Asn Trp Glu Gly Ala Leu Arg

50 55 60

Gly Ala Cys His Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe

65 70 75 80

Arg Cys

<210>715

<211>80

<212>PRT/Protein

<213>Corchorus olitorius

<400>715

Met Ala Lys Thr Leu Gln Leu Phe Ala Leu Phe Phe Ile Val Ile Leu

1 5 10 15

Leu Ala Asn Gln Glu Ile Pro Val Ala Glu Ala Lys Leu Cys Gln Lys

20 25 30

Arg Ser Lys Thr Trp Thr Gly Ile Cys Ile Lys Thr Lys Asn Cys Asp

35 40 45

Asn Gln Cys Lys Lys Trp Glu Lys Ala Glu His Gly Ala Cys His Arg

50 55 60

Gln Gly Ile Gly Phe Ala Cys Phe Cys Tyr Phe Asn Gln Lys Lys Cys

65 70 75 80

<210>716

<211>81

<212>PRT/Protein

<213>Corchorus olitorius

<400>716

Met Ala Lys Phe Val Ser Thr Val Ala Leu Leu Phe Ala Leu Phe Ile

1 5 10 15

Leu Leu Ala Ser Phe Asp Glu Gly Met Met Pro Met Ala Glu Ala Lys

20 25 30

Val Cys Ser Lys Arg Ser Lys Thr Trp Ser Gly Phe Cys Asn Ser Ser

35 40 45

Ala Asn Cys Asn Lys Gln Cys Arg Glu Trp Glu Asp Ala Lys His Gly

50 55 60

Ala Cys His Phe Glu Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asn

65 70 75 80

Cys

<210>717

<211>76

<212>PRT/Protein

<213>Solanum pennellii

<400>717

Met Asn Ser Lys Val Ile Leu Ala Leu Leu Val Cys Phe Leu Leu Ile

1 5 10 15

Ala Ser Asn Glu Met Gln Gly Gly Glu Ala Lys Val Cys Gly Arg Arg

20 25 30

Ser Ser Thr Trp Ser Gly Leu Cys Leu Asn Thr Gly Asn Cys Asn Thr

35 40 45

Gln Cys Ile Lys Trp Glu His Ala Ser Ser Gly Ala Cys His Arg Asp

50 55 60

Gly Phe Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75

<210>718

<211>82

<212>PRT/Protein

<213>Fragaria vesca

<400>718

Met Ala Lys Leu Leu Gly Tyr His Leu Val Tyr Pro Ile Leu Phe Leu

1 5 10 15

Phe Ile Phe Leu Leu Leu Ala Ser Thr Glu Met Gly Met Leu Glu Ala

20 25 30

Arg Ile Cys Gln Arg Arg Ser Lys Thr Trp Thr Gly Leu Cys Ala Asn

35 40 45

Thr Gly Asn Cys His Arg Gln Cys Arg Asn Trp Glu Gly Ala Gln Arg

50 55 60

Gly Ala Cys His Ala Gln Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe

65 70 75 80

Asn Cys

<210>719

<211>80

<212>PRT/Protein

<213>Corchorus capsularis

<400>719

Met Ala Lys Phe Val Ser Val Ala Leu Leu Leu Ala Leu Phe Ile Leu

1 5 10 15

Val Ala Ser Phe Asp Glu Gly Met Val Pro Met Ala Glu Ala Lys Leu

20 25 30

Cys Ser Lys Arg Ser Lys Thr Trp Ser Gly Phe Cys Asn Ser Ser Ala

35 40 45

Asn Cys Asn Arg Gln Cys Arg Glu Trp Glu Asp Ala Lys His Gly Ala

50 55 60

Cys His Phe Glu Phe Pro Gly Phe Ala Cys Phe Cys Tyr Phe Asp Cys

65 70 75 80

<210>720

<211>56

<212>PRT/Protein

<213>Solanum tuberosum

<400>720

Met Gln Gly Gly Glu Ala Arg Val Cys Glu Arg Arg Ser Ser Ser Thr Trp

1 5 10 15

Ser Gly Pro Cys Phe Asp Thr Gly Asn Cys Asn Arg Gln Cys Ile Asn

20 25 30

Trp Glu His Ala Ser Ser Gly Ala Cys His Arg Glu Gly Ile Gly Ser

35 40 45

Ala Cys Phe Cys Tyr Phe Asn Cys

50 55

<210>721

<211>80

<212>PRT/Protein

<213>Dimocarpus longan

<400>721

Met Ala Lys Thr Leu Lys Ser Val Gln Phe Phe Ala Leu Phe Phe Leu

1 5 10 15

Val Ile Leu Leu Ala Gly Ser Glu Met Thr Ala Val Glu Ala Leu Cys

20 25 30

Ser Lys Arg Ser Lys Thr Trp Ser Gly Pro Cys Phe Ile Thr Ser Arg

35 40 45

Cys Asp Arg Gln Cys Lys Arg Trp Glu Asn Ala Lys His Gly Ala Cys

50 55 60

His Arg Ser Gly Trp Gly Phe Ala Cys Phe Cys Tyr Phe Asn Lys Cys

65 70 75 80

<210>722

<211>80

<212>PRT/Protein

<213>Camelina sativa

<400>722

Met Ala Lys Ala Ala Thr Ile Val Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Phe Phe Ala Ala Leu Glu Thr Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Ser Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>723

<211>80

<212>PRT/Protein

<213>Arabis alpine

<400>723

Met Ala Lys Phe Ala Ser Ile Ile Ala Phe Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ser Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Tyr

20 25 30

Cys Glu Lys Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Ser Asn

35 40 45

Ala Cys Asn Asn Gln Cys Ile Asn Leu Glu Gly Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Tyr Tyr Arg Cys Ile Cys Tyr Phe Gln Cys

65 70 75 80

<210>724

<211>80

<212>PRT/Protein

<213>Theobroma cacao

<400>724

Met Ala Met Ser Leu Lys Ser Val His Phe Phe Ala Leu Phe Phe Ile

1 5 10 15

Val Val Leu Leu Ala Asn Gln Glu Met Pro Val Ala Glu Ala Lys Leu

20 25 30

Cys Gln Lys Arg Ser Lys Thr Trp Thr Gly Pro Cys Ile Lys Thr Lys

35 40 45

Asn Cys Asp His Gln Cys Arg Lys Trp Glu Lys Ala Gln His Gly Ala

50 55 60

Cys His Trp Gln Trp Pro Gly Phe Ala Cys Phe Cys Tyr Val Asn Cys

65 70 75 80

<210>725

<211>80

<212>PRT/Protein

<213>Amborella trichopoda

<400>725

Met Ala Lys Leu Val Ser Pro Lys Ala Phe Phe Val Phe Leu Phe Val

1 5 10 15

Phe Leu Leu Ile Ser Ala Ser Glu Phe Ser Gly Ser Glu Ala Lys Leu

20 25 30

Cys Gln Lys Arg Ser Arg Thr Trp Ser Gly Phe Cys Ala Asn Ser Asn

35 40 45

Asn Cys Ser Arg Gln Cys Lys Asn Leu Glu Gly Ala Arg Phe Gly Ala

50 55 60

Cys His Arg Gln Arg Ile Gly Leu Ala Cys Phe Cys Tyr Phe Asn Cys

65 70 75 80

<210>726

<211>80

<212>PRT/Protein

<213>Arabidopsis thaliana

<400>726

Met Ala Lys Ser Ala Thr Ile Val Thr Leu Phe Phe Ala Ala Leu Val

1 5 10 15

Phe Phe Ala Ala Leu Glu Ala Pro Met Val Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Ser Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>727

<211>80

<212>PRT/Protein

<213>Arabis alpine

<400>727

Met Ala Lys Phe Ala Ser Ile Ile Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ser Leu Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Gln Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Gly

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Tyr His Arg Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>728

<211>80

<212>PRT/Protein

<213>Brassica juncea

<400>728

Met Ala Lys Val Ala Ser Ile Ile Ala Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ala Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>729

<211>80

<212>PRT/Protein

<213>Brassica oleracea

<400>729

Met Ala Lys Phe Ala Ser Ile Ile Ala Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ala Leu Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>730

<211>80

<212>PRT/Protein

<213>Camelina sativa

<400>730

Met Ala Lys Pro Ala Thr Ile Val Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Phe Phe Ala Ala Leu Glu Thr Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>731

<211>80

<212>PRT/Protein

<213>Camelina sativa

<400>731

Met Ala Lys Ser Ala Thr Ile Val Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Phe Phe Ala Ala Leu Glu Thr Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>732

<211>80

<212>PRT/Protein

<213>Brassica napus

<400>732

Met Ala Lys Phe Ala Ser Ile Ile Ala Pro Leu Phe Ala Val Leu Val

1 5 10 15

Leu Phe Ala Ala Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>733

<211>80

<212>PRT/Protein

<213>Eutrema salsugineum

<400>733

Met Ala Lys Phe Ala Ser Ile Ile Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Val Phe Glu Gly Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>734

<211>80

<212>PRT/Protein

<213>Raphanus sativus

<400>734

Met Ala Lys Phe Ala Ser Ile Ile Ala Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ala Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>735

<211>80

<212>PRT/Protein

<213>Raphanus sativus

<400>735

Met Ala Lys Phe Ala Ser Ile Val Ser Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Thr Ala Phe Glu Ala Pro Ala Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>736

<211>76

<212>PRT/Protein

<213>Raphanus sativus

<400>736

Met Asn Thr Lys Val Ile Leu Ala Leu Leu Phe Cys Phe Leu Leu Val

1 5 10 15

Ala Ser Asn Glu Met Gln Val Gly Glu Ala Lys Val Cys Gln Arg Arg

20 25 30

Ser Lys Thr Trp Ser Gly Pro Cys Ile Asn Thr Gly Asn Cys Ser Arg

35 40 45

Gln Cys Lys Gln Gln Glu Asp Ala Arg Phe Gly Ala Cys His Arg Ser

50 55 60

Gly Phe Gly Phe Ala Cys Phe Cys Tyr Phe Lys Cys

65 70 75

<210>737

<211>80

<212>PRT/Protein

<213>Brassica rapa

<400>737

Met Ala Lys Phe Ala Ser Ile Ile Ala Pro Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ala Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>738

<211>76

<212>PRT/Protein

<213>Solanum pennellii

<400>738

Met Asn Thr Lys Leu Ile Leu Ala Leu Met Phe Cys Phe Leu Leu Ile

1 5 10 15

Ala Ser Asn Glu Met Gln Val Gly Glu Ala Lys Val Cys Gln Arg Arg

20 25 30

Ser Lys Thr Trp Ser Gly Pro Cys Ile Asn Thr Gly Asn Cys Ser Arg

35 40 45

Gln Cys Lys Gln Gln Glu Asp Ala Arg Phe Gly Ala Cys His Arg Ser

50 55 60

Gly Phe Gly Phe Ala Cys Phe Cys Tyr Phe Lys Cys

65 70 75

<210>739

<211>78

<212>PRT/Protein

<213>Citrus clementina

<400>739

Met Ala Lys Phe Thr Thr Thr Phe Ala Leu Leu Phe Ala Phe Phe Ile

1 5 10 15

Leu Phe Ala Ala Phe Asp Val Pro Met Ala Glu Ala Lys Val Cys Gln

20 25 30

Arg Arg Ser Lys Thr Trp Ser Gly Leu Cys Leu Asn Thr Gly Asn Cys

35 40 45

Ser Arg Gln Cys Lys Gln Gln Glu Asp Ala Arg Phe Gly Ala Cys His

50 55 60

Arg Gln Gly Ile Gly Phe Ala Cys Phe Cys Tyr Phe Lys Cys

65 70 75

<210>740

<211>80

<212>PRT/Protein

<213>Brassica rapa

<400>740

Met Ala Lys Phe Thr Ser Ile Ile Val Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Gly Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Arg Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala Arg Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>741

<211>78

<212>PRT/Protein

<213>Eutrema salsugineum

<400>741

Met Ala Lys Phe Ala Ser Ile Ile Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Thr Phe Ala Pro Thr Met Val Glu Ala Lys Leu Cys Glu

20 25 30

Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn Ala Cys

35 40 45

Lys Ser Gln Cys Gln Arg Leu Glu Gly Ala Arg His Gly Ser Cys Asn

50 55 60

Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75

<210>742

<211>79

<212>PRT/Protein

<213>Eutrema salsugineum

<400>742

Met Ala Lys Phe Ala Ser Ile Ile Thr Leu Leu Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Thr Phe Glu Ala Pro Thr Met Val Glu Ala Lys Leu Cys

20 25 30

Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn Ala

35 40 45

Cys Lys Ser Gln Cys Gln Arg Leu Glu Gly Ala Arg His Gly Ser Cys

50 55 60

Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75

<210>743

<211>80

<212>PRT/Protein

<213>Heliophila coronopifolia

<400>743

Met Ala Lys Phe Ala Ser Ile Ile Ala Phe Phe Phe Ala Ala Leu Val

1 5 10 15

Leu Phe Ala Ala Phe Glu Ala Pro Thr Ile Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Arg Asn Gln Cys Ile Asn Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>744

<211>80

<212>PRT/Protein

<213>Brassica oleracea

<400>744

Met Ala Lys Val Ala Ser Ile Val Ala Leu Leu Phe Pro Ala Leu Val

1 5 10 15

Ile Phe Ala Ala Phe Glu Ala Pro Thr Met Val Glu Ala Gln Lys Leu

20 25 30

Cys Glu Arg Pro Ser Gly Thr Trp Ser Gly Val Cys Gly Asn Asn Asn

35 40 45

Ala Cys Lys Asn Gln Cys Ile Arg Leu Glu Lys Ala Arg His Gly Ser

50 55 60

Cys Asn Tyr Val Phe Pro Ala His Lys Cys Ile Cys Tyr Phe Pro Cys

65 70 75 80

<210>745

<211>76

<212>PRT/Protein

<213>Cicer arietinum

<400>745

Met Ser Lys Phe Tyr Thr Val Phe Met Phe Leu Cys Leu Ala Leu Leu

1 5 10 15

Leu Ile Ser Ser Trp Glu Val Glu Ala Lys Leu Cys Gln Arg Arg Ser

20 25 30

Lys Thr Trp Ser Gly Pro Cys Ile Ile Thr Gly Asn Cys Lys Asn Gln

35 40 45

Cys Lys Asn Val Glu His Ala Thr Phe Gly Ala Cys His Arg Gln Gly

50 55 60

Phe Gly Phe Ala Cys Phe Cys Tyr Phe Asn Cys His

65 70 75

<210>746

<211>82

<212>PRT/Protein

<213>Citrus clementina

<400>746

Met Ala Lys Ser Val Ala Ser Ile Thr Thr Ala Phe Ala Leu Ile Phe

1 5 10 15

Ala Phe Phe Ile Leu Phe Ala Ser Phe Gly Val Pro Met Ala Glu Ala

20 25 30

Lys Val Cys Gln Arg Arg Ser Lys Thr Trp Ser Gly Pro Cys Leu Asn

35 40 45

Thr Gly Lys Cys Ser Arg Gln Cys Lys Gln Gln Glu Tyr Ala Arg Tyr

50 55 60

Gly Ala Cys Tyr Arg Gln Gly Ala Gly Tyr Ala Cys Tyr Cys Tyr Phe

65 70 75 80

Asn Cys

<210>747

<211>82

<212>PRT/Protein

<213>Citrus sinensis

<400>747

Met Ala Lys Ser Val Ala Ser Ile Thr Thr Ala Phe Ala Leu Ile Phe

1 5 10 15

Ala Phe Phe Ile Leu Phe Ala Ser Phe Glu Val Pro Met Ala Glu Ala

20 25 30

Lys Val Cys Gln Arg Arg Ser Lys Thr Trp Ser Gly Pro Cys Leu Asn

35 40 45

Thr Gly Lys Cys Ser Arg His Cys Lys Gln Gln Glu Asp Ala Arg Tyr

50 55 60

Gly Ala Cys Tyr Arg Gln Gly Thr Gly Tyr Ala Cys Phe Cys Tyr Phe

65 70 75 80

Glu Cys

<210>748

<211>78

<212>PRT/Protein

<213>Citrus sinensis

<400>748

Met Ala Lys Phe Thr Thr Thr Phe Ala Leu Leu Phe Ala Phe Phe Ile

1 5 10 15

Leu Phe Ala Ala Phe Asp Val Pro Met Ala Glu Ala Lys Val Cys Gln

20 25 30

Leu Arg Ser Lys Thr Trp Ser Gly Leu Cys Leu Asn Thr Gly Asn Cys

35 40 45

Ser Arg Gln Cys Lys Gln Gln Glu Asp Ala Arg Phe Gly Ala Cys His

50 55 60

Arg Gln Gly Ile Gly Phe Ala Cys Phe Cys Tyr Phe Lys Cys

65 70 75

<210>749

<211>76

<212>PRT/Protein

<213>Citrus sinensis

<400>749

Met Glu Arg Ser Val Arg Leu Phe Ser Thr Val Leu Leu Val Leu Leu

1 5 10 15

Leu Leu Ala Ser Glu Met Gly Leu Arg Ala Ala Glu Ala Arg Ile Cys

20 25 30

Glu Ser Gln Ser His Arg Phe Lys Gly Pro Cys Val Ser Lys Ser Asn

35 40 45

Cys Ala Ala Val Cys Gln Thr Glu Gly Phe His Gly Gly His Cys Arg

50 55 60

Gly Phe Arg Arg Arg Cys Phe Cys Thr Lys Arg Cys

65 70 75

<210>750

<211>106

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>750

Met Ser Thr Ala Thr Phe Val Asp Ile Ile Ile Ala Ile Leu Leu Pro

1 5 10 15

Pro Leu Gly Val Phe Leu Arg Phe Gly Cys Gly Val Glu Phe Trp Ile

20 25 30

Cys Leu Val Leu Thr Leu Leu Gly Tyr Ile Pro Gly Ile Ile Tyr Ala

35 40 45

Ile Tyr Val Leu Thr Lys Arg Thr Cys Glu Ser Gln Ser His Arg Phe

50 55 60

Lys Gly Pro Cys Ser Arg Asp Ser Asn Cys Ala Thr Val Cys Leu Thr

65 70 75 80

Glu Gly Phe Ser Gly Gly Asp Cys Arg Gly Phe Arg Arg Arg Cys Arg

85 90 95

Cys Thr Arg Pro Cys Val Phe Asp Glu Lys

100 105

<210>751

<211>28

<212>PRT/Protein

<213>Pseudomonas syringae

<400>751

Glu Ser Thr Asn Ile Leu Gln Arg Met Arg Glu Leu Ala Val Gln Ser

1 5 10 15

Arg Asn Asp Ser Asn Ser Ala Thr Asp Arg Glu Ala

20 25

<210>752

<211>15

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>752

Arg Ile Asn Ser Ala Lys Asp Asp Ala Ala Gly Leu Ala Ile Ala

1 5 10 15

<210>753

<211>22

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>753

Asp Arg Leu Ser Ser Gly Lys Arg Ile Asn Ser Ala Ser Asp Pro Ala

1 5 10 15

Ala Gly Leu Ala Ile Ala

twenty

<210>754

<211>8

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>754

Arg Ile Asn Ser Ala Ser Asp Asp

fifteen

<210>755

<211>8

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>755

Arg Ile Asn Asn Ala Ser Asp Asp

fifteen

<210>756

<211>8

<212>PRT/Protein

<213>Bacillus manliponensis

<400>756

Gln Ile Asn Ser Ala Ser Asp Asp

fifteen

<210>757

<211>8

<212>PRT/Protein

<213>Lysinibacillus sp.

<400>757

Arg Ile Asn Ser Ala Ala Asp Asp

fifteen

<210>758

<211>8

<212>PRT/Protein

<213>Paenibacillus sp.

<400>758

Arg Ile Asn Gly Ala Ser Asp Asp

fifteen

<210>759

<211>8

<212>PRT/Protein

<213>Aneurinibacillus sp.

<400>759

Arg Ile Asn Arg Ala Ser Asp Asp

fifteen

<210>760

<211>8

<212>PRT/Protein

<213>Escherichia coli

<400>760

Arg Ile Asn Ser Ala Lys Asp Asp

fifteen

<210>761

<211>8

<212>PRT/Protein

<213>Burkholderia ubonensis

<400>761

Arg Ile Asn Thr Ala Ala Asp Asp

fifteen

<210>762

<211>8

<212>PRT/Protein

<213>Pseudomonas syringae

<400>762

Lys Ile Asn Ser Ala Lys Asp Asp

fifteen

<210>763

<211>8

<212>PRT/Protein

<213>Lysinibacillus spp.

<400>763

Arg Ile Asn Arg Ala Gly Asp Asp

fifteen

<210>764

<211>8

<212>PRT/Protein

<213>Lysinibacillus spp.

<400>764

Lys Ile Asn Arg Ala Ser Asp Asp

fifteen

<210>765

<211>8

<212>PRT/Protein

<213>Lysinibacillus xylanilyticus

<400>765

Lys Ile Asn Arg Ala Gly Asp Asp

fifteen

<210>766

<211>8

<212>PRT/Protein

<213>Bacillus thuringiensis

<220>

<221>MISC_FEATURE/Other features

<222>(1)..(1)

<223>Xaa=Arg or Gln or Lys

<220>

<221>MISC_FEATURE/Other features

<222>(4)..(4)

<223>Xaa=Ser or Asn or Gly or Arg or Thr

<220>

<221>MISC_FEATURE/Other features

<222>(6)..(6)

<223>Xaa=Ser or Ala or Lys or Gly

<400>766

Xaa Ile Asn Xaa Ala Xaa Asp Asp

fifteen

<210>767

<211>15

<212>PRT/Protein

<213>Bacillus thuringiensis

<400>767

Ala Ile Ala Leu Gly Ala Ala Asp Asp Lys Ala Ser Asn Ile Arg

1 5 10 15

<210>768

<211>28

<212>PRT/Protein

<213>Pseudomonas syringae

<400>768

Ala Glu Arg Asp Thr Ala Ser Asn Ser Asp Asn Arg Ser Gln Val Ala

1 5 10 15

Leu Glu Arg Met Arg Gln Leu Ile Asn Thr Ser Glu

20 25

<210>769

<211>31

<212>PRT/Protein

<213>Bacillus amyloliquefaciens

<400>769

Met Ile Gln Lys Arg Lys Arg Thr Val Ser Phe Arg Leu Val Leu Met

1 5 10 15

Cys Thr Leu Leu Phe Val Ser Leu Pro Ile Thr Lys Thr Ser Ala

20 25 30

<210>770

<211>218

<212>PRT/Protein

<213>Schistosoma japonicum

<400>770

Met Ser Pro Ile Leu Gly Tyr Trp Lys Ile Lys Gly Leu Val Gln Pro

1 5 10 15

Thr Arg Leu Leu Leu Glu Tyr Leu Glu Glu Lys Tyr Glu Glu His Leu

20 25 30

Tyr Glu Arg Asp Glu Gly Asp Lys Trp Arg Asn Lys Lys Phe Glu Leu

35 40 45

Gly Leu Glu Phe Pro Asn Leu Pro Tyr Tyr Ile Asp Gly Asp Val Lys

50 55 60

Leu Thr Gln Ser Met Ala Ile Ile Arg Tyr Ile Ala Asp Lys His Asn

65 70 75 80

Met Leu Gly Gly Cys Pro Lys Glu Arg Ala Glu Ile Ser Met Leu Glu

85 90 95

Gly Ala Val Leu Asp Ile Arg Tyr Gly Val Ser Arg Ile Ala Tyr Ser

100 105 110

Lys Asp Phe Glu Thr Leu Lys Val Asp Phe Leu Ser Lys Leu Pro Glu

115 120 125

Met Leu Lys Met Phe Glu Asp Arg Leu Cys His Lys Thr Tyr Leu Asn

130 135 140

Gly Asp His Val Thr His Pro Asp Phe Met Leu Tyr Asp Ala Leu Asp

145 150 155 160

Val Val Leu Tyr Met Asp Pro Met Cys Leu Asp Ala Phe Pro Lys Leu

165 170 175

Val Cys Phe Lys Lys Arg Ile Glu Ala Ile Pro Gln Ile Asp Lys Tyr

180 185 190

Leu Lys Ser Ser Lys Tyr Ile Ala Trp Pro Leu Gln Gly Trp Gln Ala

195 200 205

Thr Phe Gly Gly Gly Asp His Pro Pro Lys

210 215

<210>771

<211>7

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>771

Gly Gly Gly Gly Gly Gly Ser

fifteen

<210>772

<211>5

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construction

<400>772

Asp Asp Asp Asp Lys

fifteen

<210>773

<211>20

<212>DNA

<213>Artificial sequence

<220>

<223>Synthetic construct (primer)

<400>773

tcgagcgcgt atgcaatacg 20

<210>774

<211>24

<212>DNA

<213>Artificial sequence

<220>

<223>Synthetic construct (primer)

<400>774

gcgttatccc gtagaaaaag gtag 24

<210>775

<211>18

<212>PRT/Protein

<213>Artificial sequence

<220>

<223>Synthetic construct (primer)

<400>775

Ala Gly Ala Cys Gly Gly Phe Thr Gly Ala Gly Thr Ala Ala Cys Gly

1 5 10 15

Cys Gly

<---

Claims (72)

1. A polypeptide for bioactive priming of a plant or plant part, wherein said bioactive priming includes improving growth, yield, health, increasing longevity, productivity and/or vitality of a plant or plant part, and/or reducing abiotic stress in said plant, or parts of said plant, and/or protection of said plant or part of said plant from disease, insects and/or nematodes, and/or enhancement of innate immune response of said plant or part of said plant, and/or alteration of plant architecture, wherein said polypeptide comprises: partial coding sequence of flagellin or flagellin-associated polypeptide, and the amino acid sequence of said flagellin or flagellin-associated polypeptide contains X ¹ -INX ² -AX ³ -DD (SEQ ID NO: 766), where: X ¹ is arginine (R), glutamine (Q) or lysine (K); X ² is serine (S), asparagine (N), glycine (G), arginine (R) or threonine (T); and X ³ is alanine (A) and the amino acid sequence of flagellin or flagellin-associated peptide contains SEQ ID NO: 291, 292, 295-298, 538, 582, 583, or 761, lysine (K) and the amino acid sequence of flagellin or flagellin- the associated peptide contains SEQ ID NO: 571 or 752, or X3 is serine (S) or glycine (G). 2. The polypeptide according to claim 1, characterized in that said flagellin or flagellin-associated polypeptide contains a chemical modification or is a variant characterized by an amino acid substitution in the amino acid sequence, where said amino acid substitution in the amino acid sequence of the specified variant includes a substitution with a β-amino acid, a D-amino acid or a non-naturally occurring amino acid; either is part of a fusion protein; or contains a protease recognition sequence. 3. The polypeptide according to claim 2, characterized in that said chemical modification includes acetylation, addition of acid, acylation, ADP-ribosylation, addition of aldehyde, addition of alkylamide, amidation, amination, biotinylation, addition of carbamate, addition of chloromethyl ketone, covalent addition of a nucleotide or nucleotide derivative, cross-linking, cyclization, formation of disulfide bonds, demethylation , ester addition, covalent crosslinking, cysteine-cysteine disulfide formation, pyroglutamate formation, formylation, gamma-carboxylation, glycosylation, GPI-anchor formation, hydrazide addition, hydroxamic acid addition, hydroxylation, iodination, lipid addition, methylation, myristiolation , oxidation, pegylation, proteolytic processing, phosphorylation, prenylation, palmitoylation, labeling for purification, pyroglutamyl addition, racemization, selenoylation, sulfonamide addition a, sulfation, transfer RNA mediated addition of amino acids to proteins, ubiquitination, addition of urea, or N-terminal modification, or C-terminal modification; or an amino acid substitution in the amino acid sequence of said variant includes a substitution with a β-amino acid, a D-amino acid, or a non-naturally occurring amino acid. 4. A polypeptide according to claim 3, characterized in that said chemical modification includes acetylation, amidation, cross-linking or cyclization. 5. A polypeptide according to claim 1, characterized in that: the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any one of SEQ ID NOs: 754-756, 758, 759 and 761-765. 6. The polypeptide according to claim. 1, characterized in that said flagellin or flagellin-associated polypeptide contains an auxiliary polypeptide. 7. A polypeptide according to claim 6, characterized in that said auxiliary polypeptide contains: a signature polypeptide, wherein the amino acid sequence of said signature polypeptide contains any of SEQ ID NOs: 542-548 or any combination thereof; or a signal anchor sort polypeptide, and the amino acid sequence of said signal anchor sort polypeptide comprises any of SEQ ID NOs: 549-562 or any combination thereof; or signature polypeptide, and the amino acid sequence of the specified signature polypeptide contains SEQ ID NO: 542; or a signal anchor sorting polypeptide, wherein the amino acid sequence of said signal anchor sorting polypeptide comprises SEQ ID NO: 549. 8. The polypeptide according to any one of paragraphs. 1-7, characterized in that said polypeptide contains an amino acid sequence according to any of SEQ ID NOs: 226-229, 232, 289-290, 571-581, 585, 752, 754-756, 758, 759 and 761-765. 9. The polypeptide according to any one of paragraphs. 1-8, characterized in that said polypeptide is isolated, concentrated from a fermentation product and/or partially purified, optionally by filtration, chromatography, or from a recombinant microorganism. 10. The polypeptide according to any one of paragraphs. 1-9, characterized in that said polypeptide contains flagellin or flagellin-associated polypeptide and: (i) flagellin or flagellin-associated polypeptide is chemically modified at the N- or C-terminus; or (ii) said flagellin or flagellin-associated polypeptide is modified by crosslinking or cyclization; or (iii) said flagellin or flagellin-associated polypeptide is from a bacterium of the genus Bacillus, Lysinibacillus, Paenibacillus, Aneurinibacillus, or any combination thereof. 11. A recombinant microorganism that expresses or overexpresses a polypeptide, said polypeptide comprising a polypeptide according to any one of paragraphs. 1, 5-9 or any combination thereof. 12. A recombinant microorganism according to claim 11, characterized in that said microorganism overexpresses said polypeptide and said polypeptide is obtained with a secretion signal. 13. Composition for bioactive priming of a plant or plant part, wherein said bioactive priming includes improving growth, yield, health, increasing lifespan, productivity and/or vitality of a plant or plant part, and/or reducing abiotic stress in said plant or parts of said plant, and/or protection of said plant or part of said plant from disease, insects and/or nematodes, and/or enhancement of the innate immune response of said plant or part of said plant, and/or alteration of plant architecture, wherein said composition contains something either from the following: an effective amount of a polypeptide according to any one of paragraphs. 1-10 or any combination of the indicated peptides and an agrochemical or carrier; or an effective amount of any combination of polypeptides according to any one of paragraphs. 1–10. 14. The composition of claim 13, further comprising an agrochemical or carrier that is naturally associated with said polypeptide. 15. The composition according to any one of paragraphs. 13 and 14, characterized in that said agrochemical contains an antibiotic, a biopesticide, a preservative, a buffering agent, a wetting agent, a surfactant, a coating agent, a monosaccharide, a polysaccharide, an abrasive agent, a pesticide, an insecticide, a herbicide, a nematocide, a bacteriocide, a fungicide , miticide, fertilizer, biostimulant, osmoprotectant, coloring agent, humectant, amino acid, biological control agent, hydrochloric acid, acetic acid and/or trifluoroacetic acid, or a combination thereof. 16. The composition according to any one of paragraphs. 13-15, characterized in that said composition contains: from about 0.00001 wt.% to about 95 wt.% of the specified polypeptide or polypeptides, from about 0.01% to about 80 wt.% of the specified agrochemical and from about 5 wt.% to about 50 wt.% of the carrier based on the total weight compositions; or from about 0.01 wt.% to about 5 wt.% of these polypeptides, from about 0.2% to about 70 wt.% of the specified agrochemical and from about 10 wt.% to about 30 wt.% carrier based on the total weight of the composition; or from about 0.05 wt.% to about 1 wt.% of these polypeptides, from about 30 wt.% to about 60 wt.% of the specified agrochemical and from about 40 wt.% to about 69 wt.% of the carrier based on the total weight of the composition. 17. Composition according to claim 16, characterized in that said agrochemical contains: hydrochloric acid, acetic acid and/or trifluoroacetic acid; or from about 0.001 wt.% to about 30 wt.%, from about 0.01 wt.% to about 20 wt.% or from 0.1 wt.% to about 5 wt.% hydrochloric acid, acetic acid and/or triperoxonane acid from the total weight of the specified composition. 18. The use of a polypeptide according to any one of paragraphs. 1-10, or any combination thereof, to coat a seed, wherein said coating is intended to improve growth, yield, health, increase longevity, productivity, and/or vitality of a plant or plant part, and/or reduce abiotic stress in said plant, or part of said plant, and/or protecting said plant or part of said plant from disease, insects and/or nematodes, and/or enhancing the innate immune response of said plant or part of said plant, and/or altering plant architecture. 19. The use of a composition according to any one of paragraphs. 13-17 for seed coating, wherein said coating is intended to improve growth, yield, health, increase longevity, productivity and/or vitality of a plant or plant part, and/or reduce abiotic stress in said plant or part of said plant, and/or protecting said plant or part of said plant from disease, insects and/or nematodes, and/or enhancing the innate immune response of said plant or part of said plant, and/or altering plant architecture. 20. The use of a recombinant microorganism according to paragraphs. 11 or 12 for seed coating, wherein said coating is intended to improve growth, yield, health, increase longevity, productivity and/or vitality of a plant or plant part, and/or reduce abiotic stress in said plant or part of said plant, and/or protecting said plant or part of said plant from disease, insects and/or nematodes, and/or enhancing the innate immune response of said plant or part of said plant, and/or altering plant architecture. 21. A method of bioactive priming of a plant or plant part, wherein said bioactive priming includes improving growth, yield, health, increasing lifespan, productivity and/or vitality of a plant or plant part, and/or reducing abiotic stress in said plant or part said plant, and/or protecting said plant or part of said plant from disease, insects and/or nematodes, and/or enhancing the innate immune response of said plant or part of said plant, and/or altering plant architecture, wherein said method includes: either from the following: (a) the use of a polypeptide according to any one of paragraphs. 1-10 or compositions according to any one of paragraphs. 13-17 on a plant, on a plant part, or in a plant growth medium, or in the rhizosphere in an area surrounding said plant or part of said plant, to improve growth, yield, health, longevity, productivity, and/or vitality said plant or part of said plant, and/or reduction of abiotic stress in said plant or part of said plant; and/or protecting said plant or part of said plant from disease, insects and/or nematodes, and/or enhancing the innate immune response of said plant or part of said plant, and/or altering plant architecture; or (b) the use of a recombinant microorganism according to any one of paragraphs. 11 or 12 on a plant, on a plant part, or in a plant growth medium, or in the rhizosphere in an area surrounding said plant or part of said plant, to improve growth, yield, health, longevity, productivity, and/or vitality said plant or part of said plant, and/or reduction of abiotic stress in said plant or part of said plant; and/or protecting said plant or part of said plant from disease, insects and/or nematodes, and/or enhancing the innate immune response of said plant or part of said plant, and/or altering the architecture of said plant, wherein said recombinant microorganism expresses a polypeptide, and the expression of the polypeptide is increased compared to the expression level of said polypeptide in a wild-type microorganism of the same species under the same conditions. 22. The method of claim 21, wherein said disease comprises Asian citrus greening, Huanglong disease (HLB), Asian soybean rust, Sclerotinia stem rot (or white mold), Pseudomonas leaf spot, or leaf spot. 23. The method according to p. 21 or 22, characterized in that the specified disease includes: (i) Asian soybean rust, leaf rot or Sclerotinia stem rot (or white mold), wherein said polypeptide or composition comprises flagellin or a flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 752 and 571; or (ii) Asian citrus green, wherein said composition comprises a bactericide and a flagellin or flagellin-associated polypeptide, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 571, and 752, or any combination thereof; or (iii) a bacterial disease, said method comprising limiting the growth of said bacteria and/or preventing said disease, wherein the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises any of SEQ ID NOs: 226, 752 and 571 or any combination thereof. 24. The method according to claim 23, characterized in that: said method is the method of (i), and the amino acid sequence of said flagellin or flagellin-associated polypeptide comprises SEQ ID NO: 226, and said composition optionally contains a fungicide, or said method is the method of (iii) and said bacteria include Pseudomanas syringae and the plant optionally includes kiwifruit; or said method is the method of (ii), and said bactericide comprises oxytetracycline. 25. The method according to any one of paragraphs. 21-24, characterized in that the protection of the specified plant or part of the specified plant from the disease includes prophylactic treatment, treatment, prevention and reduction of the progression of the disease on the plant, or on the plant part, or in the plant, or in the plant part. 26. The method according to any one of paragraphs. 21-25, characterized in that said polypeptide, said composition, or said recombinant microorganism is used exogenously on said plant, on a part of said plant, or in a growth medium for said plant, or is used endogenously in said plant or part of said plant. 27. The method according to any one of paragraphs. 21-26, characterized in that said plant part contains a cell, leaf, branch, stem, flower, foliage, floral organ, fruit, pollen, vegetable, tuber, branch, bulb, pseudobulb, pod, root, root ball, rootstock, graft, or seed; and/or said polypeptide, said composition, or said recombinant microorganism is applied to the surface of said plant, the foliage of said plant, or the seed surface of said plant; and/or said polypeptide, said composition, or said recombinant microorganism is applied to the seed surface of said plant, and said plant or said plant part is grown from said seed; and/or said polypeptide, said composition, or said recombinant microorganism is used as a foliar application agent; and/or said plant is a fruit plant or a vegetable plant, and said method provides increased yield of fruits or vegetables. 28. The method of obtaining a fusion protein in bacterial culture, where the specified fusion protein contains a polypeptide according to any one of paragraphs. 1-10 and an enterokinase (EK) cleavage site, wherein said enterokinase cleavage site enhances the activity and stability of said polypeptide, wherein said method comprises secreting said fusion protein into said bacterial culture. 29. The method according to claim 28, characterized in that: said fusion protein further comprises a protein tag; or said fusion protein further comprises a protein tag, and said protein tag contains glutathione-S-transferase (GST); or said fusion protein further comprises a protein tag and a secretion signal; or said fusion protein further comprises a protein tag and a secretion signal, and said protein tag contains glutathione-S-transferase (GST); or said fusion protein further comprises a protein tag and a secretion signal, and said secretion signal comprises an amino acid sequence comprising any of SEQ ID NOs: 563-570 or 769, or any combination thereof; or said fusion protein further comprises a protein tag and a secretion signal, and said protein tag contains glutathione-S-transferase (GST), and said secretion signal contains an amino acid sequence comprising any of SEQ ID NOs: 563-570 or 769, or any combination thereof. 30. The method of claim 28 or 29, wherein said method further comprises subjecting the resulting fusion protein to an enterokinase to cleave the cleavage site with the enterokinase and isolate said polypeptide. 31. The method according to any one of paragraphs. 28-30, characterized in that said enterokinase cleavage site contains SEQ ID NO: 772.

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