BIK1_ARATH
ID BIK1_ARATH Reviewed; 395 AA.
AC O48814;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase BIK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:24104392};
DE AltName: Full=Protein BOTRYTIS-INDUCED KINASE 1 {ECO:0000303|PubMed:16339855};
GN Name=BIK1 {ECO:0000303|PubMed:16339855};
GN OrderedLocusNames=At2g39660 {ECO:0000312|Araport:AT2G39660};
GN ORFNames=F12L6.32 {ECO:0000312|EMBL:AAM14921.1},
GN F17A14.3 {ECO:0000312|EMBL:AAB97121.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16339855; DOI=10.1105/tpc.105.035576;
RA Veronese P., Nakagami H., Bluhm B., Abuqamar S., Chen X., Salmeron J.,
RA Dietrich R.A., Hirt H., Mengiste T.;
RT "The membrane-anchored BOTRYTIS-INDUCED KINASE1 plays distinct roles in
RT Arabidopsis resistance to necrotrophic and biotrophic pathogens.";
RL Plant Cell 18:257-273(2006).
RN [5]
RP FUNCTION, INTERACTION WITH FLS2, PHOSPHORYLATION AT SER-236, INDUCTION BY
RP FLAGELLIN, AND DISRUPTION PHENOTYPE.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
RN [6]
RP FUNCTION, INTERACTION WITH FLS2 AND BAK1, AUTOPHOSPHORYLATION, AND
RP PHOSPHORYLATION AT THR-237.
RX PubMed=20404519; DOI=10.4161/psb.11500;
RA Lu D., Wu S., He P., Shan L.;
RT "Phosphorylation of receptor-like cytoplasmic kinases by bacterial
RT flagellin.";
RL Plant Signal. Behav. 5:598-600(2010).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH XANTHOMONAS
RP CAMPESTRIS XOPAC/AVRAC, PHOSPHORYLATION, AND URIDYLYLATION AT SER-236 AND
RP THR-237.
RX PubMed=22504181; DOI=10.1038/nature10962;
RA Feng F., Yang F., Rong W., Wu X., Zhang J., Chen S., He C., Zhou J.M.;
RT "A Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune
RT kinases.";
RL Nature 485:114-118(2012).
RN [8]
RP FUNCTION, INTERACTION WITH PEPR1, PHOSPHORYLATION AT SER-233; SER-236 AND
RP THR-237, AND MUTAGENESIS OF LYS-105.
RX PubMed=23431184; DOI=10.1073/pnas.1215543110;
RA Liu Z., Wu Y., Yang F., Zhang Y., Chen S., Xie Q., Tian X., Zhou J.M.;
RT "BIK1 interacts with PEPRs to mediate ethylene-induced immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6205-6210(2013).
RN [9]
RP FUNCTION, INTERACTION WITH BRI1, AND DISRUPTION PHENOTYPE.
RX PubMed=23818580; DOI=10.1073/pnas.1302154110;
RA Lin W., Lu D., Gao X., Jiang S., Ma X., Wang Z., Mengiste T., He P.,
RA Shan L.;
RT "Inverse modulation of plant immune and brassinosteroid signaling pathways
RT by the receptor-like cytoplasmic kinase BIK1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:12114-12119(2013).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-48; SER-54; THR-56;
RP SER-71; SER-129; TYR-168; SER-206; TYR-214; SER-233; SER-236; THR-237;
RP THR-242; TYR-250; SER-252; SER-253; THR-314; SER-360; THR-362 AND THR-368,
RP AND MUTAGENESIS OF ASP-202.
RX PubMed=24104392; DOI=10.1007/s13238-013-3053-6;
RA Xu J., Wei X., Yan L., Liu D., Ma Y., Guo Y., Peng C., Zhou H., Yang C.,
RA Lou Z., Shui W.;
RT "Identification and functional analysis of phosphorylation residues of the
RT Arabidopsis BOTRYTIS-INDUCED KINASE1.";
RL Protein Cell 4:771-781(2013).
RN [11]
RP FUNCTION, MUTAGENESIS OF GLY-2, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=25522736; DOI=10.1186/s12870-014-0374-4;
RA Ranf S., Eschen-Lippold L., Froehlich K., Westphal L., Scheel D., Lee J.;
RT "Microbe-associated molecular pattern-induced calcium signaling requires
RT the receptor-like cytoplasmic kinases, PBL1 and BIK1.";
RL BMC Plant Biol. 14:374-374(2014).
RN [12]
RP FUNCTION, AND INTERACTION WITH RBOHD.
RX PubMed=24629339; DOI=10.1016/j.chom.2014.02.009;
RA Li L., Li M., Yu L., Zhou Z., Liang X., Liu Z., Cai G., Gao L., Zhang X.,
RA Wang Y., Chen S., Zhou J.M.;
RT "The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase
RT RbohD to control plant immunity.";
RL Cell Host Microbe 15:329-338(2014).
RN [13]
RP INTERACTION WITH CPK28.
RX PubMed=25525792; DOI=10.1016/j.chom.2014.10.007;
RA Monaghan J., Matschi S., Shorinola O., Rovenich H., Matei A., Segonzac C.,
RA Malinovsky F.G., Rathjen J.P., MacLean D., Romeis T., Zipfel C.;
RT "The calcium-dependent protein kinase CPK28 buffers plant immunity and
RT regulates BIK1 turnover.";
RL Cell Host Microbe 16:605-615(2014).
RN [14]
RP PHOSPHORYLATION AT TYR-150; TYR-243 AND TYR-250, AND MUTAGENESIS OF
RP TYR-150; TYR-243 AND TYR-250.
RX PubMed=24532660; DOI=10.1073/pnas.1318817111;
RA Lin W., Li B., Lu D., Chen S., Zhu N., He P., Shan L.;
RT "Tyrosine phosphorylation of protein kinase complex BAK1/BIK1 mediates
RT Arabidopsis innate immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3632-3637(2014).
RN [15]
RP FUNCTION (MICROBIAL INFECTION).
RC STRAIN=cv. Columbia;
RX PubMed=26355215; DOI=10.1016/j.chom.2015.08.004;
RA Wang G., Roux B., Feng F., Guy E., Li L., Li N., Zhang X., Lautier M.,
RA Jardinaud M.-F., Chabannes M., Arlat M., Chen S., He C., Noel L.D.,
RA Zhou J.-M.;
RT "The decoy substrate of a pathogen effector and a pseudokinase specify
RT pathogen-induced modified-self recognition and immunity in plants.";
RL Cell Host Microbe 18:285-295(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-2,
RP AND MYRISTOYLATION AT GLY-2.
RX PubMed=26021844; DOI=10.1007/s00299-015-1812-y;
RA Kang G.H., Son S., Cho Y.H., Yoo S.D.;
RT "Regulatory role of BOTRYTIS INDUCED KINASE1 in ETHYLENE INSENSITIVE3-
RT dependent gene expression in Arabidopsis.";
RL Plant Cell Rep. 34:1605-1614(2015).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=27679580; DOI=10.3389/fphys.2016.00402;
RA Chen T., Bi K., He Z., Gao Z., Zhao Y., Fu Y., Cheng J., Xie J., Jiang D.;
RT "Arabidopsis mutant bik1 exhibits strong resistance to Plasmodiophora
RT brassicae.";
RL Front. Physiol. 7:402-402(2016).
RN [18]
RP ACTIVITY REGULATION, AND INTERACTION WITH PP2C38.
RX PubMed=27494702; DOI=10.1371/journal.ppat.1005811;
RA Couto D., Niebergall R., Liang X., Buecherl C.A., Sklenar J., Macho A.P.,
RA Ntoukakis V., Derbyshire P., Altenbach D., Maclean D., Robatzek S.,
RA Uhrig J., Menke F., Zhou J.M., Zipfel C.;
RT "The Arabidopsis protein phosphatase PP2C38 negatively regulates the
RT central immune kinase BIK1.";
RL PLoS Pathog. 12:E1005811-E1005811(2016).
RN [19]
RP FUNCTION, MUTAGENESIS OF LYS-105 AND LYS-106, INTERACTION WITH SIK1, PTM,
RP AND PHOSPHORYLATION AT SER-26; SER-32; SER-33; SER-34; THR-35; THR-42;
RP THR-50; SER-54; THR-56; THR-64; SER-71; THR-120; TYR-168; SER-193; SER-206;
RP SER-219; SER-233; SER-236; THR-314; THR-341; SER-360; THR-362; THR-368;
RP THR-375 AND THR-377.
RC STRAIN=cv. Columbia;
RX PubMed=30212650; DOI=10.1016/j.chom.2018.08.007;
RA Zhang M., Chiang Y.-H., Toruno T.Y., Lee D., Ma M., Liang X., Lal N.K.,
RA Lemos M., Lu Y.-J., Ma S., Liu J., Day B., Dinesh-Kumar S.P., Dehesh K.,
RA Dou D., Zhou J.-M., Coaker G.;
RT "The MAP4 Kinase SIK1 Ensures Robust Extracellular ROS Burst and
RT Antibacterial Immunity in Plants.";
RL Cell Host Microbe 24:379.e5-391.e5(2018).
RN [20]
RP FUNCTION, UBIQUITINATION AT LYS-31; LYS-41; LYS-95; LYS-170; LYS-186;
RP LYS-286; LYS-337; LYS-358 AND LYS-366, MUTAGENESIS OF GLY-2; LYS-31;
RP LYS-41; LYS-95; LYS-106; LYS-170; LYS-186; LYS-204; THR-237; TYR-250;
RP LYS-286; LYS-337; LYS-358 AND LYS-366, UBIQUITINATION, PHOSPHORYLATION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FLS2; ATL44/RHA3A AND
RP ATL45/RHA3B.
RX DOI=10.1038/s41586-020-2210-3;
RA Xiyu M., Lucas A.N.C., Michelle E.L., Kai T., Zhiping W., Jun L., Xiao Y.,
RA Bo L., Jinggeng Z., Daniel V.S., Junmin P., Brett M.T., Antje H.,
RA Eugenia R., Ping H., Libo S.;
RT "Ligand-induced monoubiquitination of BIK1 regulates plant immunity.";
RL Nature 0:0-0(2020).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), SUBCELLULAR LOCATION, FUNCTION,
RP MUTAGENESIS OF 89-SER-THR-90; THR-120 AND SER-129, SUBUNIT, INTERACTION
RP WITH EFR, AND PHOSPHORYLATION AT SER-89; THR-90; THR-120 AND SER-129.
RC STRAIN=cv. Columbia;
RX PubMed=29649442; DOI=10.1016/j.chom.2018.03.010;
RA Lal N.K., Nagalakshmi U., Hurlburt N.K., Flores R., Bak A., Sone P., Ma X.,
RA Song G., Walley J., Shan L., He P., Casteel C., Fisher A.J.,
RA Dinesh-Kumar S.P.;
RT "The receptor-like cytoplasmic kinase BIK1 localizes to the nucleus and
RT regulates defense hormone expression during plant innate immunity.";
RL Cell Host Microbe 23:485-497.e5(2018).
CC -!- FUNCTION: Plays a central role in immune responses (PubMed:20413097,
CC PubMed:29649442). Required to activate the resistance responses to
CC necrotrophic pathogens, including the regulation of defense hormone
CC expression (e.g. jasmonic acid (JA) and salicylic acid (SA))
CC (PubMed:16339855, PubMed:29649442). Phosphorylates FLS2 and BAK1
CC (PubMed:20404519, PubMed:24104392). Involved in pathogen-associated
CC molecular pattern (PAMP)-triggered immunity (PTI) signaling, including
CC calcium signaling, and defense responses downstream of FLS2; upon PAMP
CC recognition, first phosphorylated by FLS2 and SIK1 prior to being
CC monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B at the plasma
CC membrane, then internalized dynamically into endocytic compartments
CC together with FLS2 (PubMed:20413097, PubMed:25522736, Ref.20,
CC PubMed:30212650). Acts additively with PBL1 in PTI defenses
CC (PubMed:20413097). Acts as positive regulator of the PAMP flg22-induced
CC increase of cytosolic calcium. Binds directly and phosphorylates the
CC NADPH oxidase RBOHD at specific sites in a calcium-independent manner
CC to enhance reactive oxygen species (ROS) generation upon flg22
CC perception. ROS production in response to flg22 controls stomatal
CC movement and restriction of bacterial entry into leaf tissues
CC (PubMed:24629339). Seems not required for flg22-induced MAPK activation
CC (Probable). Required for Pep1-induced defenses. Pep1 is an endogenous
CC elicitor that potentiates PAMP-inducible plant responses. In
CC association with PEPR1, acts downstream of the canonical ethylene
CC signaling cascade to regulate ethylene responses (PubMed:23431184).
CC Involved in ethylene signaling. Destabilizes EIN3, the key
CC transcription activator in ethylene signaling, and represses EIN3-
CC dependent transcription (PubMed:26021844). Acts as a negative regulator
CC in brassinosteroid (BR) signaling. Functions in BR signaling by direct
CC interaction with the BR receptor BRI1 cytosolic kinase domain
CC (PubMed:23818580). {ECO:0000269|PubMed:16339855,
CC ECO:0000269|PubMed:20404519, ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:23818580,
CC ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:24629339,
CC ECO:0000269|PubMed:25522736, ECO:0000269|PubMed:26021844,
CC ECO:0000269|PubMed:29649442, ECO:0000269|PubMed:30212650,
CC ECO:0000269|Ref.20, ECO:0000305, ECO:0000305|PubMed:22504181}.
CC -!- FUNCTION: (Microbial infection) Xanthomonas campestris effector
CC AvrAC/XopAC-mediated uridylylation prevents activation by
CC phosphorylation at the same residues, thus affecting immune responses
CC and reducing defense responses toward X.campestris, mediating
CC avrAC/XopAC virulence functions. {ECO:0000269|PubMed:26355215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:24104392};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:24104392};
CC -!- ACTIVITY REGULATION: Kinase activation is repressed by the phosphatase
CC PP2C38. {ECO:0000269|PubMed:27494702}.
CC -!- SUBUNIT: Interacts with FLS2 (PubMed:20413097, PubMed:20404519).
CC Activation of FLS2 by flagellin (flg22) induces the dissociation of the
CC complex (PubMed:20413097, Ref.20). Interacts with BAK1
CC (PubMed:20404519). Interacts with the Xanthomonas campestris effector
CC XopAC/AvrAC (PubMed:22504181). Interacts with CPK28 (PubMed:25525792).
CC Interacts with PEPR1 (PubMed:23431184). Interacts with PP2C38
CC (PubMed:27494702). Interacts with BRI1 (PubMed:23818580). Interacts
CC with RBOHD (PubMed:24629339). Binds to EFR when not phosphorylated at
CC Ser-89 and Thr-90, in the absence of pathogen elicitor; dissociates
CC upon pathogen-associated molecular pattern (PAMP)-triggered activation
CC by EFR-mediated phosphorylation (PubMed:29649442). Interacts directly
CC with and phosphorylates WRKY transcription factors in the nucleus
CC involved in the jasmonic acid (JA) and salicylic acid (SA) regulation
CC (e.g. WRKY33, WRKY50, WRKY51 and WRKY57) to modulate defense hormones
CC during plant immunity (PubMed:29649442). Binds to ATL44/RHA3A and
CC ATL45/RHA3B (Ref.20). Binds to SIK1 to be phosphorylated and stabilized
CC (PubMed:30212650). {ECO:0000269|PubMed:20404519,
CC ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:22504181,
CC ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:23818580,
CC ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:25525792,
CC ECO:0000269|PubMed:27494702, ECO:0000269|PubMed:29649442,
CC ECO:0000269|PubMed:30212650, ECO:0000269|Ref.20}.
CC -!- INTERACTION:
CC O48814; Q94F62: BAK1; NbExp=5; IntAct=EBI-1238176, EBI-617138;
CC O48814; Q9FL28: FLS2; NbExp=5; IntAct=EBI-1238176, EBI-1799448;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16339855,
CC ECO:0000269|PubMed:26021844, ECO:0000269|PubMed:29649442,
CC ECO:0000269|Ref.20}; Lipid-anchor {ECO:0000269|PubMed:16339855,
CC ECO:0000269|PubMed:26021844}. Endosome membrane {ECO:0000269|Ref.20};
CC Lipid-anchor {ECO:0000269|PubMed:16339855,
CC ECO:0000269|PubMed:26021844}. Nucleus {ECO:0000269|PubMed:29649442}.
CC Note=Linked to the plasma membrane when inactivated, but moves to the
CC nucleus upon pathogen-mediated activation by phosphorylation
CC (PubMed:29649442). Internalized dynamically into endocytic compartments
CC upon the recognition of microbe-associated molecular patterns (MAMPs,
CC e.g. flg22), when monoubiquitinated after phosphorylation and
CC subsequent dissociation of the FLS2/BIK1 complex (Ref.20).
CC {ECO:0000269|PubMed:29649442, ECO:0000269|Ref.20}.
CC -!- INDUCTION: By infection with necrotrophic pathogens and by paraquat.
CC Not induced by salicylic acid, jasmonate or 1-aminocyclopropane-1-
CC carboxylate (ACC) (PubMed:16339855). Induced by flagellin (flg22)
CC (PubMed:20413097). {ECO:0000269|PubMed:16339855,
CC ECO:0000269|PubMed:20413097}.
CC -!- PTM: Phosphorylated by SIK1 to be stabilized (PubMed:30212650).
CC Phosphorylated by FLS2 and BAK1 (PubMed:20404519, Ref.20).
CC Autophosphorylated (PubMed:22504181, PubMed:23431184, PubMed:24104392,
CC PubMed:26021844). Autophosphorylation is reduced in presence of the
CC Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181, Ref.20).
CC Phosphorylated, especially by EFR at Ser-89 and Thr-90, in response to
CC the microbe-associated molecular pattern (MAMP) flg22 (PubMed:20413097,
CC PubMed:22504181, PubMed:25522736, PubMed:29649442, Ref.20).
CC Phosphorylation in response to flg22 is abolished in presence of the
CC Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181).
CC Phosphorylated at Ser-233, Ser-236 and THR-237 by PEPR1
CC (PubMed:23431184). Phosphorylated at Tyr-150, Tyr-243 and Tyr-250.
CC Tyrosine phosphorylation is required for BIK1 function in plant innate
CC immunity (PubMed:24532660). {ECO:0000269|PubMed:20404519,
CC ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:22504181,
CC ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392,
CC ECO:0000269|PubMed:24532660, ECO:0000269|PubMed:25522736,
CC ECO:0000269|PubMed:26021844, ECO:0000269|PubMed:29649442,
CC ECO:0000269|PubMed:30212650, ECO:0000269|Ref.20}.
CC -!- PTM: Uridylylated at Ser-236 and Thr-237 by the Xanthomonas campestris
CC effector XopAC/AvrAC. This conceals conserved phosphorylation sites in
CC the activation loop, reducing BIK1 kinase activity and consequently
CC inhibiting downstream signaling. {ECO:0000269|PubMed:22504181}.
CC -!- PTM: Monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B following
CC phosphorylation upon the recognition of microbe-associated molecular
CC patterns (MAMPs, e.g. flg22) by pattern recognition receptors (PRRs),
CC then released from the FLS2/BAK1 complex and internalized dynamically
CC into endocytic compartments followed by the activation of immune
CC signaling. {ECO:0000269|Ref.20}.
CC -!- DISRUPTION PHENOTYPE: Altered growth traits, early flowering, weak
CC stems, small siliques and reduced fertility. Mutant plants have a
CC severely impaired resistance to Botrytis and A.brassicicola
CC (PubMed:16339855). Reduced plant size (PubMed:20413097,
CC PubMed:27679580). Enhanced resistance to Plasmodiophora brassicae, a
CC soil-borne obligate pathogen that causes clubroot disease
CC (PubMed:27679580). Hypersensitivity to the plant hormone brassinolide
CC (PubMed:23818580). Reduced calcium levels after elicitation with
CC peptides representing bacteria-derived microbe- and damage-associated
CC molecular patterns (MAMPs, flg22 and elf18, and the endogenous DAMP
CC AtPep1) (PubMed:25522736). {ECO:0000269|PubMed:16339855,
CC ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:23818580,
CC ECO:0000269|PubMed:25522736, ECO:0000269|PubMed:27679580}.
CC -!- MISCELLANEOUS: The association with FLS2 and BAK1 is reduced after
CC flagellin perception, BIK1 being probably released from the receptor
CC complex upon phosphorylation.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC003674; AAB97121.1; -; Genomic_DNA.
DR EMBL; AC004218; AAM14921.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09703.1; -; Genomic_DNA.
DR EMBL; AF325086; AAK17154.1; -; mRNA.
DR EMBL; AY062493; AAL32571.1; -; mRNA.
DR EMBL; AY065029; AAL57667.1; -; mRNA.
DR EMBL; AY093278; AAM13277.1; -; mRNA.
DR EMBL; AY093997; AAM16258.1; -; mRNA.
DR PIR; T00574; T00574.
DR RefSeq; NP_181496.1; NM_129522.5.
DR PDB; 5TOS; X-ray; 2.35 A; A/B=1-395.
DR PDBsum; 5TOS; -.
DR AlphaFoldDB; O48814; -.
DR SMR; O48814; -.
DR BioGRID; 3887; 7.
DR DIP; DIP-51510N; -.
DR IntAct; O48814; 4.
DR STRING; 3702.AT2G39660.1; -.
DR iPTMnet; O48814; -.
DR PaxDb; O48814; -.
DR PRIDE; O48814; -.
DR ProteomicsDB; 240422; -.
DR EnsemblPlants; AT2G39660.1; AT2G39660.1; AT2G39660.
DR GeneID; 818549; -.
DR Gramene; AT2G39660.1; AT2G39660.1; AT2G39660.
DR KEGG; ath:AT2G39660; -.
DR Araport; AT2G39660; -.
DR TAIR; locus:2039772; AT2G39660.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; O48814; -.
DR OMA; HIMDQRI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O48814; -.
DR PRO; PR:O48814; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48814; baseline and differential.
DR Genevisible; O48814; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0080141; P:regulation of jasmonic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0080142; P:regulation of salicylic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IGI:TAIR.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Endosome; Immunity;
KW Innate immunity; Isopeptide bond; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:26021844"
FT CHAIN 2..395
FT /note="Serine/threonine-protein kinase BIK1"
FT /id="PRO_0000311118"
FT DOMAIN 67..356
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 354..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 89..90
FT /note="Required for physical interaction with and
FT phosphorylation of downstream signaling proteins (e.g.
FT WRKY33, WRKY50, WRKY51 and WRKY57) to activate EFR-mediated
FT immune signaling"
FT /evidence="ECO:0000269|PubMed:29649442"
FT COMPBIAS 354..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 48
FT /note="Phosphoserine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 54
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 56
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 71
FT /note="Phosphoserine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 89
FT /note="Phosphoserine; by EFR"
FT /evidence="ECO:0000269|PubMed:29649442"
FT MOD_RES 90
FT /note="Phosphothreonine; by EFR"
FT /evidence="ECO:0000269|PubMed:29649442"
FT MOD_RES 120
FT /note="Phosphothreonine; by EFR"
FT /evidence="ECO:0000269|PubMed:29649442,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 129
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 129
FT /note="Phosphoserine; by EFR"
FT /evidence="ECO:0000269|PubMed:29649442"
FT MOD_RES 150
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:24532660"
FT MOD_RES 168
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 206
FT /note="Phosphoserine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 214
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 233
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:23431184,
FT ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650"
FT MOD_RES 236
FT /note="O-UMP-serine; by Xanthomonas campestris effector
FT XopAC/AvrAC; alternate"
FT /evidence="ECO:0000269|PubMed:22504181"
FT MOD_RES 236
FT /note="Phosphoserine; by autocatalysis and BAK1; alternate"
FT /evidence="ECO:0000269|PubMed:20413097,
FT ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 237
FT /note="O-UMP-threonine; by Xanthomonas campestris effector
FT XopAC/AvrAC; alternate"
FT /evidence="ECO:0000269|PubMed:22504181"
FT MOD_RES 237
FT /note="Phosphothreonine; by autocatalysis and BAK1;
FT alternate"
FT /evidence="ECO:0000269|PubMed:20404519,
FT ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392"
FT MOD_RES 242
FT /note="Phosphothreonine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 243
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:24532660"
FT MOD_RES 250
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:24532660"
FT MOD_RES 252
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 253
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392"
FT MOD_RES 314
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 360
FT /note="Phosphoserine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 362
FT /note="Phosphothreonine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 368
FT /note="Phosphothreonine; by autocatalysis and BAK1"
FT /evidence="ECO:0000269|PubMed:24104392,
FT ECO:0000269|PubMed:30212650"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:26021844"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 2
FT /note="G->A: Mis-localization and impaired phosphorylation
FT and ubiquitination upon flagellin (flg22) treatment, but
FT conserved kinase activity and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25522736, ECO:0000269|Ref.20"
FT MUTAGEN 2
FT /note="G->S: Drastic reduction of plasma membrane
FT localization and strong increase of cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:26021844"
FT MUTAGEN 31
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-41, R-95, R-170, R-
FT 186, R-286, R-337, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 41
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-95, R-170, R-
FT 186, R-286, R-337, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 89..90
FT /note="ST->AA: Impaired sensitivity toward elf18-mediated
FT growth inhibition and increased sensitivity to Pseudomonas
FT syringae pv. tomato (Pst) DC3000 bacteria, but no growth
FT defect in normal conditions and normal mitogen-activated
FT protein kinases (MAPKs) activation during EFR-mediated
FT signaling. Enhanced interaction with the WRKY transcription
FT factors WRKY33, WRKY50, WRKY51 and WRKY57 involved in the
FT regulation of jasmonic acid (JA) and salicylic acid (SA)
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:29649442"
FT MUTAGEN 89..90
FT /note="ST->DD: Phosphomimetic, associated with an increased
FT sensitivity toward elf18-mediated growth inhibition and an
FT enhanced resistance to Pseudomonas syringae pv. tomato
FT (Pst) DC3000 bacteria despite a normal mitogen-activated
FT protein kinases (MAPKs) activation during EFR-mediated
FT signaling. Growth defect in normal conditions. Reduced
FT interaction with EFR. Increased jasmonic acid (JA) and
FT salicylic acid (SA) levels. Reduced interaction with and
FT phosphorylation of the WRKY transcription factors WRKY33,
FT WRKY50, WRKY51 and WRKY57 involved in the regulation of
FT jasmonic acid (JA) and salicylic acid (SA) biosynthesis."
FT /evidence="ECO:0000269|PubMed:29649442"
FT MUTAGEN 95
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-170, R-
FT 186, R-286, R-337, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 105
FT /note="K->A: Loss of kinase activity; when associated with
FT A-106."
FT /evidence="ECO:0000269|PubMed:30212650"
FT MUTAGEN 105
FT /note="K->E: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:23431184"
FT MUTAGEN 106
FT /note="K->A: Loss of kinase activity; when associated with
FT A-105."
FT /evidence="ECO:0000269|PubMed:30212650"
FT MUTAGEN 106
FT /note="K->R: Impaired kinase activity."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 120
FT /note="T->A: Normal sensitivity toward elf18-mediated
FT growth inhibition. Normal sensitivity toward elf18-mediated
FT growth inhibition; when associated with A-129."
FT /evidence="ECO:0000269|PubMed:29649442"
FT MUTAGEN 129
FT /note="S->A: Normal sensitivity toward elf18-mediated
FT growth inhibition. Normal sensitivity toward elf18-mediated
FT growth inhibition; when associated with A-120."
FT /evidence="ECO:0000269|PubMed:29649442"
FT MUTAGEN 150
FT /note="Y->F: Loss of function in innate immunity."
FT /evidence="ECO:0000269|PubMed:24532660"
FT MUTAGEN 170
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-95, R-
FT 186, R-286, R-337, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 186
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-95, R-
FT 170, R-286, R-337, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 202
FT /note="D->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:24104392"
FT MUTAGEN 204
FT /note="K->R: Compromised flg22-induced ubiquitination and
FT reduced phosphorylation."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 237
FT /note="T->A: Compromised flg22-induced ubiquitination."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 243
FT /note="Y->F: Loss of function in innate immunity."
FT /evidence="ECO:0000269|PubMed:24532660"
FT MUTAGEN 250
FT /note="Y->A: Compromised flg22-induced ubiquitination."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 250
FT /note="Y->F: Loss of function in innate immunity."
FT /evidence="ECO:0000269|PubMed:24532660"
FT MUTAGEN 286
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-95, R-
FT 170, R-186, R-337, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 337
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-95, R-
FT 170, R-186, R-286, R-358 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 358
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-95, R-
FT 170, R-186, R-286, R-337 and R-366."
FT /evidence="ECO:0000269|Ref.20"
FT MUTAGEN 366
FT /note="K->R: Impaired flg22-induced ubiquination,
FT internalization of BIK1 and FLS2 from the plasma membrane
FT and reactive oxygen species (ROS) production, as well as
FT enhanced susceptibilitye to the bacterial pathogen
FT Pseudomonas syringae pv. tomato (Pst) DC3000 and to the
FT fungal pathogen Botrytis cinerea, but normal
FT phosphorylation; when associated with R-31, R-41, R-95, R-
FT 170, R-186, R-286, R-337 and R-358."
FT /evidence="ECO:0000269|Ref.20"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:5TOS"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:5TOS"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5TOS"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:5TOS"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:5TOS"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:5TOS"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:5TOS"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5TOS"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5TOS"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5TOS"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:5TOS"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:5TOS"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:5TOS"
SQ SEQUENCE 395 AA; 44097 MW; 4C06B1FD01889440 CRC64;
MGSCFSSRVK ADIFHNGKSS DLYGLSLSSR KSSSTVAAAQ KTEGEILSST PVKSFTFNEL
KLATRNFRPD SVIGEGGFGC VFKGWLDEST LTPTKPGTGL VIAVKKLNQE GFQGHREWLT
EINYLGQLSH PNLVKLIGYC LEDEHRLLVY EFMQKGSLEN HLFRRGAYFK PLPWFLRVNV
ALDAAKGLAF LHSDPVKVIY RDIKASNILL DADYNAKLSD FGLARDGPMG DLSYVSTRVM
GTYGYAAPEY MSSGHLNARS DVYSFGVLLL EILSGKRALD HNRPAKEENL VDWARPYLTS
KRKVLLIVDN RLDTQYLPEE AVRMASVAVQ CLSFEPKSRP TMDQVVRALQ QLQDNLGKPS
QTNPVKDTKK LGFKTGTTKS SEKRFTQKPF GRHLV
