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Serine/threonine-protein kinase PBS1 (EC 2.7.11.1) (AvrPphB susceptible protein 1)

 PBS1_ARATH              Reviewed;         456 AA.
Q9FE20;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 135.
RecName: Full=Serine/threonine-protein kinase PBS1 {ECO:0000303|PubMed:11359614};
EC=2.7.11.1 {ECO:0000269|PubMed:11359614};
AltName: Full=AvrPphB susceptible protein 1 {ECO:0000303|PubMed:11359614};
Name=PBS1 {ECO:0000303|PubMed:11359614};
OrderedLocusNames=At5g13160 {ECO:0000312|Araport:AT5G13160};
ORFNames=T19L5.120 {ECO:0000312|EMBL:CAC05444.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY,
AUTOPHOSPHORYLATION, MUTANT PBS1-2, AND MUTAGENESIS OF GLY-252.
PubMed=11359614; DOI=10.1046/j.1365-313x.2001.01014.x;
Swiderski M.R., Innes R.W.;
"The Arabidopsis PBS1 resistance gene encodes a member of a novel
protein kinase subfamily.";
Plant J. 26:101-112(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
PARTIAL PROTEIN SEQUENCE, FUNCTION, CLEAVAGE, INTERACTION WITH
AVRPPHB, AND MUTAGENESIS OF LYS-115; GLY-241; ASP-242 AND LYS-243.
PubMed=12947197; DOI=10.1126/science.1085671;
Shao F., Golstein C., Ade J., Stoutemyer M., Dixon J.E., Innes R.W.;
"Cleavage of Arabidopsis PBS1 by a bacterial type III effector.";
Science 301:1230-1233(2003).
[6]
FUNCTION, INTERACTION WITH RPS5, AND MUTAGENESIS OF LYS-115 AND
GLY-252.
PubMed=17277084; DOI=10.1073/pnas.0608779104;
Ade J., DeYoung B.J., Golstein C., Innes R.W.;
"Indirect activation of a plant nucleotide binding site-leucine-rich
repeat protein by a bacterial protease.";
Proc. Natl. Acad. Sci. U.S.A. 104:2531-2536(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[8]
INTERACTION WITH FLS2, DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION
BY FLAGELLIN.
PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
"Receptor-like cytoplasmic kinases integrate signaling from multiple
plant immune receptors and are targeted by a Pseudomonas syringae
effector.";
Cell Host Microbe 7:290-301(2010).
[9]
FUNCTION, INTERACTION WITH RPS5, AND MUTAGENESIS OF LYS-115 AND
GLY-252.
PubMed=22372664; DOI=10.1111/j.1462-5822.2012.01779.x;
DeYoung B.J., Qi D., Kim S.H., Burke T.P., Innes R.W.;
"Activation of a plant nucleotide binding-leucine rich repeat disease
resistance protein by a modified self protein.";
Cell. Microbiol. 14:1071-1084(2012).
[10]
SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3; PHE-4 AND CYS-6,
AND MYRISTOYLATION AT GLY-2.
PubMed=22046960; DOI=10.1094/MPMI-11-10-0272;
Takemoto D., Rafiqi M., Hurley U., Lawrence G.J., Bernoux M.,
Hardham A.R., Ellis J.G., Dodds P.N., Jones D.A.;
"N-terminal motifs in some plant disease resistance proteins function
in membrane attachment and contribute to disease resistance.";
Mol. Plant Microbe Interact. 25:379-392(2012).
[11]
SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3; CYS-6; GLY-98;
GLY-103; SER-244 AND GLY-286, PALMITOYLATION AT CYS-3 AND CYS-6, AND
MOTIF.
PubMed=24225654; DOI=10.1104/pp.113.227686;
Qi D., Dubiella U., Kim S.H., Sloss D.I., Dowen R.H., Dixon J.E.,
Innes R.W.;
"Recognition of the protein kinase AVRPPHB SUSCEPTIBLE1 by the disease
resistance protein RESISTANCE TO PSEUDOMONAS SYRINGAE5 is dependent on
s-acylation and an exposed loop in AVRPPHB SUSCEPTIBLE1.";
Plant Physiol. 164:340-351(2014).
-!- FUNCTION: Protein kinase required for plant defense mechanism
mediated by the disease resistance (R) protein RPS5. In case of
infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated
defense mechanism via the cleavage of PBS1. Both kinase activity
and cleavage by avrPphB are independently required to trigger the
RPS5-mediated resistance. Contributes to PAMP-triggered immunity
(PTI) signaling and defense responses downstream of FLS2.
{ECO:0000269|PubMed:11359614, ECO:0000269|PubMed:12947197,
ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:20413097,
ECO:0000269|PubMed:22372664}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11359614}.
-!- SUBUNIT: In infected plant cells, it interacts with the P.syringae
virulence protein avrPphB. In uninfected plants,
autophosphorylated form interacts with RPS5. Interacts with FLS2.
{ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084,
ECO:0000269|PubMed:20413097}.
-!- INTERACTION:
O64973:RPS5; NbExp=2; IntAct=EBI-2357898, EBI-15620767;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor
{ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:24225654}.
-!- INDUCTION: Induced by flagellin (flg22).
{ECO:0000269|PubMed:20413097}.
-!- PTM: Cleaved by avrPphB in infected plant cells. Its cleavage
serves as a signal that triggers the RPS5-mediated defense system.
{ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084}.
-!- PTM: Autophosphorylates (Probable). Autophosphorylation may be
required to trigger the RPS5-mediated plant defense system.
{ECO:0000305}.
-!- PTM: Palmitoylation at Cys-3 and Cys-6 are required for plasma
membrane location that is essential for the RPS5-mediated plant
defense response. {ECO:0000269|PubMed:24225654}.
-!- DISRUPTION PHENOTYPE: Reduction in H(2)O(2) accumulation and
callose deposits. {ECO:0000269|PubMed:20413097}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
-----------------------------------------------------------------------
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EMBL; AF314176; AAG38109.1; -; mRNA.
EMBL; AL391711; CAC05444.1; -; Genomic_DNA.
EMBL; CP002688; AED91858.1; -; Genomic_DNA.
EMBL; AF372927; AAK50067.1; -; mRNA.
EMBL; AY078037; AAL77738.1; -; mRNA.
RefSeq; NP_196820.1; NM_121319.5.
UniGene; At.23518; -.
ProteinModelPortal; Q9FE20; -.
SMR; Q9FE20; -.
BioGrid; 16433; 2.
DIP; DIP-53310N; -.
IntAct; Q9FE20; 3.
STRING; 3702.AT5G13160.1; -.
iPTMnet; Q9FE20; -.
SwissPalm; Q9FE20; -.
PaxDb; Q9FE20; -.
PRIDE; Q9FE20; -.
EnsemblPlants; AT5G13160.1; AT5G13160.1; AT5G13160.
GeneID; 831155; -.
Gramene; AT5G13160.1; AT5G13160.1; AT5G13160.
KEGG; ath:AT5G13160; -.
Araport; AT5G13160; -.
TAIR; locus:2179857; AT5G13160.
eggNOG; KOG1187; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000116550; -.
InParanoid; Q9FE20; -.
KO; K13430; -.
OMA; RERKQPN; -.
OrthoDB; EOG093609F5; -.
PhylomeDB; Q9FE20; -.
PMAP-CutDB; Q9FE20; -.
PRO; PR:Q9FE20; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FE20; baseline and differential.
Genevisible; Q9FE20; AT.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0009816; P:defense response to bacterium, incompatible interaction; IMP:TAIR.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome;
Direct protein sequencing; Kinase; Lipoprotein; Membrane; Myristate;
Nucleotide-binding; Palmitate; Phosphoprotein; Plant defense;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000305|PubMed:22046960}.
CHAIN 2 456 Serine/threonine-protein kinase PBS1.
/FTId=PRO_0000086482.
DOMAIN 86 363 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 92 100 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 292 296 Recognition motif required for RPS5-
mediated plant resistance to P.syringae.
{ECO:0000269|PubMed:24225654}.
ACT_SITE 213 213 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 115 115 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 243 244 Cleavage; by avrPphB.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 160 160 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 248 248 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 253 253 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000303|PubMed:22046960}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:24225654}.
LIPID 6 6 S-palmitoyl cysteine.
{ECO:0000269|PubMed:24225654}.
MUTAGEN 2 2 G->A: Slightly affects plasma membrane
location. Abolishes plasma membrane
location; when associated with A-3 and A-
6. {ECO:0000269|PubMed:22046960,
ECO:0000269|PubMed:24225654}.
MUTAGEN 3 3 C->A: Affects plasma membrane location.
Abolishes plasma membrane location; when
associated with A-2 and A-6.
{ECO:0000269|PubMed:22046960,
ECO:0000269|PubMed:24225654}.
MUTAGEN 4 4 F->A: Affects plasma membrane location.
{ECO:0000269|PubMed:22046960}.
MUTAGEN 6 6 C->A: Affects plasma membrane location.
Abolishes plasma membrane location; when
associated with A-2 and A-3.
{ECO:0000269|PubMed:22046960,
ECO:0000269|PubMed:24225654}.
MUTAGEN 98 98 G->E: In pbs1-5; strongly impairs RPS5-
mediated plant resistance to P.syringae.
{ECO:0000269|PubMed:24225654}.
MUTAGEN 103 103 G->R: In pbs1-3; strongly impairs
cleavage by avrPphB and RPS5-mediated
plant resistance to P.syringae.
{ECO:0000269|PubMed:24225654}.
MUTAGEN 115 115 K->N: Abolishes kinase activity and RPS5-
mediated plant resistance to P.syringae.
{ECO:0000269|PubMed:12947197,
ECO:0000269|PubMed:17277084,
ECO:0000269|PubMed:22372664}.
MUTAGEN 241 241 G->A: Abolishes cleavage by avrPphB and
RPS5-mediated plant resistance to
P.syringae.
{ECO:0000269|PubMed:12947197}.
MUTAGEN 242 242 D->A: Strongly impairs cleavage by
avrPphB and RPS5-mediated plant
resistance to P.syringae.
{ECO:0000269|PubMed:12947197}.
MUTAGEN 243 243 K->A: Affects cleavage by avrPphB and
RPS5-mediated plant resistance to
P.syringae.
{ECO:0000269|PubMed:12947197}.
MUTAGEN 244 244 S->F: In pbs1-6; strongly impairs RPS5-
mediated plant resistance to P.syringae.
{ECO:0000269|PubMed:24225654}.
MUTAGEN 252 252 G->R: In pbs1-2; strongly impairs RPS5-
mediated plant resistance to P.syringae.
{ECO:0000269|PubMed:11359614,
ECO:0000269|PubMed:17277084,
ECO:0000269|PubMed:22372664}.
MUTAGEN 286 286 G->D: In pbs1-4; strongly impairs
cleavage by avrPphB and RPS5-mediated
plant resistance to P.syringae.
{ECO:0000269|PubMed:24225654}.
SEQUENCE 456 AA; 50384 MW; C167E4E3F47ACBC3 CRC64;
MGCFSCFDSS DDEKLNPVDE SNHGQKKQSQ PTVSNNISGL PSGGEKLSSK TNGGSKRELL
LPRDGLGQIA AHTFAFRELA AATMNFHPDT FLGEGGFGRV YKGRLDSTGQ VVAVKQLDRN
GLQGNREFLV EVLMLSLLHH PNLVNLIGYC ADGDQRLLVY EFMPLGSLED HLHDLPPDKE
ALDWNMRMKI AAGAAKGLEF LHDKANPPVI YRDFKSSNIL LDEGFHPKLS DFGLAKLGPT
GDKSHVSTRV MGTYGYCAPE YAMTGQLTVK SDVYSFGVVF LELITGRKAI DSEMPHGEQN
LVAWARPLFN DRRKFIKLAD PRLKGRFPTR ALYQALAVAS MCIQEQAATR PLIADVVTAL
SYLANQAYDP SKDDSRRNRD ERGARLITRN DDGGGSGSKF DLEGSEKEDS PRETARILNR
DINRERAVAE AKMWGESLRE KRRQSEQGTS ESNSTG


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