WR52W_ARATH
ID WR52W_ARATH Reviewed; 1373 AA.
AC C4B7M5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Disease resistance protein RRS1 {ECO:0000303|PubMed:19519800};
DE AltName: Full=Disease resistance protein RCH2 {ECO:0000303|PubMed:19519800};
DE AltName: Full=Probable WRKY transcription factor 52;
DE AltName: Full=Resistance to Colletotrichum higginsianum 2 protein {ECO:0000303|PubMed:19519800};
DE AltName: Full=Resistance to Ralstonia solanacearum 1 protein {ECO:0000303|PubMed:19519800};
GN Name=RRS1 {ECO:0000303|PubMed:19519800};
GN Synonyms=RCH2 {ECO:0000303|PubMed:19519800}, RRS1-R, WRKY52;
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 {ECO:0000312|EMBL:BAH59424.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19519800; DOI=10.1111/j.1365-313x.2009.03949.x;
RA Narusaka M., Shirasu K., Noutoshi Y., Kubo Y., Shiraishi T., Iwabuchi M.,
RA Narusaka Y.;
RT "RRS1 and RPS4 provide a dual Resistance-gene system against fungal and
RT bacterial pathogens.";
RL Plant J. 60:218-226(2009).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19826224; DOI=10.4161/psb.4.10.9640;
RA Narusaka M., Kubo Y., Shiraishi T., Iwabuchi M., Narusaka Y.;
RT "A dual resistance gene system prevents infection by three distinct
RT pathogens.";
RL Plant Signal. Behav. 4:954-955(2009).
RN [3]
RP FUNCTION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=24146667; DOI=10.3389/fpls.2013.00403;
RA Heidrich K., Tsuda K., Blanvillain-Baufume S., Wirthmueller L., Bautor J.,
RA Parker J.E.;
RT "Arabidopsis TNL-WRKY domain receptor RRS1 contributes to temperature-
RT conditioned RPS4 auto-immunity.";
RL Front. Plant Sci. 4:403-403(2013).
CC -!- FUNCTION: Transcription factor. Interacts specifically with the W box
CC (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC acting element. Acts also as a disease resistance protein involved in
CC resistance to fungal and bacterial pathogens, including R.solanacearum,
CC P.syringae pv. tomato and C.higginsianum. In presence of RPS4, elicites
CC an EDS1-dependent hypersensitive response (PubMed:24146667).
CC {ECO:0000250|UniProtKB:Q9FH83, ECO:0000269|PubMed:19519800,
CC ECO:0000269|PubMed:19826224, ECO:0000269|PubMed:24146667, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PopP2, a R.solanacearum type III effector.
CC {ECO:0000250|UniProtKB:P0DKH5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223}.
CC -!- DISRUPTION PHENOTYPE: Loss of resistance to C.higginsianum.
CC {ECO:0000269|PubMed:19826224}.
CC -!- MISCELLANEOUS: Ecotypes susceptible to C.higginsianum or
CC R.solanacearum, such as cv. Columbia, contain a protein with a
CC premature stop codon while the longer allele found in cv. Nd-1, cv.
CC Wassilewskija or cv. RLD confers resistance.
CC {ECO:0000269|PubMed:19519800}.
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DR EMBL; AB470471; BAH59424.1; -; mRNA.
DR PDB; 5W3X; X-ray; 2.00 A; B/D=1195-1273.
DR PDB; 7P8K; X-ray; 2.65 A; B=1195-1273.
DR PDBsum; 5W3X; -.
DR PDBsum; 7P8K; -.
DR AlphaFoldDB; C4B7M5; -.
DR SMR; C4B7M5; -.
DR ExpressionAtlas; C4B7M5; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 2.20.25.80; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003657; WRKY_dom.
DR InterPro; IPR036576; WRKY_dom_sf.
DR PANTHER; PTHR11017; PTHR11017; 2.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF03106; WRKY; 1.
DR SMART; SM00774; WRKY; 1.
DR SUPFAM; SSF118290; SSF118290; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
DR PROSITE; PS50811; WRKY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Leucine-rich repeat;
KW Nucleotide-binding; Nucleus; Plant defense; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1373
FT /note="Disease resistance protein RRS1"
FT /id="PRO_0000431361"
FT DOMAIN 5..146
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 170..421
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 498..522
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 535..553
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 554..575
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 577..598
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 621..646
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 665..688
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 742..766
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 768..793
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 831..854
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT DNA_BIND 1204..1272
FT /note="WRKY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 1300..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 988..1005
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT STRAND 1198..1201
FT /evidence="ECO:0007829|PDB:5W3X"
FT STRAND 1215..1221
FT /evidence="ECO:0007829|PDB:5W3X"
FT STRAND 1230..1235
FT /evidence="ECO:0007829|PDB:5W3X"
FT HELIX 1238..1241
FT /evidence="ECO:0007829|PDB:5W3X"
FT STRAND 1246..1251
FT /evidence="ECO:0007829|PDB:5W3X"
FT STRAND 1253..1257
FT /evidence="ECO:0007829|PDB:7P8K"
FT STRAND 1259..1265
FT /evidence="ECO:0007829|PDB:5W3X"
SQ SEQUENCE 1373 AA; 155399 MW; 452DCF9740321428 CRC64;
MTNCEKDEEF VCISCVEEVR YSFVSHLSEA LRRKGINNVV VGVDSDDLLF KESQAKIEKA
GVSVMVLPGN CDPSDVWLDK FAKVLECQRN NKDQAVVPVL YGDSLLRDQW LSELDFKGLS
RIHQSRKECS DSILVEEIVR DVYETHFYVG RIGIYSKLLE IENMVNKQPI GIRCVGIWGM
PGIGKTTLAK AVFDQMSSAF DASCFIEDYD KSIHEKGLYC LLEEQLLPGN DATIMKLSSL
RDRLNSKRVL VVLDDVRNAL VGESFLEGFD WLGPGSLIII TSRDKQVFCL CGINQIYEVQ
GLNEKEARQL FLLSASIKED MGEQNLQELS VRVINYANGN PLAINVYGRE LKGKKKLSEM
ETAFLKLKRR PPFKIVDAFK STYDTLSDNE KNIFLDIACF FQGENVNYVI QLLEGCGFFP
HVEIDVLVDK CLVTISENRV WLHKLTQDIG REIINGETVQ IERRRRLWEP WSIKYLLEYN
EHKANGEPKT TFKRAQGSEE IEGLFLDTSN LRFDLQPSAF KNMLNLRLLK IYCSNPEVHP
VINFPTGSLH SLPNELRLLH WENYPLKSLP QNFDPRHLVE INMPYSQLQK LWGGTKNLEM
LRTIRLCHSH HLVDIDDLLK AENLEVIDLQ GCTRLQNFPA AGRLLRLRDV NLSGCIKIKS
VLEIPPNIEK LHLQGTGILA LPVSTVKPNH RELVNFLTEI PGLSEASKLE RLTSLLESNS
SCQDLGKLIC LELKDCSCLQ SLPNMANLDL NVLDLSGCSS LNSIQGFPRF LKQLYLGGTA
IREVPQLPQS LEILNAHGSC LRSLPNMANL EFLKVLDLSG CSELETIQGF PRNLKELYFA
GTTLREVPQL PLSLEVLNAH GSDSEKLPMH YKFNNFFDLS QQVVNDFFLK TLTYVKHIPR
GYTQELINKA PTFSFSAPSH TNQNATFDLQ PGSSVMTRLN HSWRNTLVGF GMLVEVAFPE
DYCDATDFGI SCVCRWSNKE GRSCRIERNF HCWAPGKVVP KVRKDHTFVF SDVNMRPSTG
EGNDPDIWAG LVVFEFFPIN QQTKCLNDRF TVTRCGVRVI NVATGNTSLE NISLVLSLDP
VEVSGYEVLR VSYDDLQEMD KVLFLYIASL FNDEDVDFVA PLIAGIDLDV SSGLKVLADV
SLISVSSNGE IVMHSLQRQM GKEILHGQSM LLSDCESSMT ENLSDVPKKE KKHRESKVKK
VVSIPAIDEG DLWTWRKYGQ KDILGSRFPR GYYRCAYKFT HGCKATKQVQ RSETDSNMLA
ITYLSEHNHP RPTKRKALAD STRSTSSSIC SAITTSASSR VFQNKDEPNK PHLPSSSTPP
GNAAVLFKMT DMEEFQDNME VDNDVVDTRT LALFPEFQHQ PEEEYPWSTF FDY
