R13L4_ARATH
ID R13L4_ARATH Reviewed; 852 AA.
AC Q38834; Q0WUW7; Q9SVK4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Disease resistance RPP13-like protein 4;
DE AltName: Full=Disease resistance protein ZAR1 {ECO:0000305};
DE AltName: Full=Protein HOPZ-ACTIVATED RESISTANCE 1 {ECO:0000303|PubMed:20368970};
DE Short=AtZAR1 {ECO:0000303|PubMed:28652264};
GN Name=RPP13L4;
GN Synonyms=ZAR1 {ECO:0000303|PubMed:20368970, ECO:0000303|PubMed:26355215};
GN OrderedLocusNames=At3g50950 {ECO:0000312|Araport:AT3G50950};
GN ORFNames=F18B3.230 {ECO:0000312|EMBL:CAB42924.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Rouse D.T., Heazlewood J.L.;
RT "Incomplete sequence of an Arabidopsis gene with similarities to myosin
RT heavy chain.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=20368970; DOI=10.1371/journal.pgen.1000894;
RA Lewis J.D., Wu R., Guttman D.S., Desveaux D.;
RT "Allele-specific virulence attenuation of the Pseudomonas syringae HopZ1a
RT type III effector via the Arabidopsis ZAR1 resistance protein.";
RL PLoS Genet. 6:E1000894-E1000894(2010).
RN [6]
RP INTERACTION WITH ZED1.
RX PubMed=24170858; DOI=10.1073/pnas.1315520110;
RA Lewis J.D., Lee A.H., Hassan J.A., Wan J., Hurley B., Jhingree J.R.,
RA Wang P.W., Lo T., Youn J.Y., Guttman D.S., Desveaux D.;
RT "The Arabidopsis ZED1 pseudokinase is required for ZAR1-mediated immunity
RT induced by the Pseudomonas syringae type III effector HopZ1a.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18722-18727(2013).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-195; PRO-359 AND PRO-816, DISRUPTION
RP PHENOTYPE, SUBUNIT, AND INTERACTION WITH RKS1; ZED1; ZRK3; ZRK6 AND ZRK15.
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28288096; DOI=10.1038/nplants.2017.27;
RA Seto D., Koulena N., Lo T., Menna A., Guttman D.S., Desveaux D.;
RT "Expanded type III effector recognition by the ZAR1 NLR protein using ZED1-
RT related kinases.";
RL Nat. Plants 3:17027-17027(2017).
RN [9]
RP FUNCTION, AND INTERACTION WITH ZED1.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28499073; DOI=10.1111/nph.14585;
RA Wang Z., Cui D., Liu J., Zhao J., Liu C., Xin W., Li Y., Liu N., Ren D.,
RA Tang D., Hu Y.;
RT "Arabidopsis ZED1-related kinases mediate the temperature-sensitive
RT intersection of immune response and growth homeostasis.";
RL New Phytol. 215:711-724(2017).
RN [10]
RP FUNCTION, MUTAGENESIS OF VAL-202; SER-291; LEU-465; GLY-645; PRO-816 AND
RP SER-831, INTERACTION WITH ZED1/ZRK5, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28652264; DOI=10.1104/pp.17.00441;
RA Baudin M., Hassan J.A., Schreiber K.J., Lewis J.D.;
RT "Analysis of the ZAR1 immune complex reveals determinants for immunity and
RT molecular interactions.";
RL Plant Physiol. 174:2038-2053(2017).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) IN COMPLEX WITH DTP,
RP FUNCTION, MUTAGENESIS OF 1-MET--VAL-6; 1-MET--LEU-10; 1-MET--THR-23; PHE-9;
RP LEU-10; LEU-14; ILE-136; ARG-149; TRP-150; SER-152; VAL-154; LYS-195 AND
RP ARG-297, DISRUPTION PHENOTYPE, SUBUNIT, DOMAIN, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=30948527; DOI=10.1126/science.aav5870;
RA Wang J., Hu M., Wang J., Qi J., Han Z., Wang G., Qi Y., Wang H.-W.,
RA Zhou J.-M., Chai J.;
RT "Reconstitution and structure of a plant NLR resistosome conferring
RT immunity.";
RL Science 364:0-0(2019).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) IN COMPLEX WITH ADP,
RP FUNCTION, MUTAGENESIS OF VAL-544; HIS-597; TRP-825 AND PHE-839, SUBUNIT,
RP ACTIVITY REGULATION, AND INTERACTION WITH RKS1.
RC STRAIN=cv. Columbia;
RX PubMed=30948526; DOI=10.1126/science.aav5868;
RA Wang J., Wang J., Hu M., Wu S., Qi J., Wang G., Han Z., Qi Y., Gao N.,
RA Wang H.-W., Zhou J.-M., Chai J.;
RT "Ligand-triggered allosteric ADP release primes a plant NLR complex.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: CC-NB-LRR receptor-like protein required for recognition of
CC pathogenic bacteria type III effectors (T3E) such as Pseudomonas
CC syringae HopZ1a and HopF2a and Xanthomonas campestris pv. campestris
CC (Xcc) XopAC/AvrAC; this recognition requires ZED1-related kinases (e.g.
CC PBL2, ZRK3 and ZED1/ZRK5) (PubMed:20368970, PubMed:26355215,
CC PubMed:28288096, PubMed:30948527, PubMed:30948526, PubMed:28652264).
CC Confers allele-specific recognition and virulence attenuation of HopZ1a
CC (PubMed:20368970). Immunity mediated by RPP13L4/ZAR1 is independent of
CC several genes required by other resistance protein signaling pathways
CC such as NDR1 and RAR1 (PubMed:20368970). Together with ZED1/ZRK5,
CC involved in the regulation of the ambient temperature-sensitive
CC intersection of growth and immune response in the absence of pathogens
CC (PubMed:28499073). {ECO:0000269|PubMed:20368970,
CC ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:28288096,
CC ECO:0000269|PubMed:28499073, ECO:0000269|PubMed:28652264,
CC ECO:0000269|PubMed:30948526, ECO:0000269|PubMed:30948527}.
CC -!- ACTIVITY REGULATION: Exhibits autoinhibition activity.
CC {ECO:0000269|PubMed:30948526}.
CC -!- SUBUNIT: Interacts with ZED1/ZRK5 (PubMed:24170858). Component of a
CC stable high-order oligomeric complex made of RKS1 and RPP13L4/ZAR1
CC which recruits ZED1-related kinases (e.g. uridylylated PBL2 and
CC acetylated ZED1/ZRK5) in the presence of ATP and pathogenic bacteria
CC type III secreted effector (T3SE) proteins (e.g. Pseudomonas syringae
CC HopZ1a and HopF2a and Xanthomonas campestris pv. campestris (Xcc)
CC XopAC/AvrAC) to form a wheel-like pentameric resistosome; this complex
CC triggers immunity toward pathogenic bacteria (e.g. X.campestris and
CC P.syringae), especially in vascular tissues (PubMed:26355215,
CC PubMed:30948527, PubMed:30948526). Interacts with RKS1, ZED1/ZRK5,
CC ZRK3, ZRK6 and ZRK15 (PubMed:26355215, PubMed:30948526,
CC PubMed:28652264). {ECO:0000269|PubMed:24170858,
CC ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:28652264,
CC ECO:0000269|PubMed:30948526, ECO:0000269|PubMed:30948527}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30948527}.
CC Nucleus {ECO:0000269|PubMed:28652264}. Note=Associates with the plasma
CC membrane in the presence of the Xanthomonas campestris effector
CC XopAC/AvrAC. {ECO:0000269|PubMed:30948527}.
CC -!- DOMAIN: N-terminal amphipathic alpha helix form a funnel-shaped
CC structure that is required for the plasma membrane association of the
CC resistosome complex, cell death triggering, and disease resistance.
CC {ECO:0000269|PubMed:30948527}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to the pathogenic
CC biotrophic bacteria Xanthomonas campestris pv. campestris (Xcc)
CC (PubMed:26355215, PubMed:30948527). Reduced resistance to Pseudomonas
CC syringae expressing HopZ1a (PubMed:26355215, PubMed:28288096).
CC {ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:28288096,
CC ECO:0000269|PubMed:30948527}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family. RPP13
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA63149.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative genomics
CC of disease resistance gene homologs;
CC URL="http://niblrrs.ucdavis.edu";
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DR EMBL; U19616; AAA63149.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL049862; CAB42924.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78730.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78731.1; -; Genomic_DNA.
DR EMBL; AK227017; BAE99081.1; -; mRNA.
DR PIR; T08416; T08416.
DR RefSeq; NP_190664.1; NM_114955.4.
DR RefSeq; NP_850677.1; NM_180346.1.
DR PDB; 6J5T; EM; 3.40 A; C/F/G/L/O=1-852.
DR PDB; 6J5U; EM; 3.90 A; A=1-852.
DR PDB; 6J5V; EM; 4.25 A; A=1-852.
DR PDB; 6J5W; EM; 3.70 A; A=1-852.
DR PDB; 6J6I; EM; 3.70 A; C/F/G/L/O=1-852.
DR PDBsum; 6J5T; -.
DR PDBsum; 6J5U; -.
DR PDBsum; 6J5V; -.
DR PDBsum; 6J5W; -.
DR PDBsum; 6J6I; -.
DR AlphaFoldDB; Q38834; -.
DR SMR; Q38834; -.
DR BioGRID; 9577; 2.
DR DIP; DIP-48342N; -.
DR IntAct; Q38834; 1.
DR STRING; 3702.AT3G50950.1; -.
DR PaxDb; Q38834; -.
DR PRIDE; Q38834; -.
DR ProteomicsDB; 236209; -.
DR EnsemblPlants; AT3G50950.1; AT3G50950.1; AT3G50950.
DR EnsemblPlants; AT3G50950.2; AT3G50950.2; AT3G50950.
DR GeneID; 824259; -.
DR Gramene; AT3G50950.1; AT3G50950.1; AT3G50950.
DR Gramene; AT3G50950.2; AT3G50950.2; AT3G50950.
DR KEGG; ath:AT3G50950; -.
DR Araport; AT3G50950; -.
DR TAIR; locus:2078012; AT3G50950.
DR eggNOG; KOG4658; Eukaryota.
DR HOGENOM; CLU_000837_25_2_1; -.
DR InParanoid; Q38834; -.
DR OMA; MLRYMSI; -.
DR OrthoDB; 121218at2759; -.
DR PhylomeDB; Q38834; -.
DR PRO; PR:Q38834; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38834; baseline and differential.
DR Genevisible; Q38834; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
DR CDD; cd14798; RX-CC_like; 1.
DR Gene3D; 1.10.8.430; -; 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; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038005; RX-like_CC.
DR InterPro; IPR041118; Rx_N.
DR PANTHER; PTHR23155; PTHR23155; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF18052; Rx_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coiled coil; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Nucleus; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..852
FT /note="Disease resistance RPP13-like protein 4"
FT /id="PRO_0000212729"
FT DOMAIN 164..410
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 558..581
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 585..609
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 633..657
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 683..706
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 763..786
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 798..824
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT COILED 17..68
FT /evidence="ECO:0000255"
FT BINDING 149
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:30948527,
FT ECO:0007744|PDB:6J5T, ECO:0007744|PDB:6J6I"
FT BINDING 161
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:30948526,
FT ECO:0000269|PubMed:30948527, ECO:0007744|PDB:6J5T,
FT ECO:0007744|PDB:6J5W, ECO:0007744|PDB:6J6I"
FT BINDING 189..196
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:30948526,
FT ECO:0000269|PubMed:30948527, ECO:0007744|PDB:6J5T,
FT ECO:0007744|PDB:6J5W, ECO:0007744|PDB:6J6I"
FT BINDING 297
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:30948527,
FT ECO:0007744|PDB:6J5T, ECO:0007744|PDB:6J6I"
FT BINDING 363
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:30948526,
FT ECO:0007744|PDB:6J5W"
FT MUTAGEN 1..23
FT /note="Missing: Reduced ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 1..10
FT /note="Missing: Reduced ability to mediate cell death as
FT well as an increased sensitivity to the pathogenic
FT biotrophic bacteria Xanthomonas campestris pv. campestris
FT (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 1..6
FT /note="Missing: Reduced ability to mediate cell death."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 9
FT /note="F->A: Reduced ability to mediate cell death as well
FT as an increased sensitivity to the pathogenic biotrophic
FT bacteria Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-10 and A-14."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 10
FT /note="L->A: Reduced ability to mediate cell death as well
FT as an increased sensitivity to the pathogenic biotrophic
FT bacteria Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-9 and A-14."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 14
FT /note="L->A: Reduced ability to mediate cell death as well
FT as an increased sensitivity to the pathogenic biotrophic
FT bacteria Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-9 and A-10."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 136
FT /note="I->E: Reduced oligomerization activity associated
FT with a reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 149
FT /note="R->A: Reduced oligomerization activity associated
FT with a reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-297."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 150
FT /note="W->A: Reduced oligomerization activity associated
FT with a reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 152
FT /note="S->E: Reduced oligomerization activity associated
FT with a reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 154
FT /note="V->E: Reduced oligomerization activity associated
FT with a reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 195
FT /note="K->N: Lost effector-triggered immunity (ETI) in
FT response to the Xanthomonas campestris effector XopAC/AvrAC
FT in the presence of PBL2 and RKS1. Abolished XopAC/AvrAC-
FT induced self-association."
FT /evidence="ECO:0000269|PubMed:26355215,
FT ECO:0000269|PubMed:30948527"
FT MUTAGEN 202
FT /note="V->M: Abolished HopZ1a-induced hypersensitive
FT response (HR) and loss of resistance to Pseudomonas
FT syringae pv. tomato DC3000."
FT /evidence="ECO:0000269|PubMed:28652264"
FT MUTAGEN 291
FT /note="S->N: Abolished HopZ1a-induced hypersensitive
FT response (HR) and loss of resistance to Pseudomonas
FT syringae pv. tomato DC3000. Reduced interaction with ZED1."
FT /evidence="ECO:0000269|PubMed:28652264"
FT MUTAGEN 297
FT /note="R->A: Reduced oligomerization activity associated
FT with a reduced ability to mediate cell death as well as an
FT increased sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-149."
FT /evidence="ECO:0000269|PubMed:30948527"
FT MUTAGEN 359
FT /note="P->L: Lost ability to trigger cell death in response
FT to the Xanthomonas campestris effector XopAC/AvrAC in the
FT presence of PBL2 and RKS1."
FT /evidence="ECO:0000269|PubMed:26355215"
FT MUTAGEN 465
FT /note="L->F: Abolished HopZ1a-induced hypersensitive
FT response (HR) and loss of resistance to Pseudomonas
FT syringae pv. tomato DC3000."
FT /evidence="ECO:0000269|PubMed:28652264"
FT MUTAGEN 544
FT /note="V->E: Impaired interaction with RKS1 and reduced
FT ability to mediate cell death as well as an increased
FT sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 597
FT /note="H->E: Impaired interaction with RKS1 and reduced
FT ability to mediate cell death as well as an increased
FT sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc)."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 645
FT /note="G->E: Abolished HopZ1a-induced hypersensitive
FT response (HR) and loss of resistance to Pseudomonas
FT syringae pv. tomato DC3000. Impaired interaction with
FT ZED1."
FT /evidence="ECO:0000269|PubMed:28652264"
FT MUTAGEN 816
FT /note="P->L: Lost ability to trigger cell death in response
FT to the Xanthomonas campestris effector XopAC/AvrAC in the
FT presence of PBL2 and RKS1. Impaired interactions with RKS1,
FT ZED1, ZRK3, ZRK6 and ZRK15."
FT /evidence="ECO:0000269|PubMed:26355215,
FT ECO:0000269|PubMed:28652264"
FT MUTAGEN 825
FT /note="W->A: Impaired interaction with RKS1 and reduced
FT ability to mediate cell death as well as an increased
FT sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-839."
FT /evidence="ECO:0000269|PubMed:30948526"
FT MUTAGEN 831
FT /note="S->F: Abolished HopZ1a-induced hypersensitive
FT response (HR) and loss of resistance to Pseudomonas
FT syringae pv. tomato DC3000."
FT /evidence="ECO:0000269|PubMed:28652264"
FT MUTAGEN 839
FT /note="F->A: Impaired interaction with RKS1 and reduced
FT ability to mediate cell death as well as an increased
FT sensitivity to the pathogenic biotrophic bacteria
FT Xanthomonas campestris pv. campestris (Xcc); when
FT associated with A-825."
FT /evidence="ECO:0000269|PubMed:30948526"
FT CONFLICT 37
FT /note="E -> K (in Ref. 1; AAA63149)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..130
FT /note="Missing (in Ref. 1; AAA63149)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..136
FT /note="EFI -> KFR (in Ref. 1; AAA63149)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="S -> T (in Ref. 1; AAA63149)"
FT /evidence="ECO:0000305"
FT HELIX 7..25
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 27..48
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 56..76
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 109..135
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 332..337
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 489..499
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 549..555
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 579..583
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 605..608
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 637..640
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 678..682
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 701..707
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 715..718
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 726..732
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:6J5T"
FT TURN 760..762
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 768..771
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 795..800
FT /evidence="ECO:0007829|PDB:6J5T"
FT HELIX 808..814
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 819..825
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 832..835
FT /evidence="ECO:0007829|PDB:6J5T"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:6J5T"
SQ SEQUENCE 852 AA; 97040 MW; 4A1DE0EF393801B6 CRC64;
MVDAVVTVFL EKTLNILEEK GRTVSDYRKQ LEDLQSELKY MQSFLKDAER QKRTNETLRT
LVADLRELVY EAEDILVDCQ LADGDDGNEQ RSSNAWLSRL HPARVPLQYK KSKRLQEINE
RITKIKSQVE PYFEFITPSN VGRDNGTDRW SSPVYDHTQV VGLEGDKRKI KEWLFRSNDS
QLLIMAFVGM GGLGKTTIAQ EVFNDKEIEH RFERRIWVSV SQTFTEEQIM RSILRNLGDA
SVGDDIGTLL RKIQQYLLGK RYLIVMDDVW DKNLSWWDKI YQGLPRGQGG SVIVTTRSES
VAKRVQARDD KTHRPELLSP DNSWLLFCNV AFAANDGTCE RPELEDVGKE IVTKCKGLPL
TIKAVGGLLL CKDHVYHEWR RIAEHFQDEL RGNTSETDNV MSSLQLSYDE LPSHLKSCIL
TLSLYPEDCV IPKQQLVHGW IGEGFVMWRN GRSATESGED CFSGLTNRCL IEVVDKTYSG
TIITCKIHDM VRDLVIDIAK KDSFSNPEGL NCRHLGISGN FDEKQIKVNH KLRGVVSTTK
TGEVNKLNSD LAKKFTDCKY LRVLDISKSI FDAPLSEILD EIASLQHLAC LSLSNTHPLI
QFPRSMEDLH NLQILDASYC QNLKQLQPCI VLFKKLLVLD MTNCGSLECF PKGIGSLVKL
EVLLGFKPAR SNNGCKLSEV KNLTNLRKLG LSLTRGDQIE EEELDSLINL SKLMSISINC
YDSYGDDLIT KIDALTPPHQ LHELSLQFYP GKSSPSWLSP HKLPMLRYMS ICSGNLVKMQ
EPFWGNENTH WRIEGLMLSS LSDLDMDWEV LQQSMPYLRT VTANWCPELE SFAIEDVGFR
GGVWMKTPLH RT
