RPS5_ARATH
ID RPS5_ARATH Reviewed; 889 AA.
AC O64973; O81402; O82098; O82100;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Disease resistance protein RPS5;
DE AltName: Full=Resistance to Pseudomonas syringae protein 5;
DE AltName: Full=pNd3/pNd10;
GN Name=RPS5; OrderedLocusNames=At1g12220; ORFNames=T28K15.5;
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], FUNCTION, AND MUTANTS RPS5-1 AND RPS5-2.
RC STRAIN=cv. Columbia;
RX PubMed=9724691; DOI=10.2307/3870609;
RA Warren R.F., Henk A., Mowery P., Holub E., Innes R.W.;
RT "A mutation within the leucine-rich repeat domain of the Arabidopsis
RT disease resistance gene RPS5 partially suppresses multiple bacterial and
RT downy mildew resistance genes.";
RL Plant Cell 10:1439-1452(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-355.
RC STRAIN=cv. Nd-1;
RX PubMed=9670562; DOI=10.1046/j.1365-313x.1998.00138.x;
RA Speulman E., Bouchez D., Holub E.B., Beynon J.L.;
RT "Disease resistance gene homologs correlate with disease resistance loci of
RT Arabidopsis thaliana.";
RL Plant J. 14:467-474(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-347.
RC STRAIN=cv. Columbia;
RX PubMed=9530866; DOI=10.1094/mpmi.1998.11.4.251;
RA Aarts M.G.M., te Lintel Hekkert B., Holub E.B., Beynon J.L., Stiekema W.J.,
RA Pereira A.;
RT "Identification of R-gene homologous DNA fragments genetically linked to
RT disease resistance loci in Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 11:251-258(1998).
RN [7]
RP FUNCTION.
RX PubMed=12947197; DOI=10.1126/science.1085671;
RA Shao F., Golstein C., Ade J., Stoutemyer M., Dixon J.E., Innes R.W.;
RT "Cleavage of Arabidopsis PBS1 by a bacterial type III effector.";
RL Science 301:1230-1233(2003).
RN [8]
RP FUNCTION, INTERACTION WITH PBS1, SUBUNIT, AND MUTAGENESIS OF LYS-189 AND
RP ASP-266.
RX PubMed=17277084; DOI=10.1073/pnas.0608779104;
RA Ade J., DeYoung B.J., Golstein C., Innes R.W.;
RT "Indirect activation of a plant nucleotide binding site-leucine-rich repeat
RT protein by a bacterial protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2531-2536(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH PBS1.
RX PubMed=22372664; DOI=10.1111/j.1462-5822.2012.01779.x;
RA DeYoung B.J., Qi D., Kim S.H., Burke T.P., Innes R.W.;
RT "Activation of a plant nucleotide binding-leucine rich repeat disease
RT resistance protein by a modified self protein.";
RL Cell. Microbiol. 14:1071-1084(2012).
RN [10]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4, AND
RP MUTAGENESIS OF GLY-2; CYS-4 AND SER-6.
RX PubMed=22046960; DOI=10.1094/mpmi-11-10-0272;
RA Takemoto D., Rafiqi M., Hurley U., Lawrence G.J., Bernoux M., Hardham A.R.,
RA Ellis J.G., Dodds P.N., Jones D.A.;
RT "N-terminal motifs in some plant disease resistance proteins function in
RT membrane attachment and contribute to disease resistance.";
RL Mol. Plant Microbe Interact. 25:379-392(2012).
RN [11]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2-GLY-GLY-3 AND CYS-4.
RX PubMed=22331412; DOI=10.1104/pp.112.194035;
RA Qi D., DeYoung B.J., Innes R.W.;
RT "Structure-function analysis of the coiled-coil and leucine-rich repeat
RT domains of the RPS5 disease resistance protein.";
RL Plant Physiol. 158:1819-1832(2012).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the avrPphB type III effector avirulence protein from Pseudomonas
CC syringae. Also confers resistance against Hyaloperonospora parasitica
CC (downy mildew). Resistance proteins guard the plant against pathogens
CC that contain an appropriate avirulence protein via an indirect
CC interaction with this avirulence protein. That triggers a defense
CC system including the hypersensitive response, which restricts the
CC pathogen growth. Requires PBS1 to trigger the defense reaction against
CC avrPphB. In case of infection by Pseudomonas syringae, AvrPphB triggers
CC RPS5-mediated defense mechanism via the cleavage of PBS1, suggesting
CC that the cleavage of PBS1 could trigger an exchange of ADP for ATP,
CC thereby activating RPS5. May function as a fine-tuned sensor of
CC alterations in the structure of the effector target PBS1.
CC {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084,
CC ECO:0000269|PubMed:22372664, ECO:0000269|PubMed:9724691}.
CC -!- SUBUNIT: In uninfected plants, interacts with PBS1 through the coiled
CC coil domain. Homodimer. {ECO:0000269|PubMed:17277084,
CC ECO:0000269|PubMed:22372664}.
CC -!- INTERACTION:
CC O64973; Q9FE20: PBS1; NbExp=2; IntAct=EBI-15620767, EBI-2357898;
CC O64973; O64973: RPS5; NbExp=6; IntAct=EBI-15620767, EBI-15620767;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor
CC {ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:22331412}.
CC -!- DOMAIN: The LRR repeats probably act as specificity determinant of
CC pathogen recognition. {ECO:0000250}.
CC -!- MISCELLANEOUS: RPS5 is absent in cv. Landsberg erecta.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {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; AF074916; AAC26126.1; -; Genomic_DNA.
DR EMBL; AC022522; AAG12572.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28851.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28852.1; -; Genomic_DNA.
DR EMBL; BT010583; AAQ82844.1; -; mRNA.
DR EMBL; U97219; AAC50027.1; -; Genomic_DNA.
DR EMBL; U97221; AAC19138.1; -; Genomic_DNA.
DR EMBL; AF039379; AAC14555.1; -; Genomic_DNA.
DR PIR; C86257; C86257.
DR RefSeq; NP_001184970.1; NM_001198041.2.
DR RefSeq; NP_172686.1; NM_101094.3.
DR AlphaFoldDB; O64973; -.
DR SMR; O64973; -.
DR BioGRID; 23015; 3.
DR DIP; DIP-60862N; -.
DR IntAct; O64973; 2.
DR STRING; 3702.AT1G12220.2; -.
DR iPTMnet; O64973; -.
DR PaxDb; O64973; -.
DR PRIDE; O64973; -.
DR ProteomicsDB; 228024; -.
DR EnsemblPlants; AT1G12220.1; AT1G12220.1; AT1G12220.
DR EnsemblPlants; AT1G12220.2; AT1G12220.2; AT1G12220.
DR GeneID; 837775; -.
DR Gramene; AT1G12220.1; AT1G12220.1; AT1G12220.
DR Gramene; AT1G12220.2; AT1G12220.2; AT1G12220.
DR KEGG; ath:AT1G12220; -.
DR Araport; AT1G12220; -.
DR TAIR; locus:2201996; AT1G12220.
DR eggNOG; KOG4658; Eukaryota.
DR HOGENOM; CLU_000427_4_0_1; -.
DR InParanoid; O64973; -.
DR OrthoDB; 236715at2759; -.
DR PhylomeDB; O64973; -.
DR PRO; PR:O64973; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64973; baseline and differential.
DR Genevisible; O64973; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000166; F:nucleotide binding; IMP:TAIR.
DR GO; GO:0038023; F:signaling receptor activity; IMP:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR Gene3D; 1.10.10.10; -; 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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23155; PTHR23155; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Coiled coil; Hypersensitive response;
KW Leucine-rich repeat; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Palmitate; Plant defense; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..889
FT /note="Disease resistance protein RPS5"
FT /id="PRO_0000212730"
FT DOMAIN 140..444
FT /note="NB-ARC"
FT REPEAT 518..539
FT /note="LRR 1"
FT REPEAT 540..561
FT /note="LRR 2"
FT REPEAT 564..586
FT /note="LRR 3"
FT REPEAT 588..610
FT /note="LRR 4"
FT REPEAT 611..633
FT /note="LRR 5"
FT REPEAT 634..656
FT /note="LRR 6"
FT COILED 29..58
FT /evidence="ECO:0000255"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:22046960"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000303|PubMed:22046960"
FT MUTAGEN 2..3
FT /note="GG->AA: Affects plasma membrane location. Reduces
FT RPS5-mediated plant resistance to P.syringae. Abolishes
FT RPS5-mediated plant resistance to P.syringae; when
FT associated with A-4."
FT /evidence="ECO:0000269|PubMed:22331412"
FT MUTAGEN 2
FT /note="G->A: Affects plasma membrane location."
FT /evidence="ECO:0000269|PubMed:22046960"
FT MUTAGEN 4
FT /note="C->A: Slightly affects plasma membrane location.
FT Abolishes RPS5-mediated plant resistance to P.syringae;
FT when associated with 2-AA-3."
FT /evidence="ECO:0000269|PubMed:22046960,
FT ECO:0000269|PubMed:22331412"
FT MUTAGEN 6
FT /note="S->A: Affects plasma membrane location."
FT /evidence="ECO:0000269|PubMed:22046960"
FT MUTAGEN 189
FT /note="K->N: Abolishes RPS5-mediated plant resistance to
FT P.syringae."
FT /evidence="ECO:0000269|PubMed:17277084"
FT MUTAGEN 266
FT /note="D->E: Induces RPS5-mediated plant resistance to
FT P.syringae."
FT /evidence="ECO:0000269|PubMed:17277084"
FT MUTAGEN 572
FT /note="E->K: In rps5-1; impairs defense reaction against
FT pathogens."
FT MUTAGEN 799
FT /note="P->S: In rps5-1; impairs defense reaction against
FT pathogens."
FT CONFLICT 194..196
FT /note="TKI -> RRS (in Ref. 6; AAC14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..207
FT /note="RF -> SI (in Ref. 6; AAC14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="V -> A (in Ref. 5; AAC19138)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="S -> P (in Ref. 6; AAC14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="S -> G (in Ref. 5; AAC50027)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> T (in Ref. 5; AAC50027)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="L -> S (in Ref. 6; AAC14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="A -> V (in Ref. 5; AAC19138)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="H -> P (in Ref. 5; AAC50027)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="D -> A (in Ref. 5; AAC19138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 889 AA; 101802 MW; 7B421BBE599E5171 CRC64;
MGGCFSVSLP CDQVVSQFSQ LLCVRGSYIH NLSKNLASLQ KAMRMLKARQ YDVIRRLETE
EFTGRQQRLS QVQVWLTSVL IIQNQFNDLL RSNEVELQRL CLCGFCSKDL KLSYRYGKRV
IMMLKEVESL SSQGFFDVVS EATPFADVDE IPFQPTIVGQ EIMLEKAWNR LMEDGSGILG
LYGMGGVGKT TLLTKINNKF SKIDDRFDVV IWVVVSRSST VRKIQRDIAE KVGLGGMEWS
EKNDNQIAVD IHNVLRRRKF VLLLDDIWEK VNLKAVGVPY PSKDNGCKVA FTTRSRDVCG
RMGVDDPMEV SCLQPEESWD LFQMKVGKNT LGSHPDIPGL ARKVARKCRG LPLALNVIGE
AMACKRTVHE WCHAIDVLTS SAIDFSGMED EILHVLKYSY DNLNGELMKS CFLYCSLFPE
DYLIDKEGLV DYWISEGFIN EKEGRERNIN QGYEIIGTLV RACLLLEEER NKSNVKMHDV
VREMALWISS DLGKQKEKCI VRAGVGLREV PKVKDWNTVR KISLMNNEIE EIFDSHECAA
LTTLFLQKND VVKISAEFFR CMPHLVVLDL SENQSLNELP EEISELASLR YFNLSYTCIH
QLPVGLWTLK KLIHLNLEHM SSLGSILGIS NLWNLRTLGL RDSRLLLDMS LVKELQLLEH
LEVITLDISS SLVAEPLLCS QRLVECIKEV DFKYLKEESV RVLTLPTMGN LRKLGIKRCG
MREIKIERTT SSSSRNKSPT TPCFSNLSRV FIAKCHGLKD LTWLLFAPNL TFLEVGFSKE
VEDIISEEKA EEHSATIVPF RKLETLHLFE LRGLKRIYAK ALHFPCLKVI HVEKCEKLRK
LPLDSKSGIA GEELVIYYGE REWIERVEWE DQATQLRFLP SSRWRWRET
