ARPT2_PSEUB
ID ARPT2_PSEUB Reviewed; 255 AA.
AC Q6LAD6; Q05324; Q4LBF4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Cysteine protease avirulence protein AvrRpt2;
DE Short=Avirulence protein AvrRpt2;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=avrRpt2;
OS Pseudomonas syringae pv. tomato.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JL1065;
RX PubMed=1824334; DOI=10.2307/3869199;
RA Whalen M.C., Innes R.W., Bent A.F., Staskawicz B.J.;
RT "Identification of Pseudomonas syringae pathogens of Arabidopsis and a
RT bacterial locus determining avirulence on both Arabidopsis and soybean.";
RL Plant Cell 3:49-59(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JL1065;
RX PubMed=8335641; DOI=10.1128/jb.175.15.4859-4869.1993;
RA Innes R.W., Bent A.F., Kunkel B.N., Bisgrove S.R., Staskawicz B.J.;
RT "Molecular analysis of avirulence gene avrRpt2 and identification of a
RT putative regulatory sequence common to all known Pseudomonas syringae
RT avirulence genes.";
RL J. Bacteriol. 175:4859-4869(1993).
RN [3]
RP SEQUENCE REVISION.
RC STRAIN=JL1065;
RA Innes R.W.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JL1065;
RA Pitman A.R., Jackson R.W., Mansfield J.W., Thwaites R., Arnold D.L.;
RT "Plant resistance drives evolution of virulence in Pseudomonas syringae pv.
RT phaseolicola by deletion of a chromosomal genomic island.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, PROTEOLYTIC PROCESSING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10361296; DOI=10.1046/j.1365-2958.1999.01403.x;
RA Mudgett M.B., Staskawicz B.J.;
RT "Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein:
RT demonstration of secretion and processing during bacterial pathogenesis.";
RL Mol. Microbiol. 32:927-941(1999).
RN [6]
RP PROTEIN SEQUENCE OF 3-41; 52-57; 63-82; 136-144; 148-162 AND 169-185,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION AS A CYSTEINE PROTEASE, AND
RP CYCLOPHILIN PROCESSING ACTIVATION.
RX PubMed=15746386; DOI=10.1126/science.1108633;
RA Coaker G., Falick A., Staskawicz B.J.;
RT "Activation of a phytopathogenic bacterial effector protein by a eukaryotic
RT cyclophilin.";
RL Science 308:548-550(2005).
RN [7]
RP INTERFERENCE WITH RPM1 ACTIVATION.
RX PubMed=12239384; DOI=10.2307/3870268;
RA Ritter C., Dangl J.L.;
RT "Interference between two specific pathogen recognition events mediated by
RT distinct plant disease resistance genes.";
RL Plant Cell 8:251-257(1996).
RN [8]
RP FUNCTION IN VIRULENCE.
RX PubMed=11106023; DOI=10.1094/mpmi.2000.13.12.1312;
RA Chen Z., Kloek A.P., Boch J., Katagiri F., Kunkel B.N.;
RT "The Pseudomonas syringae avrRpt2 gene product promotes pathogen virulence
RT from inside plant cells.";
RL Mol. Plant Microbe Interact. 13:1312-1321(2000).
RN [9]
RP SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF CYS-122;
RP GLY-131; GLY-141 AND GLY-194.
RX PubMed=11204781; DOI=10.1094/mpmi.2001.14.2.181;
RA Axtell M.J., McNellis T.W., Mudgett M.B., Hsu C.S., Staskawicz B.J.;
RT "Mutational analysis of the Arabidopsis RPS2 disease resistance gene and
RT the corresponding pseudomonas syringae avrRpt2 avirulence gene.";
RL Mol. Plant Microbe Interact. 14:181-188(2001).
RN [10]
RP FUNCTION AS A THIOL PROTEASE, AND MUTAGENESIS OF CYS-122; HIS-208 AND
RP ASP-226.
RX PubMed=12950919; DOI=10.1046/j.1365-2958.2003.03666.x;
RA Axtell M.J., Chisholm S.T., Dahlbeck D., Staskawicz B.J.;
RT "Genetic and molecular evidence that the Pseudomonas syringae type III
RT effector protein AvrRpt2 is a cysteine protease.";
RL Mol. Microbiol. 49:1537-1546(2003).
RN [11]
RP PROTEOLYTIC PROCESSING BY HOST FACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 61-GLY-ARG-62; 63-HIS-LYS-64; 65-ILE-GLU-66; 67-VAL-PRO-68;
RP ALA-69; PHE-70; GLY-71; GLY-72; 75-LYS-LYS-76; SER-78 AND 203-PRO-ASN-204.
RX PubMed=14526114; DOI=10.1104/pp.103.025999;
RA Jin P., Wood M.D., Wu Y., Xie Z., Katagiri F.;
RT "Cleavage of the Pseudomonas syringae type III effector AvrRpt2 requires a
RT host factor(s) common among eukaryotes and is important for AvrRpt2
RT localization in the host cell.";
RL Plant Physiol. 133:1072-1082(2003).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF CYS-122; GLY-131; GLY-141; GLU-150 AND
RP GLY-194.
RX PubMed=15000398; DOI=10.1094/mpmi.2004.17.3.313;
RA Lim M.T.S., Kunkel B.N.;
RT "Mutations in the Pseudomonas syringae avrRpt2 gene that dissociate its
RT virulence and avirulence activities lead to decreased efficiency in
RT AvrRpt2-induced disappearance of RIN4.";
RL Mol. Plant Microbe Interact. 17:313-321(2004).
RN [13]
RP VIRULENCE ACTIVITY INDEPENDENT OF RIN4, AND MUTAGENESIS OF TYR-191 AND
RP ASP-216.
RX PubMed=15546361; DOI=10.1111/j.1365-313x.2004.02251.x;
RA Lim M.T.S., Kunkel B.N.;
RT "The Pseudomonas syringae type III effector AvrRpt2 promotes virulence
RT independently of RIN4, a predicted virulence target in Arabidopsis
RT thaliana.";
RL Plant J. 40:790-798(2004).
RN [14]
RP PAMP-INDUCED SIGNALING, AND MUTAGENESIS OF CYS-122.
RX PubMed=15935761; DOI=10.1016/j.cell.2005.03.025;
RA Kim M.G., da Cunha L., McFall A.J., Belkhadir Y., DebRoy S., Dangl J.L.,
RA Mackey D.;
RT "Two Pseudomonas syringae type III effectors inhibit RIN4-regulated basal
RT defense in Arabidopsis.";
RL Cell 121:749-759(2005).
RN [15]
RP FUNCTION IN VIRULENCE.
RC STRAIN=JL1065;
RX PubMed=16042008; DOI=10.1094/mpmi-18-0626;
RA Lim M.T.S., Kunkel B.N.;
RT "The Pseudomonas syringae avrRpt2 gene contributes to virulence on
RT tomato.";
RL Mol. Plant Microbe Interact. 18:626-633(2005).
RN [16]
RP INTERFERENCE WITH RPM1 ACTIVATION.
RX PubMed=15845764; DOI=10.1073/pnas.0500792102;
RA Kim H.-S., Desveaux D., Singer A.U., Patel P., Sondek J., Dangl J.L.;
RT "The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally
RT acylated target, RIN4, from Arabidopsis membranes to block RPM1
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6496-6501(2005).
CC -!- FUNCTION: Effector protein involved in gene-for-gene resistance in
CC plants expressing RPS2. Its thiol protease activity is required for the
CC degradation of plant cell RIN4 and consequent activation of RPS2 during
CC bacterial infection. The activation of RPS2 is sufficient for the
CC induction of hypersensitive response (HR) and plant resistance.
CC Cleavage of RIN4 by AvrRpt2 also interferes with RPM1-mediated
CC resistance activated by either AvrRpm1 or AvrB. Contributes to
CC virulence in plants lacking the resistance protein RPS2 promoting
CC pathogen growth and disease symptoms. Inhibits PAMP (pathogen-
CC associated molecular patterns)-induced signaling compromising the
CC host's basal defense system. Blocks plant callose deposition, flg22 (a
CC peptide corresponding to the most conserved domain of flagellin)
CC induced accumulation of PR-1, PR-2 and PR-5 and activation of GST6
CC transcription. The mechanism of virulence is unknown, but this activity
CC is independent of ethylene and salicylic acid response pathways and
CC independent of RIN4 disappearance. {ECO:0000269|PubMed:11106023,
CC ECO:0000269|PubMed:12950919, ECO:0000269|PubMed:15000398,
CC ECO:0000269|PubMed:15746386, ECO:0000269|PubMed:16042008}.
CC -!- SUBUNIT: Interacts physically with plant cell ROC1 (Arabidopsis single-
CC domain cyclophilin) and RIN4.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10361296,
CC ECO:0000269|PubMed:11204781, ECO:0000269|PubMed:14526114}. Host cell
CC membrane {ECO:0000269|PubMed:14526114}. Note=Secreted via type III
CC secretion system (TTSS) (PubMed:14526114). Localized to the plant cell
CC membrane (PubMed:14526114).
CC -!- PTM: Autocleaved inside plant cells upon activation by cyclophilin.
CC Cleavage is crucial in subcellular location and in eliciting HR.
CC Inhibited by cyclosporin A (cyclophilin inhibitor).
CC -!- MISCELLANEOUS: Only naturally present in strain JL1065.
CC -!- MISCELLANEOUS: The C-terminal cleaved product is sufficient to trigger
CC the RPS2-dependent immune response.
CC -!- SIMILARITY: Belongs to the peptidase C70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI36145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z21715; CAA79815.2; -; Genomic_DNA.
DR EMBL; L11355; AAA71943.1; -; Genomic_DNA.
DR EMBL; AJ870977; CAI36145.1; ALT_INIT; Genomic_DNA.
DR PIR; A40613; A40613.
DR AlphaFoldDB; Q6LAD6; -.
DR SMR; Q6LAD6; -.
DR MEROPS; C70.001; -.
DR KEGG; ag:CAA79815; -.
DR PHI-base; PHI:5502; -.
DR PHI-base; PHI:979; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR022118; Peptidase_C70_AvrRpt2.
DR Pfam; PF12385; Peptidase_C70; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Direct protein sequencing; Host cell membrane;
KW Host membrane; Hydrolase; Hypersensitive response elicitation; Membrane;
KW Protease; Secreted; Thiol protease; Virulence; Zymogen.
FT PROPEP 1..71
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:10361296"
FT /id="PRO_0000043329"
FT CHAIN 72..255
FT /note="Cysteine protease avirulence protein AvrRpt2"
FT /id="PRO_0000043330"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..71
FT /note="Determinants of cleavage specificity"
FT REGION 76..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Nucleophile"
FT ACT_SITE 208
FT ACT_SITE 226
FT SITE 71..72
FT /note="Cleavage; by autolysis"
FT MUTAGEN 61..62
FT /note="GR->AA: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 63..64
FT /note="HK->AA: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 65..66
FT /note="IE->AA: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 67..68
FT /note="VP->AA: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 69
FT /note="A->S: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 70
FT /note="F->A: Partially cleaved. Mainly localized to the
FT chloroplast."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 71
FT /note="G->A: Partially cleaved. Mainly localized to the
FT chloroplast."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 72
FT /note="G->A: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 75..76
FT /note="KK->LL: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 78
FT /note="S->R: No effect in cleavage."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 122
FT /note="C->A: Abolishes the normal in planta processing,
FT RIN4 degradation and fails to elicit RPS2-dependent defense
FT response. Loses its ability to inhibit PAMP-induced growth
FT suppression."
FT /evidence="ECO:0000269|PubMed:11204781,
FT ECO:0000269|PubMed:12950919, ECO:0000269|PubMed:15000398,
FT ECO:0000269|PubMed:15935761"
FT MUTAGEN 122
FT /note="C->Y: Deficient in both cleavage and recognition by
FT RPS2 plant cells. Fails to elicit RPS2-dependent defense
FT response. Localized to the chloroplast."
FT /evidence="ECO:0000269|PubMed:11204781,
FT ECO:0000269|PubMed:12950919, ECO:0000269|PubMed:15000398,
FT ECO:0000269|PubMed:15935761"
FT MUTAGEN 131
FT /note="G->D: Fails to elicit RPS2-dependent defense
FT response."
FT /evidence="ECO:0000269|PubMed:11204781,
FT ECO:0000269|PubMed:15000398"
FT MUTAGEN 141
FT /note="G->R: Deficient in both cleavage and recognition by
FT RPS2 plant cells. Fails to elicit RPS2-dependent defense
FT response."
FT /evidence="ECO:0000269|PubMed:11204781,
FT ECO:0000269|PubMed:15000398"
FT MUTAGEN 150
FT /note="E->S: No effect in cleavage and fails to recognize
FT RPS2 plant cells."
FT /evidence="ECO:0000269|PubMed:15000398"
FT MUTAGEN 191
FT /note="Y->C: Fails to induce RIN4 disappearance and
FT avirulence but retains virulence activity."
FT /evidence="ECO:0000269|PubMed:15546361"
FT MUTAGEN 194
FT /note="G->E: Deficient in both cleavage and recognition by
FT RPS2 plant cells. Fails to elicit RPS2-dependent defense
FT response."
FT /evidence="ECO:0000269|PubMed:11204781,
FT ECO:0000269|PubMed:15000398"
FT MUTAGEN 194
FT /note="G->R: Fails to elicit RPS2-dependent defense
FT response."
FT /evidence="ECO:0000269|PubMed:11204781,
FT ECO:0000269|PubMed:15000398"
FT MUTAGEN 203..204
FT /note="PN->RS: No effect in cleavage and fails to recognize
FT RPS2 plant cells."
FT /evidence="ECO:0000269|PubMed:14526114"
FT MUTAGEN 208
FT /note="H->A: Abolishes the normal in planta processing,
FT RIN4 degradation and fails to elicit RPS2-dependent defense
FT response."
FT /evidence="ECO:0000269|PubMed:12950919"
FT MUTAGEN 216
FT /note="D->E: Fails to induce RIN4 disappearance and
FT avirulence but retains virulence activity."
FT /evidence="ECO:0000269|PubMed:15546361"
FT MUTAGEN 226
FT /note="D->A: Produces an unstable protein and fails to
FT elicit RPS2-dependent defense response."
FT /evidence="ECO:0000269|PubMed:12950919"
FT CONFLICT 151
FT /note="G -> A (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28158 MW; F206185E51CEEC28 CRC64;
MKIAPVAINH SPLSREVPSH AAPTQAKQTN LQSEAGDLDA RKSSASSPET RALLATKTVL
GRHKIEVPAF GGWFKKKSSK HETGGSSANA DSSSVASDST EKPLFRLTHV PYVSQGNERM
GCWYACARMV GHSVEAGPRL GLPELYEGRE GPAGLQDFSD VERFIHNEGL TRVDLPDNER
FTHEELGALL YKHGPIIFGW KTPNDSWHMS VLTGVDKETS SITFHDPRQG PDLAMPLDYF
NQRLAWQVPH AMLYR
