ID   AVRV_XANEU              Reviewed;         373 AA.
AC   Q08678;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Serine/threonine-protein acetyltransferase AvrRxv {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:O68718};
DE   AltName: Full=Avirulence protein AvrRxv;
DE   AltName: Full=TAL effector protein AvrRxv;
GN   Name=avrRxv;
OS   Xanthomonas euvesicatoria.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=456327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=75-3;
RX   PubMed=8274773; DOI=10.1094/mpmi-6-616;
RA   Whalen M.C., Wang J.F., Carland F.M., Heiskell M.E., Dahlbeck D.,
RA   Minsavage G.V., Jones J.B., Scott J.W., Stall R.E., Staskawicz B.J.;
RT   "Avirulence gene avrRxv from Xanthomonas campestris pv. vesicatoria
RT   specifies resistance on tomato line Hawaii 7998.";
RL   Mol. Plant Microbe Interact. 6:616-627(1993).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=75-3;
RX   PubMed=10430949; DOI=10.1073/pnas.96.16.9368;
RA   Rossier O., Wengelnik K., Hahn K., Bonas U.;
RT   "The Xanthomonas Hrp type III system secretes proteins from plant and
RT   mammalian bacterial pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9368-9373(1999).
CC   -!- FUNCTION: Serine/threonine-protein acetyltransferase translocated into
CC       infected cells, which mediates acetylation of serine and threonine
CC       residues of host target proteins (By similarity). Induces a
CC       hypersensitive response (HR) in tomato cv. Hawaii 7998 (S.lycopersicum)
CC       carrying the resistance gene (PubMed:10430949, PubMed:8274773).
CC       {ECO:0000250|UniProtKB:O68718, ECO:0000269|PubMed:10430949,
CC       ECO:0000303|PubMed:8274773}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-
CC         [protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:141025; Evidence={ECO:0000250|UniProtKB:O68718};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC         Evidence={ECO:0000250|UniProtKB:O68718};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:141128; Evidence={ECO:0000250|UniProtKB:O68718};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC         Evidence={ECO:0000250|UniProtKB:O68718};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10430949}.
CC       Note=Probably secreted via a type III secretion system (TTSS).
CC       {ECO:0000303|PubMed:10430949}.
CC   -!- DISRUPTION PHENOTYPE: No longer inhibits growth of bacteria encoding
CC       this gene on tomato cv. Hawaii 7998. {ECO:0000269|PubMed:8274773}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC       {ECO:0000305}.
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DR   EMBL; L20423; AAA27595.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q08678; -.
DR   SMR; Q08678; -.
DR   MEROPS; C55.006; -.
DR   OMA; ICHDSAQ; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005083; Ser/Thr_AcTrfase.
DR   Pfam; PF03421; Acetyltransf_14; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Secreted; Transferase; Virulence.
FT   CHAIN           1..373
FT                   /note="Serine/threonine-protein acetyltransferase AvrRxv"
FT                   /id="PRO_0000064776"
FT   REGION          29..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..66
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   BINDING         180
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   BINDING         239..240
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT   BINDING         308..311
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VE93"
SQ   SEQUENCE   373 AA;  42021 MW;  12FB6B01EA7F9E43 CRC64;
     MCDSIRVQFR SIQKMVVKMK KFFRSLGVGG SSSSRFQHHI PEADSAPSSK ASTPPASPPP
     DSPPSNSAFS ALPTRPRKKA EALSDAVESR GHLAPPSLVS YANATLDQLR RNEPISESLR
     LMDIENLPHL VRSYDNRLNN LNLRSFDTPG QFLHDLSRWH KTGLPLRAVV RLDEDPRRWH
     RVAFDVRNHE SGHTTIIALE PASAYNPDHM PGFVKMRENL TSQFGRKISF AVIEAEALKS
     IGGCVIFSLD YALAAYQERS TFDQWHKDLR KKGNIKGMTP ESQHLNELGV YLLKGTRLLP
     ANFYKHAHSR RTIDELEADQ PGASGTDVRS GRAAVYKESL SRRLEEFQVQ RDKTYSMSIE
     ASRARKIRHA LES