ID   SPVC_SALDU              Reviewed;         241 AA.
AC   P0A2N0; P21456;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=MAPK phosphothreonine lyase;
DE            EC=4.2.3.-;
DE   AltName: Full=27.5 kDa virulence protein;
DE   AltName: Full=Secreted effector protein SpvC;
DE   AltName: Full=Virulence protein SpvC;
GN   Name=spvC; Synonyms=mkaD, vsdD;
OS   Salmonella dublin.
OG   Plasmid pSDL2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=98360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Lane;
RX   PubMed=2041471; DOI=10.1111/j.1365-2958.1991.tb02111.x;
RA   Krause M., Roudier C., Fierer J., Harwood J., Guiney D.;
RT   "Molecular analysis of the virulence locus of the Salmonella dublin plasmid
RT   pSDL2.";
RL   Mol. Microbiol. 5:307-316(1991).
RN   [2]
RP   DISRUPTION PHENOTYPE UPON MOUSE INFECTION.
RC   STRAIN=Lane;
RX   PubMed=1400193; DOI=10.1128/jb.174.20.6418-6423.1992;
RA   Roudier C., Fierer J., Guiney D.G.;
RT   "Characterization of translation termination mutations in the spv operon of
RT   the Salmonella virulence plasmid pSDL2.";
RL   J. Bacteriol. 174:6418-6423(1992).
CC   -!- FUNCTION: Secreted effector that irreversibly inactivates host MAP
CC       kinases by catalyzing the dephosphorylation of the phosphothreonine
CC       residue in the pT-X-pY motif present in MAPKs, via a beta-elimination
CC       reaction leading to a dehydrobutyrine residue. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Decreased virulence in mice.
CC       {ECO:0000269|PubMed:1400193}.
CC   -!- MISCELLANEOUS: In Salmonella spp. the spv gene cluster is encoded on a
CC       highly transmissible plasmid.
CC   -!- SIMILARITY: Belongs to the phosphothreonine lyase family.
CC       {ECO:0000305}.
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DR   EMBL; X56727; CAA40050.1; -; Genomic_DNA.
DR   RefSeq; WP_001122242.1; NZ_VDCP01000013.1.
DR   RefSeq; YP_001716114.1; NC_010422.1.
DR   RefSeq; YP_003264391.1; NC_013437.1.
DR   RefSeq; YP_003864188.1; NC_014476.2.
DR   RefSeq; YP_006954899.1; NC_019106.1.
DR   RefSeq; YP_006955267.1; NC_019108.1.
DR   RefSeq; YP_006955407.1; NC_019109.1.
DR   RefSeq; YP_006955574.1; NC_019001.1.
DR   AlphaFoldDB; P0A2N0; -.
DR   SMR; P0A2N0; -.
DR   PHI-base; PHI:4517; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2430.10; -; 1.
DR   InterPro; IPR003519; OspF/SpvC.
DR   InterPro; IPR038498; OspF/SpvC_sf.
DR   Pfam; PF03536; VRP3; 1.
DR   PRINTS; PR01342; SALVRPPROT.
PE   3: Inferred from homology;
KW   Lyase; Plasmid; Secreted; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..241
FT                   /note="MAPK phosphothreonine lyase"
FT                   /id="PRO_0000221669"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   241 AA;  27646 MW;  77625271D78F8814 CRC64;
     MPINRPNLNL NIPPLNIVAA YDGAEIPSTN KHLKNNFNSL HNQMRKMPVS HFKEALDVPD
     YSGMRQSGFF AMSQGFQLNN HGYDVFIHAR RESPQSQGKF AGDKFHISVL RDMVPQAFQA
     LSGLLFSEDS PVDKWKVTDM EKVVQQARVS LGAQFTLYIK PDQENSQYSA SFLHKTRQFI
     ECLESRLSEN GVISGQCPES DVHPENWKYL SYRNELRSGR DGGEMQRQAL REEPFYRLMT
     E