SPVC_SALCH
ID SPVC_SALCH Reviewed; 241 AA.
AC P15805; Q5J4C7; Q7DIJ7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 107.
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;
GN Name=spvC; OrderedLocusNames=SCH_V05;
OS Salmonella choleraesuis (strain SC-B67).
OG Plasmid pKDSc50, and Plasmid pSCV50.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RF-1; PLASMID=pKDSc50;
RX PubMed=2315022; DOI=10.1093/nar/18.4.1055;
RA Matsui H., Kawahara K., Terakado N., Danbara H.;
RT "Nucleotide sequence of a gene encoding a 29 kDa polypeptide in mba region
RT of the virulence plasmid, pKDSC50, of Salmonella choleraesuis.";
RL Nucleic Acids Res. 18:1055-1055(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RF-1; PLASMID=pKDSc50;
RX PubMed=11254626; DOI=10.1128/iai.69.4.2612-2620.2001;
RA Haneda T., Okada N., Nakazawa N., Kawakami T., Danbara H.;
RT "Complete DNA sequence and comparative analysis of the 50-kilobase
RT virulence plasmid of Salmonella enterica serovar Choleraesuis.";
RL Infect. Immun. 69:2612-2620(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67; PLASMID=pSCV50;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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 -!- SIMILARITY: Belongs to the phosphothreonine lyase family.
CC {ECO:0000305}.
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DR EMBL; X51453; CAA35819.1; -; Genomic_DNA.
DR EMBL; AB040415; BAB20512.1; -; Genomic_DNA.
DR EMBL; AY509003; AAS58878.1; -; Genomic_DNA.
DR PIR; S08402; S08402.
DR RefSeq; NP_073229.1; NC_002638.1.
DR RefSeq; WP_010904474.1; NC_006855.1.
DR RefSeq; YP_001598063.1; NC_010119.1.
DR AlphaFoldDB; P15805; -.
DR SMR; P15805; -.
DR EnsemblBacteria; AAS58878; AAS58878; SCH_V05.
DR KEGG; sec:SCH_V05; -.
DR HOGENOM; CLU_100525_0_0_6; -.
DR OMA; RVDQQSR; -.
DR Proteomes; UP000000538; Plasmid pSCV50.
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_0000221667"
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; 27668 MW; B0B2DD1FF726C65D CRC64;
MPINRPNLNL HIPPLNIVAA YDGAEIPSTN KHLKNNFNSL HNQMRKMPLS HFKEALDVPD
YSGMRQSGFF AMSQGFQLNN HGYDVFIHAR RESPQSLGKF AGDKFHISVL RDMVPQAFQA
LSGLLFSEDS PVDKWKVTDM EKVVQQARVS LGAQFTLYIK PDQENSQYSA SFLHKTRQFI
ECLESRLSEN GVISGQCPES DVHPENWKYL SYRNELRSGR DGGEMQRQAL REEPFYRLMT
E