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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
 
 
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