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YOPT1_YERE8
ID   YOPT1_YERE8             Reviewed;         322 AA.
AC   A1JU65; Q84GU1; Q93KV0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cysteine protease yopT1;
DE            EC=3.4.22.-;
GN   Name=yopT1; OrderedLocusNames=YEP0005;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OG   Plasmid pYVe8081.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11402007; DOI=10.1128/iai.69.7.4627-4638.2001;
RA   Snellings N.J., Popek M., Lindler L.E.;
RT   "Complete DNA sequence of Yersinia enterocolitica serotype 0:8 low-calcium-
RT   response plasmid reveals a new virulence plasmid-associated replicon.";
RL   Infect. Immun. 69:4627-4638(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Cysteine protease, which is translocated into infected cells
CC       and plays a central role in pathogenesis by cleaving the C-terminus end
CC       of the human small GTPase RhoA/ARHA, a regulator of cytoskeleton. Once
CC       cleaved, ARHA loses its lipid modification, and is released from the
CC       cell membrane, leading to the subsequent disruption of actin
CC       cytoskeleton of the host cell (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with human ARHA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=In infected cells, it is
CC       cytoplasmic. Translocated into the host cell by the type III secretion
CC       apparatus with the help of the SycT chaperone (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C58 family. {ECO:0000305}.
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DR   EMBL; AF336309; AAK69206.1; -; Genomic_DNA.
DR   EMBL; AM286416; CAL10029.1; -; Genomic_DNA.
DR   RefSeq; NP_863507.1; NC_005017.1.
DR   RefSeq; WP_011117629.1; NC_008791.1.
DR   RefSeq; YP_001004061.1; NC_008791.1.
DR   AlphaFoldDB; A1JU65; -.
DR   SMR; A1JU65; -.
DR   STRING; 393305.YEP0005; -.
DR   MEROPS; C58.001; -.
DR   EnsemblBacteria; CAL10029; CAL10029; YEP0005.
DR   KEGG; yen:YEP0005; -.
DR   PATRIC; fig|393305.7.peg.5; -.
DR   eggNOG; COG3177; Bacteria.
DR   HOGENOM; CLU_073575_0_0_6; -.
DR   OMA; QSTMTEY; -.
DR   PRO; PR:A1JU65; -.
DR   Proteomes; UP000000642; Plasmid pYVe8081.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003951; Peptidase_C58.
DR   InterPro; IPR006473; Peptidase_C58_Yopt.
DR   Pfam; PF03543; Peptidase_C58; 1.
DR   PRINTS; PR01376; BACSURFANTGN.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   TIGRFAMs; TIGR01586; yopT_cys_prot; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Protease; Secreted; Thiol protease; Virulence.
FT   CHAIN           1..322
FT                   /note="Cysteine protease yopT1"
FT                   /id="PRO_0000281776"
FT   REGION          42..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  36082 MW;  EE3F60CC5B8CBF48 CRC64;
     MDSIHGHYHI QLSNYSAGEN LQSATPPEGV IGAHRVKVET ALSHSNRQKK LSATIKHNQS
     SRSMLDRKLT SDGKVNQRSS FTFSMIMYRM IHFVLSTRVP AVRESVANYG GNINFKFAQT
     KGAFLHQIIK HSDTARGACE ALCAHWIRSH AQGQSLFDQL YVGGRKGKFQ IDTLYSIKQL
     QIDGCKADVD QDEVTLDWLK KNGISERMIE RHCLLPTVDV TGTTGSEGPD QLLNAILDTN
     GIGYGYKKIS LSGQMSGHTI AAYVNENSGV TFFDPNFGEF HFSDKEKFSK WFTNSFWENS
     MYHYPLGVGQ SFSVFTFDSK EV
 
 
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