ID   YOPT_YERPS              Reviewed;         322 AA.
AC   Q93RN4; Q663M5;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cysteine protease YopT;
DE            EC=3.4.22.-;
GN   Name=yopT; OrderedLocusNames=pYV0041;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OG   Plasmid pYV36, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Y36; PLASMID=pYV36;
RX   PubMed=11518333; DOI=10.1078/0723-2020-00040;
RA   Arnold T., Hensel A., Hagen R., Aleksic S., Neubauer H., Scholz H.C.;
RT   "A highly specific one-step PCR - assay for the rapid discrimination of
RT   enteropathogenic Yersinia enterocolitica from pathogenic Yersinia
RT   pseudotuberculosis and Yersinia pestis.";
RL   Syst. Appl. Microbiol. 24:285-289(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953; PLASMID=pYV;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN   [3]
RP   BIOCHEMICAL CHARACTERIZATION, FUNCTION, AND MUTAGENESIS OF CYS-139.
RX   PubMed=12538863; DOI=10.1073/pnas.252770599;
RA   Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.;
RT   "Biochemical characterization of the Yersinia YopT protease: cleavage site
RT   and recognition elements in Rho GTPases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003).
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. {ECO:0000269|PubMed:12538863}.
CC   -!- SUBUNIT: Interacts with human ARHA.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In infected cells,
CC       it is cytoplasmic. Translocated into the host cell by the type III
CC       secretion apparatus with the help of the SycT chaperone (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C58 family. {ECO:0000305}.
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DR   EMBL; AJ304833; CAC39270.1; -; Genomic_DNA.
DR   EMBL; BX936399; CAF25384.1; -; Genomic_DNA.
DR   RefSeq; WP_011191374.1; NZ_CP009711.1.
DR   AlphaFoldDB; Q93RN4; -.
DR   SMR; Q93RN4; -.
DR   MEROPS; C58.001; -.
DR   EnsemblBacteria; CAF25384; CAF25384; pYV0041.
DR   GeneID; 66841056; -.
DR   KEGG; ypo:BZ17_4198; -.
DR   KEGG; yps:pYV0041; -.
DR   PATRIC; fig|273123.14.peg.4424; -.
DR   OMA; QSTMTEY; -.
DR   Proteomes; UP000001011; Plasmid pYV.
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   1: Evidence at protein level;
KW   Hydrolase; Plasmid; Protease; Secreted; Thiol protease; Virulence.
FT   CHAIN           1..322
FT                   /note="Cysteine protease YopT"
FT                   /id="PRO_0000192514"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         139
FT                   /note="C->S: Abolishes the cleavage of ARHA."
FT                   /evidence="ECO:0000269|PubMed:12538863"
FT   CONFLICT        2
FT                   /note="N -> D (in Ref. 1; CAC39270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147..148
FT                   /note="IR -> DQ (in Ref. 1; CAC39270)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  36366 MW;  28A67C437FBC8A63 CRC64;
     MNSIHGHYHI QLSNYSAGEN LQSATLTEGV IGAHRVKVET ALSHSNLQKK LSATIKHNQS
     GRSMLDRKLT SDGKANQRSS FTFSMIMYRM IHFVLSTRVP AVRESVANYG GNINFKFAQT
     KGAFLHKIIK HSDTASGVCE ALCAHWIRSH AQGQSLFDQL YVGGRKGKFQ IDTLYSIKQL
     QIDGCKADVD QDEVTLDWFK KNGISERMIE RHCLLRPVDV TGTTESEGLD QLLNAILDTH
     GIGYGYKKIH LSGQMSAHAI AAYVNEKSGV TFFDPNFGEF HFSDKEKFRK WFTNSFWDNS
     MYHYPLGVGQ RFRVLTFDSK EV