ID   YOPT_YEREN              Reviewed;         322 AA.
AC   P27475; Q9S4Y3;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cysteine protease YopT;
DE            EC=3.4.22.-;
GN   Name=yopT;
OS   Yersinia enterocolitica.
OG   Plasmid pYVe227, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=W22703 / Serotype O:9 / Biotype 2; PLASMID=pYVe227;
RX   PubMed=9723929; DOI=10.1046/j.1365-2958.1998.00992.x;
RA   Iriarte M., Cornelis G.R.;
RT   "YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of
RT   host cells.";
RL   Mol. Microbiol. 29:915-929(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
RC   STRAIN=439-80 / Serotype O:9; PLASMID=pYV;
RX   PubMed=2129533; DOI=10.1128/iai.58.9.2840-2849.1990;
RA   Michiels T., Wattiau P., Brasseur R., Ruysschaert J.M., Cornelis G.;
RT   "Secretion of Yop proteins by Yersiniae.";
RL   Infect. Immun. 58:2840-2849(1990).
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 {ECO:0000269|PubMed:9723929}. Note=In
CC       infected cells, it is cytoplasmic. Translocated into the host cell by
CC       the type III secretion apparatus with the help of the SycT chaperone.
CC   -!- SIMILARITY: Belongs to the peptidase C58 family. {ECO:0000305}.
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DR   EMBL; AF102990; AAD16808.1; -; Genomic_DNA.
DR   EMBL; X52753; CAA36963.1; -; Genomic_DNA.
DR   PIR; S14239; S14239.
DR   RefSeq; NP_052385.1; NC_002120.1.
DR   RefSeq; WP_010891203.1; NZ_SJZK01000009.1.
DR   AlphaFoldDB; P27475; -.
DR   SMR; P27475; -.
DR   MEROPS; C58.001; -.
DR   PATRIC; fig|630.129.peg.4336; -.
DR   OMA; QSTMTEY; -.
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 YopT"
FT                   /id="PRO_0000192511"
FT   REGION          43..72
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;  36439 MW;  E1B14582A2AFF15F CRC64;
     MDSIHGHYHI QLSNYSAGEN LQSATLTEGV IGAHRVKVET ALSHSNRQKK LSATIKHNQS
     SRSMLDRKLT SDGKANQRSS FTFSMIMYRM IHFVLSTRVP AVRESVANYG GNINFKFAQT
     KGAFLHQIIK HSDTASGVCE ALCAHWIWSH AQGQSLFDQL YVGGRKGKFQ IDTLYSIKQL
     QIDGCKADVD QDEVTLDWFK KKGISERMIE RHCLLRPVDV TGTTESEGPD QLLNAILDTH
     GIGYGYKKIY LSGQMSAHAI AAYVNEKSGV TFFDPNFGEF HFSDKEKFRK WFTNSFWENS
     MYHYPLGVGQ RFSVLTFDSK EV