ID   YOPT1_YEREN             Reviewed;         322 AA.
AC   P0C2N1; Q84GU1; Q93KV0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Cysteine protease yopT1;
DE            EC=3.4.22.-;
GN   Name=yopT1;
OS   Yersinia enterocolitica.
OG   Plasmid pYVa127/90.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A127/90 / Serotype O:8 / Biotype 1B; PLASMID=pYVa127/90;
RX   PubMed=14527656; DOI=10.1016/s0923-2508(03)00147-5;
RA   Foultier B., Cornelis G.R.;
RT   "DNA sequence and analysis of the pYVa127/90 virulence plasmid of Yersinia
RT   enterocolitica strain A127/90.";
RL   Res. Microbiol. 154:553-557(2003).
RN   [2]
RP   FUNCTION.
RC   STRAIN=Serotype O:8;
RX   PubMed=10506187; DOI=10.1074/jbc.274.41.29289;
RA   Zumbihl R., Aepfelbacher M., Andor A., Jacobi C.A., Ruckdeschel K.,
RA   Rouot B., Heesemann J.;
RT   "The cytotoxin YopT of Yersinia enterocolitica induces modification and
RT   cellular redistribution of the small GTP-binding protein RhoA.";
RL   J. Biol. Chem. 274:29289-29293(1999).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=JB580v / Serotype O:8;
RX   PubMed=11705930; DOI=10.1128/iai.69.12.7535-7543.2001;
RA   Sorg I., Goehring U.M., Aktories K., Schmidt G.;
RT   "Recombinant Yersinia YopT leads to uncoupling of RhoA-effector
RT   interaction.";
RL   Infect. Immun. 69:7535-7543(2001).
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:10506187,
CC       ECO:0000269|PubMed:11705930}.
CC   -!- SUBUNIT: Interacts with human ARHA.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11705930}. 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; AY150843; AAN37539.1; -; Genomic_DNA.
DR   RefSeq; NP_783657.1; NC_004564.1.
DR   RefSeq; WP_005176719.1; NZ_NWMR01000110.1.
DR   AlphaFoldDB; P0C2N1; -.
DR   SMR; P0C2N1; -.
DR   MEROPS; C58.001; -.
DR   OrthoDB; 1445297at2; -.
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_0000192512"
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;  36201 MW;  4B46FBB9F8A308CB CRC64;
     MDSIHGHYHI QLSNYSAGEN LQSATLTEGV IGAHRVKVET ALSHSNRQKK LSATIKHNQS
     SRSMLDRKLT SDGKVNQRSS FTFSMIMYRM IHFVLSTRVP AVRESVANYG GNINFKFAQT
     KGAFLHQIIK HSDTARGACE ALCAHWIRSH AQGQSLFDQL YVGGRKGKFQ IDTLYSIKQL
     QIDGCKADVD QDEVTLDWLK KNGISERMIE RHCLLPTVDV TGTTGSEGPD QLLNAILDTH
     GIGYGYKKIY LSGQMSGHTI AAYVNENSGV TFFDPNFGEF HFSDKEQFSK WFTNSFWENS
     MYHYPLGVGQ SFSVFTFDSK EV