YOPT_YERPE
ID YOPT_YERPE Reviewed; 322 AA.
AC O68703;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cysteine protease YopT;
DE EC=3.4.22.-;
GN Name=yopT; OrderedLocusNames=YPCD1.20, y5059, y0065, YP_pCD67;
OS Yersinia pestis.
OG Plasmid pCD1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA Blattner F.R.;
RT "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT Yersinia pestis KIM5.";
RL Infect. Immun. 66:4611-4623(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA Brubaker R.R., Garcia E.;
RT "Structural organization of virulence-associated plasmids of Yersinia
RT pestis.";
RL J. Bacteriol. 180:5192-5202(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [5]
RP ENZYME ACTIVITY, FUNCTION, INTERACTION WITH HUMAN ARHA, AND MUTAGENESIS OF
RP CYS-139; TRP-146; ARG-165; HIS-258; ASP-274; GLU-279 AND SER-300.
RX PubMed=12062101; DOI=10.1016/s0092-8674(02)00766-3;
RA Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.;
RT "A Yersinia effector and a Pseudomonas avirulence protein define a family
RT of cysteine proteases functioning in bacterial pathogenesis.";
RL Cell 109:575-588(2002).
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:12062101}.
CC -!- SUBUNIT: Interacts with human ARHA. {ECO:0000269|PubMed:12062101}.
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.
CC -!- SIMILARITY: Belongs to the peptidase C58 family. {ECO:0000305}.
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DR EMBL; AF074612; AAC69833.1; -; Genomic_DNA.
DR EMBL; AF053946; AAC62582.1; -; Genomic_DNA.
DR EMBL; AL117189; CAB54897.1; -; Genomic_DNA.
DR EMBL; AE017043; AAS58582.1; -; Genomic_DNA.
DR PIR; T43601; T43601.
DR RefSeq; NP_395155.1; NC_003131.1.
DR RefSeq; NP_857758.1; NC_004836.1.
DR RefSeq; NP_857958.1; NC_004839.1.
DR RefSeq; WP_002213006.1; NZ_WUCM01000119.1.
DR AlphaFoldDB; O68703; -.
DR SMR; O68703; -.
DR IntAct; O68703; 1.
DR MINT; O68703; -.
DR STRING; 214092.5832441; -.
DR MEROPS; C58.001; -.
DR DNASU; 1149322; -.
DR EnsemblBacteria; AAS58582; AAS58582; YP_pCD67.
DR KEGG; ype:YPCD1.20; -.
DR KEGG; ypm:YP_pCD67; -.
DR PATRIC; fig|214092.21.peg.24; -.
DR eggNOG; COG3177; Bacteria.
DR HOGENOM; CLU_073575_0_0_6; -.
DR OMA; QSTMTEY; -.
DR Proteomes; UP000000815; Plasmid pCD1.
DR Proteomes; UP000001019; Plasmid pCD1.
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; Reference proteome; Secreted; Thiol protease;
KW Virulence.
FT CHAIN 1..322
FT /note="Cysteine protease YopT"
FT /id="PRO_0000192513"
FT ACT_SITE 139
FT ACT_SITE 258
FT ACT_SITE 274
FT MUTAGEN 139
FT /note="C->S: Loss of function; abolishes the cleavage of
FT ARHA."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 146
FT /note="W->A: Abolishes cytotoxicity."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 165
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 258
FT /note="H->A: Loss of function; abolishes the cleavage of
FT ARHA."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 274
FT /note="D->A: Loss of function; abolishes the cleavage of
FT ARHA."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 279
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 300
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:12062101"
SQ SEQUENCE 322 AA; 36308 MW; 2B964F437FBC8A63 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 WFTNSFWGNS
MYHYPLGVGQ RFRVLTFDSK EV
