(data stored in ACNUC9435 zone)

SWISSPROT: YOPH_YERPS

ID   YOPH_YERPS              Reviewed;         468 AA.
AC   P08538; Q663H2;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 3.
DT   11-DEC-2019, entry version 144.
DE   RecName: Full=Tyrosine-protein phosphatase YopH;
DE            EC=3.1.3.48;
DE   AltName: Full=Virulence protein;
GN   Name=yopH; Synonyms=yop2b; OrderedLocusNames=pYV0094;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OG   Plasmid pIB1, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX   PubMed=2837614; DOI=10.1111/j.1365-2958.1988.tb00025.x;
RA   Boelin I., Wolf-Watz H.;
RT   "The plasmid-encoded Yop2b protein of Yersinia pseudotuberculosis is a
RT   virulence determinant regulated by calcium and temperature at the level of
RT   transcription.";
RL   Mol. Microbiol. 2:237-245(1988).
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   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS.
RX   PubMed=1705028; DOI=10.1073/pnas.88.4.1187;
RA   Bliska J.B., Guan K.L., Dixon J.E., Falkow S.;
RT   "Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia
RT   virulence determinant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1187-1191(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-129.
RX   PubMed=11737640; DOI=10.1046/j.0950-382x.2001.02711.x;
RA   Smith C.L., Khandelwal P., Keliikuli K., Zuiderweg E.R., Saper M.A.;
RT   "Structure of the type III secretion and substrate-binding domain of
RT   Yersinia YopH phosphatase.";
RL   Mol. Microbiol. 42:967-979(2001).
RN   [5]
RP   STRUCTURE BY NMR OF 1-129.
RX   PubMed=12234185; DOI=10.1021/bi026333l;
RA   Khandelwal P., Keliikuli K., Smith C.L., Saper M.A., Zuiderweg E.R.;
RT   "Solution structure and phosphopeptide binding to the N-terminal domain of
RT   Yersinia YopH: comparison with a crystal structure.";
RL   Biochemistry 41:11425-11437(2002).
CC   -!- FUNCTION: Essential virulence determinant. This protein is a protein
CC       tyrosine phosphatase. The essential function of YopH in Yersinia
CC       pathogenesis is host-protein dephosphorylation. It contributes to the
CC       ability of the bacteria to resist phagocytosis by peritoneal
CC       macrophages. {ECO:0000269|PubMed:1705028}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044, ECO:0000269|PubMed:1705028};
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion
CC       system.
CC   -!- INDUCTION: At 37 degrees Celsius in the absence of calcium.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
DR   EMBL; Y00551; CAA68629.1; -; Genomic_DNA.
DR   EMBL; BX936399; CAF25437.1; -; Genomic_DNA.
DR   PIR; S01054; S01054.
DR   RefSeq; WP_002213278.1; NZ_CP009711.1.
DR   PDB; 1K46; X-ray; 2.20 A; A=1-129.
DR   PDB; 1M0V; NMR; -; A=1-129.
DR   PDBsum; 1K46; -.
DR   PDBsum; 1M0V; -.
DR   SMR; P08538; -.
DR   IntAct; P08538; 1.
DR   ChEMBL; CHEMBL5835; -.
DR   PRIDE; P08538; -.
DR   EnsemblBacteria; CAF25437; CAF25437; pYV0094.
DR   GeneID; 39573291; -.
DR   KEGG; ypo:BZ17_4241; -.
DR   KEGG; yps:pYV0094; -.
DR   PATRIC; fig|273123.14.peg.4476; -.
DR   HOGENOM; HOG000219626; -.
DR   KO; K23474; -.
DR   OMA; HNLNNYE; -.
DR   EvolutionaryTrace; P08538; -.
DR   PRO; PR:P08538; -.
DR   Proteomes; UP000001011; Plasmid pYV.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1570.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR015103; ProtTyrPase_YopH_N.
DR   InterPro; IPR036484; ProtTyrPase_YopH_N_sf.
DR   InterPro; IPR000242; PTPase_domain.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR003546; Tyr_Pase_SptP/YopH.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   Pfam; PF09013; YopH_N; 1.
DR   PRINTS; PR01371; BACYPHPHTASE.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF64449; SSF64449; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P08538.
DR   SWISS-2DPAGE; P08538.
KW   3D-structure; Hydrolase; Plasmid; Protein phosphatase; Secreted; Virulence.
FT   CHAIN           1..468
FT                   /note="Tyrosine-protein phosphatase YopH"
FT                   /id="PRO_0000094862"
FT   DOMAIN          152..461
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        403
FT                   /note="Phosphocysteine intermediate"
FT   MUTAGEN         403
FT                   /note="C->A: Abolishes PTPase activity and significantly
FT                   reduces the virulence."
FT                   /evidence="ECO:0000269|PubMed:1705028"
FT   CONFLICT        211
FT                   /note="A -> R (in Ref. 1; CAA68629)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..17
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   STRAND          24..34
FT                   /evidence="ECO:0000244|PDB:1M0V"
FT   HELIX           44..46
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   HELIX           50..62
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   TURN            63..65
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   HELIX           70..82
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   STRAND          88..94
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   STRAND          97..106
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   HELIX           110..124
FT                   /evidence="ECO:0000244|PDB:1K46"
FT   STRAND          126..128
FT                   /evidence="ECO:0000244|PDB:1M0V"
SQ   SEQUENCE   468 AA;  50869 MW;  9EA639C08197EA81 CRC64;
     MNLSLSDLHR QVSRLVQQES GDCTGKLRGN VAANKETTFQ GLTIASGARE SEKVFAQTVL
     SHVANVVLTQ EDTAKLLQST VKHNLNNYDL RSVGNGNSVL VSLRSDQMTL QDAKVLLEAA
     LRQESGARGH VSSHSHSALH APGTPVREGL RSHLDPRTPP LPPRERPHTS GHHGAGEARA
     TAPSTVSPYG PEARAELSSR LTTLRNTLAP ATNDPRYLQA CGGEKLNRFR DIQCCRQTAV
     RADLNANYIQ VGNTRTIACQ YPLQSQLESH FRMLAENRTP VLAVLASSSE IANQRFGMPD
     YFRQSGTYGS ITVESKMTQQ VGLGDGIMAD MYTLTIREAG QKTISVPVVH VGNWPDQTAV
     SSEVTKALAS LVDQTAETKR NMYESKGSSA VGDDSKLRPV IHCRAGVGRT AQLIGAMCMN
     DSRNSQLSVE DMVSQMRVQR NGIMVQKDEQ LDVLIKLAEG QGRPLLNS
//

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