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Database: UniProt
Entry: P15273
LinkDB: P15273
Original site: P15273 
ID   YOPH_YEREN              Reviewed;         468 AA.
AC   P15273;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   26-NOV-2014, entry version 116.
DE   RecName: Full=Tyrosine-protein phosphatase YopH;
DE            EC=3.1.3.48;
DE   AltName: Full=Virulence protein;
GN   Name=yopH; Synonyms=yop51;
OS   Yersinia enterocolitica.
OG   Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W22703 / Serotype O:9 / Biotype 2;
RX   PubMed=3244311; DOI=10.1016/0882-4010(88)90006-X;
RA   Michiels T., Cornelis G.;
RT   "Nucleotide sequence and transcription analysis of yop51 from Yersinia
RT   enterocolitica W22703.";
RL   Microb. Pathog. 5:449-459(1988).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2166336; DOI=10.1126/science.2166336;
RA   Guan K.L., Dixon J.E.;
RT   "Protein tyrosine phosphatase activity of an essential virulence
RT   determinant in Yersinia.";
RL   Science 249:553-556(1990).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1429715;
RA   Zhang Z.-Y., Clemens J.C., Schubert H.L., Stuckey J.A.,
RA   Fischer M.W.F., Hume D.M., Saper M.A., Dixon J.E.;
RT   "Expression, purification, and physicochemical characterization of a
RT   recombinant Yersinia protein tyrosine phosphatase.";
RL   J. Biol. Chem. 267:23759-23766(1992).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=8052312; DOI=10.1038/370571a0;
RA   Stuckey J.A., Schubert H.L., Fauman E.B., Zhang Z.-Y., Dixon J.E.,
RA   Saper M.A.;
RT   "Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A
RT   and the complex with tungstate.";
RL   Nature 370:571-575(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 186-468.
RX   PubMed=8702535; DOI=10.1074/jbc.271.31.18780;
RA   Fauman E.B., Yuvaniyama C., Schubert H.L., Stuckey J.A., Saper M.A.;
RT   "The X-ray crystal structures of Yersinia tyrosine phosphatase with
RT   bound tungstate and nitrate. Mechanistic implications.";
RL   J. Biol. Chem. 271:18780-18788(1996).
CC   -!- FUNCTION: Essential virulence determinant. This protein is a
CC       protein tyrosine phosphatase. The essential function of YopH in
CC       Yersinia pathogenesis is host-protein dephosphorylation. It
CC       contributes to the ability of the bacteria to resist phagocytosis
CC       by peritoneal macrophages. {ECO:0000269|PubMed:2166336}.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
CC       ECO:0000269|PubMed:2166336}.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III
CC       secretion system.
CC   -!- INDUCTION: At 37 degrees Celsius in the absence of calcium.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
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DR   EMBL; M30457; AAA19860.1; -; Unassigned_DNA.
DR   PIR; A53889; A53889.
DR   RefSeq; NP_052424.1; NC_002120.1.
DR   PDB; 1LYV; X-ray; 1.36 A; A=163-468.
DR   PDB; 1PA9; X-ray; 2.00 A; A=185-468.
DR   PDB; 1XXP; X-ray; 3.00 A; A/B=163-468.
DR   PDB; 1XXV; X-ray; 2.50 A; A/B=163-468.
DR   PDB; 1YPT; X-ray; 2.50 A; A/B=164-468.
DR   PDB; 1YTN; X-ray; 2.40 A; A=164-468.
DR   PDB; 1YTS; X-ray; 2.50 A; A=191-468.
DR   PDB; 1YTW; X-ray; 2.40 A; A=164-468.
DR   PDB; 2I42; X-ray; 2.20 A; A=164-468.
DR   PDB; 3BLT; X-ray; 2.20 A; A=164-468.
DR   PDB; 3BLU; X-ray; 2.00 A; A=164-468.
DR   PDB; 3BM8; X-ray; 2.70 A; A=164-468.
DR   PDB; 3F99; X-ray; 1.65 A; A=164-468.
DR   PDB; 3F9A; X-ray; 1.69 A; A=164-468.
DR   PDB; 3F9B; X-ray; 1.42 A; A=164-468.
DR   PDB; 3U96; X-ray; 1.80 A; A/B=163-468.
DR   PDB; 4GF3; X-ray; 1.90 A; B=21-63.
DR   PDBsum; 1LYV; -.
DR   PDBsum; 1PA9; -.
DR   PDBsum; 1XXP; -.
DR   PDBsum; 1XXV; -.
DR   PDBsum; 1YPT; -.
DR   PDBsum; 1YTN; -.
DR   PDBsum; 1YTS; -.
DR   PDBsum; 1YTW; -.
DR   PDBsum; 2I42; -.
DR   PDBsum; 3BLT; -.
DR   PDBsum; 3BLU; -.
DR   PDBsum; 3BM8; -.
DR   PDBsum; 3F99; -.
DR   PDBsum; 3F9A; -.
DR   PDBsum; 3F9B; -.
DR   PDBsum; 3U96; -.
DR   PDBsum; 4GF3; -.
DR   ProteinModelPortal; P15273; -.
DR   SMR; P15273; 1-129, 182-468.
DR   BindingDB; P15273; -.
DR   ChEMBL; CHEMBL4404; -.
DR   PptaseDB; P3D0412160; -.
DR   GeneID; 1239155; -.
DR   SABIO-RK; P15273; -.
DR   EvolutionaryTrace; P15273; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   InterPro; IPR003546; Tyr_Pase_SptP/YopH.
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   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;
KW   3D-structure; Hydrolase; Plasmid; Protein phosphatase; Secreted;
KW   Virulence.
FT   CHAIN         1    468       Tyrosine-protein phosphatase YopH.
FT                                /FTId=PRO_0000094861.
FT   DOMAIN      152    461       Tyrosine-protein phosphatase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   ACT_SITE    403    403       Phosphocysteine intermediate.
FT   STRAND       37     39       {ECO:0000244|PDB:4GF3}.
FT   STRAND       42     46       {ECO:0000244|PDB:4GF3}.
FT   HELIX        50     62       {ECO:0000244|PDB:4GF3}.
FT   HELIX       191    208       {ECO:0000244|PDB:1LYV}.
FT   STRAND      221    224       {ECO:0000244|PDB:3F9B}.
FT   HELIX       236    238       {ECO:0000244|PDB:1LYV}.
FT   STRAND      239    241       {ECO:0000244|PDB:1LYV}.
FT   STRAND      246    251       {ECO:0000244|PDB:1LYV}.
FT   STRAND      254    259       {ECO:0000244|PDB:1LYV}.
FT   HELIX       264    266       {ECO:0000244|PDB:1LYV}.
FT   HELIX       267    276       {ECO:0000244|PDB:1LYV}.
FT   STRAND      282    284       {ECO:0000244|PDB:1LYV}.
FT   HELIX       288    292       {ECO:0000244|PDB:1LYV}.
FT   HELIX       294    296       {ECO:0000244|PDB:1LYV}.
FT   STRAND      302    304       {ECO:0000244|PDB:1LYV}.
FT   STRAND      306    308       {ECO:0000244|PDB:1LYV}.
FT   STRAND      311    324       {ECO:0000244|PDB:1LYV}.
FT   STRAND      327    338       {ECO:0000244|PDB:1LYV}.
FT   STRAND      344    351       {ECO:0000244|PDB:1LYV}.
FT   STRAND      356    358       {ECO:0000244|PDB:3F99}.
FT   HELIX       362    385       {ECO:0000244|PDB:1LYV}.
FT   HELIX       389    392       {ECO:0000244|PDB:1LYV}.
FT   STRAND      394    397       {ECO:0000244|PDB:1YTN}.
FT   STRAND      400    402       {ECO:0000244|PDB:1LYV}.
FT   STRAND      404    408       {ECO:0000244|PDB:1LYV}.
FT   HELIX       409    419       {ECO:0000244|PDB:1LYV}.
FT   HELIX       422    424       {ECO:0000244|PDB:1LYV}.
FT   HELIX       429    439       {ECO:0000244|PDB:1LYV}.
FT   HELIX       448    461       {ECO:0000244|PDB:1LYV}.
SQ   SEQUENCE   468 AA;  50939 MW;  B207D0B1AC830AF9 CRC64;
     MNLSLSDLHR QVSRLVQQES GDCTGKLRGN VAANKETTFQ GLTIASGARE SEKVFAQTVL
     SHVANIVLTQ EDTAKLLQST VKHNLNNYEL RSVGNGNSVL VSLRSDQMTL QDAKVLLEAA
     LRQESGARGH VSSHSHSVLH 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 VADDSKLRPV IHCRAGVGRT AQLIGAMCMN
     DSRNSQLSVE DMVSQMRVQR NGIMVQKDEQ LDVLIKLAEG QGRPLLNS
//
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