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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   09-JUL-2014, entry version 113.
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.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
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.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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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-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; 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   ACT_SITE    403    403       Phosphocysteine intermediate.
FT   STRAND       37     39
FT   STRAND       42     46
FT   HELIX        50     62
FT   HELIX       191    208
FT   STRAND      221    224
FT   HELIX       236    238
FT   STRAND      239    241
FT   STRAND      246    251
FT   STRAND      254    259
FT   HELIX       264    266
FT   HELIX       267    276
FT   STRAND      282    284
FT   HELIX       288    292
FT   HELIX       294    296
FT   STRAND      302    304
FT   STRAND      306    308
FT   STRAND      311    324
FT   STRAND      327    338
FT   STRAND      344    351
FT   STRAND      356    358
FT   HELIX       362    385
FT   HELIX       389    392
FT   STRAND      394    397
FT   STRAND      400    402
FT   STRAND      404    408
FT   HELIX       409    419
FT   HELIX       422    424
FT   HELIX       429    439
FT   HELIX       448    461
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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