YOPH_YEREN
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 03-AUG-2022, entry version 148.
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; Enterobacterales;
OC Yersiniaceae; 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; DOI=10.1016/s0021-9258(18)35903-9;
RA Zhang Z.-Y., Clemens J.C., Schubert H.L., Stuckey J.A., Fischer M.W.F.,
RA 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 and
RT 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 bound
RT tungstate and nitrate. Mechanistic implications.";
RL J. Biol. Chem. 271:18780-18788(1996).
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:2166336}.
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:2166336};
CC -!- SUBUNIT: Monomer.
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}.
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DR EMBL; M30457; AAA19860.1; -; Unassigned_DNA.
DR PIR; A53889; A53889.
DR RefSeq; NP_052424.1; NC_002120.1.
DR RefSeq; WP_010891234.1; NZ_SJZK01000009.1.
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 PDB; 4YAA; X-ray; 1.05 A; A=164-468.
DR PDB; 4Z6B; X-ray; 1.20 A; A=164-468.
DR PDB; 4ZI4; X-ray; 1.12 A; A=164-468.
DR PDB; 4ZN5; X-ray; 1.12 A; A=164-468.
DR PDB; 6XFT; X-ray; 1.78 A; A=164-468.
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 PDBsum; 4YAA; -.
DR PDBsum; 4Z6B; -.
DR PDBsum; 4ZI4; -.
DR PDBsum; 4ZN5; -.
DR PDBsum; 6XFT; -.
DR AlphaFoldDB; P15273; -.
DR BMRB; P15273; -.
DR SMR; P15273; -.
DR BindingDB; P15273; -.
DR ChEMBL; CHEMBL4404; -.
DR DrugBank; DB01800; 4-Nitrocatechol sulfate.
DR DrugBank; DB08433; phenyl ethenesulfonate.
DR BRENDA; 3.1.3.48; 6741.
DR SABIO-RK; P15273; -.
DR EvolutionaryTrace; P15273; -.
DR PRO; PR: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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR DisProt; DP01528; -.
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; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
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 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;
KW 3D-structure; Hydrolase; Plasmid; Protein phosphatase; Secreted; Virulence.
FT CHAIN 1..468
FT /note="Tyrosine-protein phosphatase YopH"
FT /id="PRO_0000094861"
FT DOMAIN 152..461
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 127..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /note="Phosphocysteine intermediate"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4GF3"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4GF3"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:4GF3"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4ZN5"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4ZI4"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 311..324
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 327..338
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 362..385
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4YAA"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1YTN"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 409..419
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:4ZI4"
FT HELIX 429..439
FT /evidence="ECO:0007829|PDB:4YAA"
FT HELIX 448..460
FT /evidence="ECO:0007829|PDB:4YAA"
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
