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 03-AUG-2022, entry version 156.
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}.
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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 AlphaFoldDB; P08538; -.
DR BMRB; P08538; -.
DR SASBDB; P08538; -.
DR SMR; P08538; -.
DR IntAct; P08538; 1.
DR ChEMBL; CHEMBL5835; -.
DR EnsemblBacteria; CAF25437; CAF25437; pYV0094.
DR GeneID; 66841085; -.
DR KEGG; ypo:BZ17_4241; -.
DR KEGG; yps:pYV0094; -.
DR PATRIC; fig|273123.14.peg.4476; -.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
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_0000094862"
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 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:0007829|PDB:1K46"
FT STRAND 24..34
FT /evidence="ECO:0007829|PDB:1M0V"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1K46"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:1K46"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1K46"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1K46"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1K46"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:1K46"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:1K46"
FT STRAND 126..128
FT /evidence="ECO:0007829|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
