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P08538 (YOPH_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase YopH

EC=3.1.3.48
Alternative name(s):
Virulence protein
Gene names
Name:yopH
Synonyms:yop2b
Ordered Locus Names:pYV0094
Encoded onPlasmid pIB1 Ref.1
Plasmid pYV Ref.2
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages. Ref.3

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.3

Subcellular location

Secreted. Note: Secreted via type III secretion system.

Induction

At 37 degrees Celsius in the absence of calcium.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Plasmid
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Tyrosine-protein phosphatase YopH
PRO_0000094862

Regions

Domain152 – 461310Tyrosine-protein phosphatase

Sites

Active site4031Phosphocysteine intermediate

Experimental info

Mutagenesis4031C → A: Abolishes PTPase activity and significantly reduces the virulence.
Sequence conflict2111A → R in CAA68629. Ref.1

Secondary structure

.................... 468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08538 [UniParc].

Last modified November 23, 2004. Version 3.
Checksum: 9EA639C08197EA81

FASTA46850,869
        10         20         30         40         50         60 
MNLSLSDLHR QVSRLVQQES GDCTGKLRGN VAANKETTFQ GLTIASGARE SEKVFAQTVL 

        70         80         90        100        110        120 
SHVANVVLTQ EDTAKLLQST VKHNLNNYDL RSVGNGNSVL VSLRSDQMTL QDAKVLLEAA 

       130        140        150        160        170        180 
LRQESGARGH VSSHSHSALH APGTPVREGL RSHLDPRTPP LPPRERPHTS GHHGAGEARA 

       190        200        210        220        230        240 
TAPSTVSPYG PEARAELSSR LTTLRNTLAP ATNDPRYLQA CGGEKLNRFR DIQCCRQTAV 

       250        260        270        280        290        300 
RADLNANYIQ VGNTRTIACQ YPLQSQLESH FRMLAENRTP VLAVLASSSE IANQRFGMPD 

       310        320        330        340        350        360 
YFRQSGTYGS ITVESKMTQQ VGLGDGIMAD MYTLTIREAG QKTISVPVVH VGNWPDQTAV 

       370        380        390        400        410        420 
SSEVTKALAS LVDQTAETKR NMYESKGSSA VGDDSKLRPV IHCRAGVGRT AQLIGAMCMN 

       430        440        450        460 
DSRNSQLSVE DMVSQMRVQR NGIMVQKDEQ LDVLIKLAEG QGRPLLNS 

« Hide

References

« Hide 'large scale' references
[1]"The plasmid-encoded Yop2b protein of Yersinia pseudotuberculosis is a virulence determinant regulated by calcium and temperature at the level of transcription."
Boelin I., Wolf-Watz H.
Mol. Microbiol. 2:237-245(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YPIII / Serotype O:3.
[2]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.
[3]"Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant."
Bliska J.B., Guan K.L., Dixon J.E., Falkow S.
Proc. Natl. Acad. Sci. U.S.A. 88:1187-1191(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS.
[4]"Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase."
Smith C.L., Khandelwal P., Keliikuli K., Zuiderweg E.R., Saper M.A.
Mol. Microbiol. 42:967-979(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-129.
[5]"Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure."
Khandelwal P., Keliikuli K., Smith C.L., Saper M.A., Zuiderweg E.R.
Biochemistry 41:11425-11437(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00551 Genomic DNA. Translation: CAA68629.1.
BX936399 Genomic DNA. Translation: CAF25437.1.
PIRS01054.
RefSeqYP_068503.1. NC_006153.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K46X-ray2.20A1-129[»]
1M0VNMR-A1-129[»]
ProteinModelPortalP08538.
SMRP08538. Positions 1-129, 182-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08538. 1 interaction.
STRING273123.pYV0094.

Chemistry

BindingDBP08538.
ChEMBLCHEMBL5835.

Protein family/group databases

PptaseDBP3D0412161.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF25437; CAF25437; pYV0094.
GeneID2952987.
KEGGyps:pYV0094.
PATRIC18637944. VBIYerPse22266_0099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG74835.
HOGENOMHOG000219626.
OMASHVANIV.
OrthoDBEOG6423BT.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-4190-MONOMER.

Family and domain databases

Gene3D3.30.1570.10. 1 hit.
3.90.190.10. 1 hit.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR015103. ProtTyrPase_YopH_N.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR003546. Tyr_Pase_SptP/YopH.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
PF09013. YopH_N. 1 hit.
[Graphical view]
PRINTSPR01371. BACYPHPHTASE.
PR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
SSF64449. SSF64449. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08538.

Entry information

Entry nameYOPH_YERPS
AccessionPrimary (citable) accession number: P08538
Secondary accession number(s): Q663H2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 23, 2004
Last modified: June 11, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references