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P08538

- YOPH_YERPS

UniProt

P08538 - YOPH_YERPS

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Protein
Tyrosine-protein phosphatase YopH
Gene
yopH, yop2b, pYV0094
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei403 – 4031Phosphocysteine intermediate

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciYPSE273123:GI1M-4190-MONOMER.

Protein family/group databases

PptaseDBiP3D0412161.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase YopH (EC:3.1.3.48)
Alternative name(s):
Virulence protein
Gene namesi
Name:yopH
Synonyms:yop2b
Ordered Locus Names:pYV0094
Encoded oniPlasmid pIB11 Publication
Plasmid pYV1 Publication
OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
Taxonomic identifieri273123 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001011: Plasmid pYV

Subcellular locationi

Secreted
Note: Secreted via type III secretion system.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi403 – 4031C → A: Abolishes PTPase activity and significantly reduces the virulence.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Tyrosine-protein phosphatase YopH
PRO_0000094862Add
BLAST

Expressioni

Inductioni

At 37 degrees Celsius in the absence of calcium.

Interactioni

Protein-protein interaction databases

IntActiP08538. 1 interaction.
STRINGi273123.pYV0094.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713
Beta strandi24 – 3411
Helixi44 – 463
Helixi50 – 6213
Turni63 – 653
Helixi70 – 8213
Beta strandi88 – 947
Beta strandi97 – 10610
Helixi110 – 12415
Beta strandi126 – 1283

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K46X-ray2.20A1-129[»]
1M0VNMR-A1-129[»]
ProteinModelPortaliP08538.
SMRiP08538. Positions 1-129, 182-468.

Miscellaneous databases

EvolutionaryTraceiP08538.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 461310Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG74835.
HOGENOMiHOG000219626.
OMAiSHVANIV.
OrthoDBiEOG6423BT.

Family and domain databases

Gene3Di3.30.1570.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR029021. 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]
PfamiPF00102. Y_phosphatase. 1 hit.
PF09013. YopH_N. 1 hit.
[Graphical view]
PRINTSiPR01371. BACYPHPHTASE.
PR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF64449. SSF64449. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08538-1 [UniParc]FASTAAdd to Basket

« Hide

MNLSLSDLHR QVSRLVQQES GDCTGKLRGN VAANKETTFQ GLTIASGARE    50
SEKVFAQTVL SHVANVVLTQ EDTAKLLQST VKHNLNNYDL RSVGNGNSVL 100
VSLRSDQMTL QDAKVLLEAA LRQESGARGH VSSHSHSALH APGTPVREGL 150
RSHLDPRTPP LPPRERPHTS GHHGAGEARA TAPSTVSPYG PEARAELSSR 200
LTTLRNTLAP ATNDPRYLQA CGGEKLNRFR DIQCCRQTAV RADLNANYIQ 250
VGNTRTIACQ YPLQSQLESH FRMLAENRTP VLAVLASSSE IANQRFGMPD 300
YFRQSGTYGS ITVESKMTQQ VGLGDGIMAD MYTLTIREAG QKTISVPVVH 350
VGNWPDQTAV SSEVTKALAS LVDQTAETKR NMYESKGSSA VGDDSKLRPV 400
IHCRAGVGRT AQLIGAMCMN DSRNSQLSVE DMVSQMRVQR NGIMVQKDEQ 450
LDVLIKLAEG QGRPLLNS 468
Length:468
Mass (Da):50,869
Last modified:November 23, 2004 - v3
Checksum:i9EA639C08197EA81
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111A → R in CAA68629. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00551 Genomic DNA. Translation: CAA68629.1.
BX936399 Genomic DNA. Translation: CAF25437.1.
PIRiS01054.
RefSeqiYP_068503.1. NC_006153.2.

Genome annotation databases

EnsemblBacteriaiCAF25437; CAF25437; pYV0094.
GeneIDi2952987.
KEGGiyps:pYV0094.
PATRICi18637944. VBIYerPse22266_0099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00551 Genomic DNA. Translation: CAA68629.1 .
BX936399 Genomic DNA. Translation: CAF25437.1 .
PIRi S01054.
RefSeqi YP_068503.1. NC_006153.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K46 X-ray 2.20 A 1-129 [» ]
1M0V NMR - A 1-129 [» ]
ProteinModelPortali P08538.
SMRi P08538. Positions 1-129, 182-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08538. 1 interaction.
STRINGi 273123.pYV0094.

Chemistry

BindingDBi P08538.
ChEMBLi CHEMBL5835.

Protein family/group databases

PptaseDBi P3D0412161.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF25437 ; CAF25437 ; pYV0094 .
GeneIDi 2952987.
KEGGi yps:pYV0094.
PATRICi 18637944. VBIYerPse22266_0099.

Phylogenomic databases

eggNOGi NOG74835.
HOGENOMi HOG000219626.
OMAi SHVANIV.
OrthoDBi EOG6423BT.

Enzyme and pathway databases

BioCyci YPSE273123:GI1M-4190-MONOMER.

Miscellaneous databases

EvolutionaryTracei P08538.

Family and domain databases

Gene3Di 3.30.1570.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR029021. 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 ]
Pfami PF00102. Y_phosphatase. 1 hit.
PF09013. YopH_N. 1 hit.
[Graphical view ]
PRINTSi PR01371. BACYPHPHTASE.
PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF64449. SSF64449. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    Plasmid: pIB1
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IP32953.
    Plasmid: pYV
  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.

Entry informationi

Entry nameiYOPH_YERPS
AccessioniPrimary (citable) accession number: P08538
Secondary accession number(s): Q663H2
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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