P08538 (YOPH_YERPS) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tyrosine-protein phosphatase YopH EC=3.1.3.48 Alternative name(s): Virulence protein | ||||||
| Gene names |
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| Encoded on | Plasmid pIB1 Ref.1 Plasmid pYV Ref.2 | ||||||
| Organism | Yersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 273123 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › ![]() |
Protein attributes
| Sequence length | 468 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 process | Virulence |
| Cellular component | Secreted |
| Molecular function | Hydrolase Protein phosphatase |
| Technical term | 3D-structure Complete proteome Plasmid |
| Gene Ontology (GO) | |
| Biological_process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine dephosphorylationInferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 468 | 468 | Tyrosine-protein phosphatase YopH | PRO_0000094862 | ||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||
| Domain | 152 – 461 | 310 | Tyrosine-protein phosphatase | |||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||
| Active site | 403 | 1 | Phosphocysteine intermediate | |||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||
| Mutagenesis | 403 | 1 | C → A: Abolishes PTPase activity and significantly reduces the virulence. | |||||||||||||||||||||||||
| Sequence conflict | 211 | 1 | A → R in CAA68629. Ref.1 | |||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||
| Helix | 5 – 17 | 13 | ||||||||||||||||||||||||||
| Beta strand | 24 – 34 | 11 | ||||||||||||||||||||||||||
| Helix | 44 – 46 | 3 | ||||||||||||||||||||||||||
| Helix | 50 – 62 | 13 | ||||||||||||||||||||||||||
| Turn | 63 – 65 | 3 | ||||||||||||||||||||||||||
| Helix | 70 – 82 | 13 | ||||||||||||||||||||||||||
| Beta strand | 88 – 94 | 7 | ||||||||||||||||||||||||||
| Beta strand | 97 – 106 | 10 | ||||||||||||||||||||||||||
| Helix | 110 – 124 | 15 | ||||||||||||||||||||||||||
| Beta strand | 126 – 128 | 3 | ||||||||||||||||||||||||||
Sequences
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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. 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. | ||||||||||||||||||
| PIR | S01054. | ||||||||||||||||||
| RefSeq | YP_068503.1. NC_006153.2. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P08538. | ||||||||||||||||||
| SMR | P08538. Positions 1-129, 182-468. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P08538. 1 interaction. | ||||||||||||||||||
| STRING | 273123.pYV0094. | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| PptaseDB | P3D0412161. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | CAF25437; CAF25437; pYV0094. | ||||||||||||||||||
| GeneID | 2952987. | ||||||||||||||||||
| KEGG | yps:pYV0094. | ||||||||||||||||||
| PATRIC | 18637944. VBIYerPse22266_0099. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | NOG74835. | ||||||||||||||||||
| HOGENOM | HOG000219626. | ||||||||||||||||||
| OMA | SHVANIV. | ||||||||||||||||||
| ProtClustDB | CLSK862151. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 3.30.1570.10. 1 hit. | ||||||||||||||||||
| InterPro | 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] | ||||||||||||||||||
| Pfam | PF00102. Y_phosphatase. 1 hit. PF09013. YopH_N. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR01371. BACYPHPHTASE. PR00700. PRTYPHPHTASE. | ||||||||||||||||||
| SMART | SM00194. PTPc. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF64449. ProtTyrPase_YopH_N. 1 hit. | ||||||||||||||||||
| PROSITE | PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| BindingDB | P08538. | ||||||||||||||||||
| ChEMBL | CHEMBL5835. | ||||||||||||||||||
| EvolutionaryTrace | P08538. | ||||||||||||||||||
Entry information
| Entry name | YOPH_YERPS | ||||||||
| Accession | Primary (citable) accession number: P08538 Secondary accession number(s): Q663H2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
