P0C5D3 (PTPB_STAAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 20.
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: Low molecular weight protein-tyrosine-phosphatase PtpB EC=3.1.3.48 Alternative name(s): Phosphotyrosine phosphatase B Short name=PTPase B | ||
| Gene names |
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| Organism | Staphylococcus aureus | ||
| Taxonomic identifier | 1280 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus![]() |
Protein attributes
| Sequence length | 139 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Dephosphorylates the phosphotyrosine-containing proteins. |
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1 |
| Enzyme regulation | Inhibited by N-ethylmaleimide and sodium orthovanadate. Ref.1 |
| Sequence similarities | Belongs to the low molecular weight phosphotyrosine protein phosphatase family. |
| Biophysicochemical properties | Kinetic parameters: KM=1.5 mM for p-nitrophenyl-phosphate (at pH 6.2 and 37 degrees Celsius) Ref.1 Vmax=1.4 µmol/min/mg enzyme (at pH 6.2 and 37 degrees Celsius) pH dependence: Optimum pH is 5.7-6.5. Temperature dependence: Optimum temperature is about 40 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Hydrolase Protein phosphatase |
| Gene Ontology (GO) | |
| Biological_process | peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC |
| Molecular_function | protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Staphylococcus aureus contains two low-molecular-mass phosphotyrosine protein phosphatases." Soulat D., Vaganay E., Duclos B., Genestier A.-L., Etienne J., Cozzone A.J. J. Bacteriol. 184:5194-5199(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: Reynolds. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P0C5D3. |
| SMR | P0C5D3. Positions 1-134. |
| ModBase | Search... |
Protein family/group databases | |
| PptaseDB | P3D0411153. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR023485. Ptyr_pPase_SF. IPR000106. Tyr_phospatase/Ars_reductase. IPR017867. Tyr_phospatase_low_mol_wt. [Graphical view] |
| PANTHER | PTHR11717. PTHR11717. 1 hit. |
| Pfam | PF01451. LMWPc. 1 hit. [Graphical view] |
| PRINTS | PR00719. LMWPTPASE. |
| SMART | SM00226. LMWPc. 1 hit. [Graphical view] |
| SUPFAM | SSF52788. Tyr_Pase_low_mol_wt. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PTPB_STAAU | ||||||||
| Accession | Primary (citable) accession number: P0C5D3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
