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P0C5D2

- PTPA_STAAU

UniProt

P0C5D2 - PTPA_STAAU

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Protein

Low molecular weight protein-tyrosine-phosphatase PtpA

Gene
ptpA
Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Dephosphorylates the phosphotyrosine-containing proteins.

Catalytic activityi

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

Enzyme regulationi

Inhibited by N-ethylmaleimide and sodium orthovanadate.1 Publication

Kineticsi

  1. KM=1.2 mM for p-nitrophenyl-phosphate (at pH 6.2 and 37 degrees Celsius)1 Publication

Vmax=33.6 µmol/min/mg enzyme (at pH 6.2 and 37 degrees Celsius)

pH dependencei

Optimum pH is 6.2.

Temperature dependencei

Optimum temperature is about 40 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Nucleophile By similarity
Active sitei14 – 141 By similarity
Active sitei120 – 1201Proton donor By similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Protein family/group databases

PptaseDBiP3D0411152.

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight protein-tyrosine-phosphatase PtpA (EC:3.1.3.48)
Alternative name(s):
Phosphotyrosine phosphatase A
Short name:
PTPase A
Gene namesi
Name:ptpA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154Low molecular weight protein-tyrosine-phosphatase PtpAPRO_0000300656Add
BLAST

Proteomic databases

PRIDEiP0C5D2.

Structurei

Secondary structure

1
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312
Helixi14 – 2815
Beta strandi33 – 408
Helixi52 – 609
Beta strandi80 – 867
Helixi87 – 9610
Beta strandi102 – 1065
Helixi107 – 1104
Helixi121 – 1244
Helixi127 – 14822

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ROFX-ray1.03A1-152[»]
ProteinModelPortaliP0C5D2.
SMRiP0C5D2. Positions 1-152.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717. PTHR11717. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C5D2-1 [UniParc]FASTAAdd to Basket

« Hide

MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP    50
HEGTQKILNK HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKSINPNL 100
KGQLFKLLEF SNMEESDVPD PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN 150
LKEG 154
Length:154
Mass (Da):17,491
Last modified:September 11, 2007 - v1
Checksum:i67E81E0B8125B1E8
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ROF X-ray 1.03 A 1-152 [» ]
ProteinModelPortali P0C5D2.
SMRi P0C5D2. Positions 1-152.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PptaseDBi P3D0411152.

Proteomic databases

PRIDEi P0C5D2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view ]
PANTHERi PTHR11717. PTHR11717. 1 hit.
Pfami PF01451. LMWPc. 1 hit.
[Graphical view ]
PRINTSi PR00719. LMWPTPASE.
SMARTi SM00226. LMWPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52788. SSF52788. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPTPA_STAAU
AccessioniPrimary (citable) accession number: P0C5D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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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