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Low molecular weight protein-tyrosine-phosphatase PtpB (EC 3.1.3.48) (Phosphotyrosine phosphatase B) (PTPase B)

 PTPB_STAAU              Reviewed;         139 AA.
P0C5D3;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 1.
05-DEC-2018, entry version 54.
RecName: Full=Low molecular weight protein-tyrosine-phosphatase PtpB;
EC=3.1.3.48;
AltName: Full=Phosphotyrosine phosphatase B;
Short=PTPase B;
Name=ptpB;
Staphylococcus aureus.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, CATALYTIC
ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=Reynolds;
PubMed=12193638; DOI=10.1128/JB.184.18.5194-5199.2002;
Soulat D., Vaganay E., Duclos B., Genestier A.-L., Etienne J.,
Cozzone A.J.;
"Staphylococcus aureus contains two low-molecular-mass phosphotyrosine
protein phosphatases.";
J. Bacteriol. 184:5194-5199(2002).
-!- FUNCTION: Dephosphorylates the phosphotyrosine-containing
proteins.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000269|PubMed:12193638};
-!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and sodium
orthovanadate. {ECO:0000269|PubMed:12193638}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 mM for p-nitrophenyl-phosphate (at pH 6.2 and 37 degrees
Celsius) {ECO:0000269|PubMed:12193638};
Vmax=1.4 umol/min/mg enzyme (at pH 6.2 and 37 degrees Celsius)
{ECO:0000269|PubMed:12193638};
pH dependence:
Optimum pH is 5.7-6.5. {ECO:0000269|PubMed:12193638};
Temperature dependence:
Optimum temperature is about 40 degrees Celsius.
{ECO:0000269|PubMed:12193638};
-!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
protein phosphatase family. {ECO:0000305}.
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RefSeq; WP_000697334.1; NZ_UHCX01000001.1.
ProteinModelPortal; P0C5D3; -.
SMR; P0C5D3; -.
eggNOG; ENOG4107WAU; Bacteria.
eggNOG; COG0394; LUCA.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
InterPro; IPR023485; Ptyr_pPase.
InterPro; IPR036196; Ptyr_pPase_sf.
InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
Pfam; PF01451; LMWPc; 1.
PRINTS; PR00719; LMWPTPASE.
SMART; SM00226; LMWPc; 1.
SUPFAM; SSF52788; SSF52788; 1.
1: Evidence at protein level;
Hydrolase; Protein phosphatase.
CHAIN 1 139 Low molecular weight protein-tyrosine-
phosphatase PtpB.
/FTId=PRO_0000300670.
ACT_SITE 7 7 Nucleophile. {ECO:0000250}.
ACT_SITE 13 13 {ECO:0000250}.
ACT_SITE 111 111 Proton donor. {ECO:0000250}.
SEQUENCE 139 AA; 15788 MW; 63EB2C0E2A53EA5B CRC64;
MKILFVCTGN TCRSPLAESI AKEVMPNHQF ESRGIFAVNN QGVSNYVEDL VEEHHLAETT
LSQQFTEADL KADIILTMSY SHKELIEAHF GLQNHVFTLH EYVKEAGEVI DPYGGTKEMY
VHTYEELVSL ILKLKDIIC


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