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Low molecular weight protein-tyrosine-phosphatase Ptp (EC 3.1.3.48)

 PTP_ACIJO               Reviewed;         142 AA.
O52787;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 69.
RecName: Full=Low molecular weight protein-tyrosine-phosphatase Ptp;
EC=3.1.3.48;
Name=ptp;
Acinetobacter johnsonii.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Moraxellaceae; Acinetobacter.
NCBI_TaxID=40214;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9434192; DOI=10.1016/S0378-1119(97)00554-4;
Grangeasse C., Doublet P., Vaganay E., Vincent C., Deleage G.,
Duclos B., Cozzone A.J.;
"Characterization of a bacterial gene encoding an autophosphorylating
protein tyrosine kinase.";
Gene 204:259-265(1997).
[2]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-10 AND ARG-16.
PubMed=9571056; DOI=10.1006/jmbi.1998.1650;
Grangeasse C., Doublet P., Vincent C., Vaganay E., Riberty M.,
Duclos B., Cozzone A.J.;
"Functional characterization of the low-molecular-mass
phosphotyrosine-protein phosphatase of Acinetobacter johnsonii.";
J. Mol. Biol. 278:339-347(1998).
-!- FUNCTION: Dephosphorylates ptk. May be involved in the production
and the transport of exopolysaccharides.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- ACTIVITY REGULATION: Inhibited by ammonium molybdate, sodium
orthovanadate, N-ethylmaleimide and iodoacetic acid.
-!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
-!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
protein phosphatase family. {ECO:0000305}.
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EMBL; Y15162; CAA75430.1; -; Genomic_DNA.
ProteinModelPortal; O52787; -.
SMR; O52787; -.
UniPathway; UPA00631; -.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
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;
Exopolysaccharide synthesis; Hydrolase; Protein phosphatase.
CHAIN 1 142 Low molecular weight protein-tyrosine-
phosphatase Ptp.
/FTId=PRO_0000046566.
ACT_SITE 10 10 Nucleophile. {ECO:0000250}.
ACT_SITE 15 15 {ECO:0000250}.
ACT_SITE 115 115 Proton donor. {ECO:0000250}.
MUTAGEN 10 10 C->S: Loss of activity.
{ECO:0000269|PubMed:9571056}.
MUTAGEN 16 16 R->K: Loss of activity.
{ECO:0000269|PubMed:9571056}.
SEQUENCE 142 AA; 16215 MW; 62B53F3BDDBA5986 CRC64;
MQFKNILVVC IGNICRSPMA EYLLKQNYPQ LTIHSAGISG MIGYSADEKA QLCMERIGID
MSPHIAKKLN AELLKQADLI LVMSQNQQKH IEQTWPFAKG KTFRLGHWQG KNIPDPYQHD
QAFFDETSLL IQTCVADWTK HI


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