ID   PTP_ACIJO               Reviewed;         142 AA.
AC   O52787;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase Ptp;
DE            EC=3.1.3.48;
GN   Name=ptp;
OS   Acinetobacter johnsonii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=40214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9434192; DOI=10.1016/s0378-1119(97)00554-4;
RA   Grangeasse C., Doublet P., Vaganay E., Vincent C., Deleage G., Duclos B.,
RA   Cozzone A.J.;
RT   "Characterization of a bacterial gene encoding an autophosphorylating
RT   protein tyrosine kinase.";
RL   Gene 204:259-265(1997).
RN   [2]
RP   CHARACTERIZATION, AND MUTAGENESIS OF CYS-10 AND ARG-16.
RX   PubMed=9571056; DOI=10.1006/jmbi.1998.1650;
RA   Grangeasse C., Doublet P., Vincent C., Vaganay E., Riberty M., Duclos B.,
RA   Cozzone A.J.;
RT   "Functional characterization of the low-molecular-mass phosphotyrosine-
RT   protein phosphatase of Acinetobacter johnsonii.";
RL   J. Mol. Biol. 278:339-347(1998).
CC   -!- FUNCTION: Dephosphorylates ptk. May be involved in the production and
CC       the transport of exopolysaccharides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC   -!- ACTIVITY REGULATION: Inhibited by ammonium molybdate, sodium
CC       orthovanadate, N-ethylmaleimide and iodoacetic acid.
CC   -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; Y15162; CAA75430.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52787; -.
DR   SMR; O52787; -.
DR   UniPathway; UPA00631; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
PE   1: Evidence at protein level;
KW   Exopolysaccharide synthesis; Hydrolase; Protein phosphatase.
FT   CHAIN           1..142
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   Ptp"
FT                   /id="PRO_0000046566"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        16
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   MUTAGEN         10
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9571056"
FT   MUTAGEN         16
FT                   /note="R->K: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9571056"
SQ   SEQUENCE   142 AA;  16215 MW;  62B53F3BDDBA5986 CRC64;
     MQFKNILVVC IGNICRSPMA EYLLKQNYPQ LTIHSAGISG MIGYSADEKA QLCMERIGID
     MSPHIAKKLN AELLKQADLI LVMSQNQQKH IEQTWPFAKG KTFRLGHWQG KNIPDPYQHD
     QAFFDETSLL IQTCVADWTK HI