ID   EPSP_RALSL              Reviewed;         145 AA.
AC   Q45408;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable low molecular weight protein-tyrosine-phosphatase EpsP;
DE            EC=3.1.3.48;
GN   Name=epsP;
OS   Ralstonia solanacearum (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AW;
RX   PubMed=7476194; DOI=10.1111/j.1365-2958.1995.tb02323.x;
RA   Huang J., Schell M.;
RT   "Molecular characterization of the eps gene cluster of Pseudomonas
RT   solanacearum and its transcriptional regulation at a single promoter.";
RL   Mol. Microbiol. 16:977-989(1995).
CC   -!- FUNCTION: May be involved in assembly or function of the EPS I
CC       polymerization/export complex and/or the EpsB ATPase. Alternatively it
CC       may function in the removal of the terminal phosphate from C55-
CC       isoprenyl pyrophosphate in order to recycle the C55-isoprenyl phosphate
CC       lipid carrier used in the synthesis of polysaccharide repeat units.
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   -!- 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; U17898; AAA91623.1; -; Genomic_DNA.
DR   PIR; S77635; S77635.
DR   AlphaFoldDB; Q45408; -.
DR   SMR; Q45408; -.
DR   STRING; 859657.RPSI07_mp1013; -.
DR   UniPathway; UPA00631; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide 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   3: Inferred from homology;
KW   Hydrolase; Lipopolysaccharide biosynthesis; Protein phosphatase.
FT   CHAIN           1..145
FT                   /note="Probable low molecular weight protein-tyrosine-
FT                   phosphatase EpsP"
FT                   /id="PRO_0000046571"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   145 AA;  15711 MW;  E2E4D3947CB750AE CRC64;
     MIKTILVVCI GNICRSPMAQ ALLRQALPGV SVISAGIGAL SGYPADPSAV EVMAQHGIDI
     SEHRAQQLTG SLVNRADLIL VMGGAQKREI QARHPSKTGS VFRLGEMEQF DIDDPYRKQM
     MAFEDALAMI QRGVDAWVPR IRALG