EPSP_RALSO
ID EPSP_RALSO Reviewed; 145 AA.
AC P58596;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable low molecular weight protein-tyrosine-phosphatase EpsP;
DE EC=3.1.3.48;
GN Name=epsP; OrderedLocusNames=RSp1019; ORFNames=RS02353;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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 (By
CC similarity). {ECO:0000250}.
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; AL646053; CAD18170.1; -; Genomic_DNA.
DR RefSeq; WP_011004309.1; NC_003296.1.
DR AlphaFoldDB; P58596; -.
DR SMR; P58596; -.
DR STRING; 267608.RSp1019; -.
DR EnsemblBacteria; CAD18170; CAD18170; RSp1019.
DR GeneID; 60503930; -.
DR KEGG; rso:RSp1019; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_1_1_4; -.
DR OMA; AFFPQKA; -.
DR UniPathway; UPA00631; -.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..145
FT /note="Probable low molecular weight protein-tyrosine-
FT phosphatase EpsP"
FT /id="PRO_0000046570"
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; 15719 MW; 2873645F50134AA9 CRC64;
MIKTILVVCI GNICRSPMAQ ALLRQSLPGV SVISAGIGAL SGYPADPSAV EVMAHHGIDI
SEHRAQQLTG SLVSRADLIL VMDGAQKQEI QSRHPAKTGS VFRLGEMEQF DIADPYRKQL
TAFEEALEMI QRGVDAWVPR IRALG
