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Database: UniProt
Entry: B1FMG7_9BURK
LinkDB: B1FMG7_9BURK
Original site: B1FMG7_9BURK 
ID   B1FMG7_9BURK            Unreviewed;       155 AA.
AC   B1FMG7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=BamIOP4010DRAFT_5228 {ECO:0000313|EMBL:EDT01266.1};
OS   Burkholderia ambifaria IOP40-10.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT01266.1, ECO:0000313|Proteomes:UP000005463};
RN   [1] {ECO:0000313|EMBL:EDT01266.1, ECO:0000313|Proteomes:UP000005463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT01266.1,
RC   ECO:0000313|Proteomes:UP000005463};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Tiedje J., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Burkholderia ambifaria
RT   IOP40-10.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC         glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:82795; EC=3.1.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00000941};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDT01266.1}.
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DR   EMBL; ABLC01000196; EDT01266.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1FMG7; -.
DR   PATRIC; fig|396596.7.peg.2131; -.
DR   Proteomes; UP000005463; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd16432; CheB_Rec; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR   PANTHER; PTHR42872:SF6; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   PROSITE; PS50122; CHEB; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDT01266.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          1..155
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
SQ   SEQUENCE   155 AA;  16671 MW;  67C27F3D98F4553C CRC64;
     MIIQHVDRAF AEGMAQWLDG QTPLTVRVAR EGDRPQPGVA LLAATDDHLR ITRAGTLEYT
     REPAATPYRP SVDVFFNSLT EHWPGRVIGV LLTGMGRDGA IGLKALRMKG YHTIAQDEAT
     SAVYGMPKAA ATLGAARAIL PLERIAGELA ALARI
//
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