ID A0A1W1W0H1_9BACT Unreviewed; 327 AA.
AC A0A1W1W0H1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=SAMN00120144_3825 {ECO:0000313|EMBL:SMB98614.1};
OS Hymenobacter roseosalivarius DSM 11622.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=645990 {ECO:0000313|EMBL:SMB98614.1, ECO:0000313|Proteomes:UP000192266};
RN [1] {ECO:0000313|EMBL:SMB98614.1, ECO:0000313|Proteomes:UP000192266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11622 {ECO:0000313|EMBL:SMB98614.1,
RC ECO:0000313|Proteomes:UP000192266};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWWW01000085; SMB98614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1W0H1; -.
DR STRING; 645990.SAMN00120144_3825; -.
DR Proteomes; UP000192266; 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:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16433; CheB; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011247; Chemotax_prot-Glu_Me-esterase.
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 PIRSF; PIRSF036461; Chmtx_methlestr; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000192266}.
FT DOMAIN 19..180
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
SQ SEQUENCE 327 AA; 35677 MW; 2ED0EBFE40211A6F CRC64;
MAKGPSLRTS PRPTLTAGAL GAAVLLVQHF APHSSGSHLV ERLSRRTFLN CRLPNDGDRI
EPNTVYLPPP DRHLLVKDGH MLVTKGPREN HYRPAADALF RSAAAHYGTA VIGVVLTGML
HDGTAGLELI KRAGGLAVVQ DPREAEYPSM PESALSNVPV DYVLPIAEMG ELLTRLVQIP
SSGNSNVPEN IKLEAAIAER VVGTTDEVLR LGKPSTMTCP DCGGALFELR HGKLLRYRCH
TGHGFTANAL PKSTQHSLEE TLWVALRMME ERKNLLTSMA SRGTGLFSVQ QEERIEEIKQ
HINRLREFLL NGVNGSTAVT IPEEEQS
//
