ID A0A1T4K219_9BACT Unreviewed; 192 AA.
AC A0A1T4K219;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=SAMN04488132_101404 {ECO:0000313|EMBL:SJZ36516.1};
OS Sediminibacterium ginsengisoli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Sediminibacterium.
OX NCBI_TaxID=413434 {ECO:0000313|EMBL:SJZ36516.1, ECO:0000313|Proteomes:UP000190888};
RN [1] {ECO:0000313|EMBL:SJZ36516.1, ECO:0000313|Proteomes:UP000190888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22335 {ECO:0000313|EMBL:SJZ36516.1,
RC ECO:0000313|Proteomes:UP000190888};
RA Peterson S.W.;
RL Submitted (FEB-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};
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DR EMBL; FUWH01000001; SJZ36516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4K219; -.
DR STRING; 413434.SAMN04488132_101404; -.
DR OrthoDB; 1524092at2; -.
DR Proteomes; UP000190888; 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:UniProtKB-UniRule.
DR CDD; cd16433; CheB; 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:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 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 Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Reference proteome {ECO:0000313|Proteomes:UP000190888}.
FT DOMAIN 6..192
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 192 AA; 20382 MW; 53263D71D10412FC CRC64;
MEKDKVRSSC CLAVIGGSAG SLDAILKILP CLNTGAAYAV VIVQHRKPLQ DSPLADILSD
KTGWSVKEVE EKETVTPGTV YIAPADYHLL FETDHSFSLD ASEKVNYSRP SIDVTFESAA
DVYGSSVIGI LLSGANADGV EGLQKIRDAG GICIVQDPAT AEVSYMPAEA LRRLQPDLVL
PAEGIGMYLN AI
//