ID A0A1M5JCM9_9FLAO Unreviewed; 183 AA.
AC A0A1M5JCM9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=SAMN05443373_101620 {ECO:0000313|EMBL:SHG38298.1};
OS Flavobacterium granuli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=280093 {ECO:0000313|EMBL:SHG38298.1, ECO:0000313|Proteomes:UP000184384};
RN [1] {ECO:0000313|Proteomes:UP000184384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19729 {ECO:0000313|Proteomes:UP000184384};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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; FQWO01000001; SHG38298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5JCM9; -.
DR STRING; 280093.SAMN05443373_101620; -.
DR Proteomes; UP000184384; 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}.
FT DOMAIN 1..174
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 7
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 183 AA; 20551 MW; D53FE30D5E2632E0 CRC64;
MIIIGGSAGS FNTILSILNG LDKNFSVPIV IVLHRLKNYE SSFEDILRHH THYIVKEVED
KEIIKNGIVY TAPSNYHLLL EENNTFSLDV SELVNYSRPS IDVTFESASA ILKEKCCGIL
LSGANNDGAK GLKRIAENNG TTIIQDCQEA EYKNMPNAAK LIYKYHQELN TKNIINKLNN
EYC
//
