ID A0A1U9NCF9_9GAMM Unreviewed; 306 AA.
AC A0A1U9NCF9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=B0D95_15230 {ECO:0000313|EMBL:AQT61309.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT61309.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT61309.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT61309.1,
RC ECO:0000313|Proteomes:UP000189646};
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; CP019799; AQT61309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NCF9; -.
DR STRING; 1945512.B0D95_15230; -.
DR KEGG; ceb:B0D95_15230; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000189646; Chromosome.
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 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 Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Reference proteome {ECO:0000313|Proteomes:UP000189646}.
FT DOMAIN 114..303
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 306 AA; 33142 MW; 7017FD079F7FD1BD CRC64;
MLRLGLLVDN TAKQKALAQL VAQAGHKVGL SWVLDGSAQP DKDTTLDAWL VDIAEESHDD
QLLDDLFAQS RIPIILSDSS EFRIGSEEHN AWLRRTGMRL QRLRSDINLQ QSTPASELWL
LAASTGGPAA VKRFLAELPA NLGIAFLYIQ HIDAQQAVTL NRMMSNAGHY PAMVATQGLV
LAANSLTLIT ARDPVELLDN GTLMLNYGQQ WKGSYAPSID QVAANAARIY RERCNLIIFT
GMGDDGAASC RLIKQVGGKV WAQSPSDCTS DSMPVSALAT GCVSLTGSPE YLARALVQTR
QTTNHN
//
