ID A7ZCI2_CAMC1 Unreviewed; 188 AA.
AC A7ZCI2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN Name=cheB' {ECO:0000313|EMBL:EAT98008.1};
GN ORFNames=CCC13826_0841 {ECO:0000313|EMBL:EAT98008.1};
OS Campylobacter concisus (strain 13826).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104 {ECO:0000313|EMBL:EAT98008.1, ECO:0000313|Proteomes:UP000001121};
RN [1] {ECO:0000313|Proteomes:UP000001121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826 {ECO:0000313|Proteomes:UP000001121};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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; CP000792; EAT98008.1; -; Genomic_DNA.
DR RefSeq; WP_012001461.1; NC_009802.2.
DR AlphaFoldDB; A7ZCI2; -.
DR SMR; A7ZCI2; -.
DR STRING; 360104.CCC13826_0841; -.
DR KEGG; cco:CCC13826_0841; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_2_7; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000001121; 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:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
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 Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}.
FT DOMAIN 1..188
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 11
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 188 AA; 20639 MW; FC7E1D95CA09B0AA CRC64;
MAQKLVLIGA STGGPGHIKK LLKDINLNGA MVVIAQHMNK MFINSFVTQM GRECNINVEI
LSEKTNLREN IVYICDQNFE ISATLPVSAK PQPEIKTIYT PNVDVLFNSG TQIAKNVNLL
AILLTGIGDD GAAGLDKLYK AGAKCVAENE ESAIVYGMPK RAKELNQNLK SLNLMMIRKE
LEEFLNAF
//
