ID S7WYG7_9BACT Unreviewed; 157 AA.
AC S7WYG7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=ADICYQ_1971 {ECO:0000313|EMBL:EPR69003.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR69003.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR69003.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR69003.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPR69003.1}.
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DR EMBL; ATNM01000084; EPR69003.1; -; Genomic_DNA.
DR STRING; 641524.ADICYQ_1971; -.
DR PATRIC; fig|641524.5.peg.1956; -.
DR eggNOG; COG2201; Bacteria.
DR Proteomes; UP000014974; 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:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
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: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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EPR69003.1}.
FT DOMAIN 1..155
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
SQ SEQUENCE 157 AA; 16652 MW; 6DA8DC8E771F60BC CRC64;
MPEGFTASLA DRLNHLSDIQ VKEAKDGEAA LNGCVYIAPG GKNISVIKNS EGLQIVLDNH
DTPSRHKPSA DYLFRSVGKL TDYEKVAVIM TGMGSDGTAG LKDMLTAGNV KAIAESEESC
VVYGMPKAAV KAGLIHEIKH VEDIAASITS CVKKXRV
//
