ID A0A2T6FQT1_9GAMM Unreviewed; 199 AA.
AC A0A2T6FQT1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=B0W54_02035 {ECO:0000313|EMBL:PUA30797.1};
OS Cellvibrio sp. 79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1954207 {ECO:0000313|EMBL:PUA30797.1, ECO:0000313|Proteomes:UP000243979};
RN [1] {ECO:0000313|EMBL:PUA30797.1, ECO:0000313|Proteomes:UP000243979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=79 {ECO:0000313|EMBL:PUA30797.1};
RA Zhang Y., Xu J., Wang N.;
RT "Cellvibrio sp. 79 recovered from metagenome.";
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};
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:PUA30797.1}.
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DR EMBL; MVDH01000001; PUA30797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6FQT1; -.
DR Proteomes; UP000243979; 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.
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:UP000243979}.
FT DOMAIN 8..189
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 22
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 199 AA; 21680 MW; EB66239B9D63BE9A CRC64;
MTDEDASKLS GRRIEAIVIG ASAGGIRALM LLLGKLPAHF RVPIIIVLHM PDTRESRLAE
VFQHHTAMTV TMAEDKERIS PGTIYFAGPG YHLSIERERC FSLSCEEPLH YSRPSIDFLM
SSAADAYGAS LAGILLTGAN QDGAEGMAGI HNNGGLTIVQ DPAEAEMAFM PQAALDLFTP
DFIMPLEQIQ HLIFRLEKS
//