ID A0A3N2DGK3_9GAMM Unreviewed; 327 AA.
AC A0A3N2DGK3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=EDC56_3157 {ECO:0000313|EMBL:ROR98917.1};
OS Sinobacterium caligoides.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Sinobacterium.
OX NCBI_TaxID=933926 {ECO:0000313|EMBL:ROR98917.1, ECO:0000313|Proteomes:UP000275394};
RN [1] {ECO:0000313|EMBL:ROR98917.1, ECO:0000313|Proteomes:UP000275394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100316 {ECO:0000313|EMBL:ROR98917.1,
RC ECO:0000313|Proteomes:UP000275394};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) 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:ROR98917.1}.
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DR EMBL; RKHR01000006; ROR98917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2DGK3; -.
DR Proteomes; UP000275394; 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 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:UP000275394}.
FT DOMAIN 143..324
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 327 AA; 35656 MW; C350897B151C1458 CRC64;
MAVVNPRVGL VVDDPLQQHQ LKVLLQEHGY QLGLLISPEQ LTPQHIVDAA VHLWLLCLAD
VSRHEEVLES LLSDAEVPVL IEDGSEQWAD EEGPSPRHRR LIKQLNKALP VLSESDAHVE
NPILSRAQEV SEETQVACNV WVLGVSLGGP EAVCEFLSMV PADLPVAFVY AQHIDEQFNE
TLLLAVSKQS SMPAKVLRSG DRLRHGELGL MPVRQRLKLL PLGQVMIVDE PWPGPFSPSI
DCLMSDVAHH YGRYSGGIIF SGMGDDGAEG SKQMTLAGGR VWLQSFDSCA NSAMPEATAA
VGNYERIATP AELAAALVDE YKQVDNA
//
