ID A0A0Q6W6Q9_9BURK Unreviewed; 363 AA.
AC A0A0Q6W6Q9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=ASD15_29565 {ECO:0000313|EMBL:KQV86226.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV86226.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV86226.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV86226.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV86226.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV86226.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQV86226.1}.
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DR EMBL; LMDJ01000008; KQV86226.1; -; Genomic_DNA.
DR RefSeq; WP_057155067.1; NZ_LMDJ01000008.1.
DR AlphaFoldDB; A0A0Q6W6Q9; -.
DR OrthoDB; 9791760at2; -.
DR Proteomes; UP000051876; 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; IPR011247; Chemotax_prot-Glu_Me-esterase.
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 PIRSF; PIRSF036461; Chmtx_methlestr; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876}.
FT DOMAIN 3..194
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 14
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 363 AA; 38554 MW; 0E99E351ADA2BC86 CRC64;
MTPATDKVIV IGASAGGLDA LKRVLGKLPA DFPAPVLVVM HIGARESILP ALLRKVCALQ
VRHARDGELL AQPMILVAPP DRHMMVARDG PIGCVRLTYG AMENYTRPAI DPLFRSAAAA
YGAGATGVIL TGYLDDGTAG LQAIKACGGT AVVQDPSDAF AESMPSSALE RVAVDYVLKL
DDIGDMLLTL AGAPLPPSEL DATQDLSKEA AMESKPREVP EWIAVENRYA GGEGELRDLE
RIARPSTFTC PECHGALWEV RERVAGAASS GNANGKPRPR YRCHTGHSFT ALALEHTQDR
VVEEAVWSAI RALHEKEELA RRLAEHAHSN GLPGAAADYQ ARAESARRSA AVLRNNLVRG
AGG
//
