ID A0A017HIS6_9RHOB Unreviewed; 342 AA.
AC A0A017HIS6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=Rumeso_04292 {ECO:0000313|EMBL:EYD74235.1};
OS Rubellimicrobium mesophilum DSM 19309.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD74235.1, ECO:0000313|Proteomes:UP000019666};
RN [1] {ECO:0000313|EMBL:EYD74235.1, ECO:0000313|Proteomes:UP000019666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD74235.1,
RC ECO:0000313|Proteomes:UP000019666};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (FEB-2013) 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:EYD74235.1}.
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DR EMBL; AOSK01000120; EYD74235.1; -; Genomic_DNA.
DR RefSeq; WP_037283793.1; NZ_KK088626.1.
DR AlphaFoldDB; A0A017HIS6; -.
DR STRING; 442562.Rumeso_04292; -.
DR PATRIC; fig|442562.3.peg.4226; -.
DR HOGENOM; CLU_000445_51_1_5; -.
DR OrthoDB; 9791760at2; -.
DR Proteomes; UP000019666; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019666}.
FT DOMAIN 1..189
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 342 AA; 36249 MW; E431811AE5645358 CRC64;
MDTRDIIVIG GSSGATAPLK TILGALPTDL PAAVFIVLHI PARSLGILTT VAQAAGRLPV
RPAADGMPIE LGHIYLGVPD RHLLLVDGHI RLGRGPRENM ARPAIDPLFR SAAVSYGSRV
VGVLLSGLLN DGAAGLSAIK RCGGLALVQD PQDAIADAMP LAALQAVTAD LVAASGRIGD
VLSDLVREPA GPRVPIPPEI RLEVDIAAGE RVDSGVLRRF ADPAALICPD CGGVMSQVRE
PGPLRFRCQV GHAKTAEVLA YEQENAVDEA LRVALRIIEE RAELVSRMAE DGRKTGRRAV
AEMYQERAEE YRHYADTLRR AVLMSMGRAE PSGDEGGQEE AK
//
