ID A0A1G6YN42_9BURK Unreviewed; 335 AA.
AC A0A1G6YN42;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=SAMN05192589_110101 {ECO:0000313|EMBL:SDD91087.1};
OS Paracidovorax valerianellae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=187868 {ECO:0000313|EMBL:SDD91087.1, ECO:0000313|Proteomes:UP000198781};
RN [1] {ECO:0000313|EMBL:SDD91087.1, ECO:0000313|Proteomes:UP000198781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16619 {ECO:0000313|EMBL:SDD91087.1,
RC ECO:0000313|Proteomes:UP000198781};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FMZC01000010; SDD91087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6YN42; -.
DR STRING; 187868.SAMN05192589_110101; -.
DR OrthoDB; 9791760at2; -.
DR Proteomes; UP000198781; 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:UP000198781}.
FT DOMAIN 3..191
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 15
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 335 AA; 35821 MW; E05F24619B78FA97 CRC64;
MNPSAETPFI FIGASAGGVY AMLDLVTALP AGFPAPIFFV QHIGSMRSHL PDLLNTRGPN
RALTARDGDV PQPGTIYIAP SDHHMLLEGG VVRLSRGPKE HHARPAIDPL FRSAALDCGA
RAVGVVLTGM LDDGTAGLRA IKDCGGIAVV QDPEDAYEPS MPRSALACVE VDHVVPLGGL
GALLCQLAQP RARRLPVLPP MSWRREHALG AGDHNVENLM AIADPSTFTC PDCGGVLFEL
KDKRPVRYRC HTGHAFSLRS LAHTQEQTTD AALWAALRTL QEKESILRHL ADLHQGSDAQ
TTAQALREAD ELAIACSALR RLTEKSPSPE SFGAP
//
