ID A0A420DH41_9RHOB Unreviewed; 332 AA.
AC A0A420DH41;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=C8N30_2607 {ECO:0000313|EMBL:RKE93544.1};
OS Sulfitobacter guttiformis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=74349 {ECO:0000313|EMBL:RKE93544.1, ECO:0000313|Proteomes:UP000284407};
RN [1] {ECO:0000313|EMBL:RKE93544.1, ECO:0000313|Proteomes:UP000284407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11458 {ECO:0000313|EMBL:RKE93544.1,
RC ECO:0000313|Proteomes:UP000284407};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (SEP-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:RKE93544.1}.
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DR EMBL; RAQK01000002; RKE93544.1; -; Genomic_DNA.
DR RefSeq; WP_025062410.1; NZ_RAQK01000002.1.
DR AlphaFoldDB; A0A420DH41; -.
DR STRING; 1443111.Z949_1921; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000284407; 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; cd16432; CheB_Rec; 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; 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:UP000284407}.
FT DOMAIN 146..332
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 332 AA; 35931 MW; 276369C50483ED9C CRC64;
MSSKSIIVAT PYSADLNRWQ NILSDTPEVH IKAHAPSLME LFDKVEHGPP NVVLIESGLC
ATDEFELIVT LFDALDVRWL KFTHGDKLND GRDNASQLFK NGGLFSISLT QDDRLLIGQV
LSTAYSRQRA EPPVERMASA TSRRFKRIVL IGSSTGGVDA LKNVLSKFDA DCPPTVVVQH
TSQGFGGGLT RVLGRASGAR IKPFEPNALL RSGTVYVIAG LPQHIVLNPS NRPYLQTCSD
PPMDGHMPSI DKLFLSCVPF ANRIVGCILT GMGKDGARGL LELRKAGART LSQDRESSVV
YGMPSAAWST GASMQQVPLT AMGETILREA TL
//
