GenomeNet

Database: UniProt
Entry: A0A0F3K6H7_9GAMM
LinkDB: A0A0F3K6H7_9GAMM
Original site: A0A0F3K6H7_9GAMM 
ID   A0A0F3K6H7_9GAMM        Unreviewed;       189 AA.
AC   A0A0F3K6H7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=VI08_18380 {ECO:0000313|EMBL:KJV26572.1};
OS   Luteibacter yeojuensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=345309 {ECO:0000313|EMBL:KJV26572.1, ECO:0000313|Proteomes:UP000033651};
RN   [1] {ECO:0000313|EMBL:KJV26572.1, ECO:0000313|Proteomes:UP000033651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SU11 {ECO:0000313|EMBL:KJV26572.1,
RC   ECO:0000313|Proteomes:UP000033651};
RA   Sulaiman J., Priya K., Chan K.-G.;
RT   "Draft genome sequence of Luteibacter yeojuensis strain SU11.";
RL   Submitted (MAR-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:KJV26572.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JZRB01000054; KJV26572.1; -; Genomic_DNA.
DR   RefSeq; WP_045831096.1; NZ_JZRB01000054.1.
DR   AlphaFoldDB; A0A0F3K6H7; -.
DR   PATRIC; fig|345309.4.peg.3485; -.
DR   OrthoDB; 9791760at2; -.
DR   Proteomes; UP000033651; 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; 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}.
FT   DOMAIN          1..183
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        132
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   189 AA;  19349 MW;  9F9318D2E70DAAF6 CRC64;
     MTARAAIAMG CSAGGLAALQ RVLPALDRRL AVPVVVCAHT GSADVSLLVE LLGRVSALPV
     VEAAEREPAD PGVVHVAPSG YHLLVEPNAH FSLNVDARVT YARPSIDVLF ETAAGAWKDG
     LVAVLMTGAN SDGAQGLRAV RQAGGYALVQ DPASAESDVM PRAGLDIAGA DACLPLDQIA
     ARLNQLCLP
//
DBGET integrated database retrieval system