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Database: UniProt
Entry: A0A495J150_9SPHI
LinkDB: A0A495J150_9SPHI
Original site: A0A495J150_9SPHI 
ID   A0A495J150_9SPHI        Unreviewed;       205 AA.
AC   A0A495J150;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=BDD43_2875 {ECO:0000313|EMBL:RKR82690.1};
OS   Mucilaginibacter gracilis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=423350 {ECO:0000313|EMBL:RKR82690.1, ECO:0000313|Proteomes:UP000268007};
RN   [1] {ECO:0000313|EMBL:RKR82690.1, ECO:0000313|Proteomes:UP000268007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18602 {ECO:0000313|EMBL:RKR82690.1,
RC   ECO:0000313|Proteomes:UP000268007};
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 (OCT-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:RKR82690.1}.
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DR   EMBL; RBKU01000001; RKR82690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495J150; -.
DR   Proteomes; UP000268007; 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: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:UP000268007}.
FT   DOMAIN          12..191
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   205 AA;  22204 MW;  F6D7CBB1D079A9C0 CRC64;
     MDSDNYENLL KRLSAAEVVI LGGSAGSFTP IFNIIKMLPQ TYNKAIVIVI HRGKNNFSDI
     ENLFGDNCRI LVSEITDKDK ITGGHVYIAP ANYHTLFEKR KTFALDVSEQ VWYSKPSIDV
     TFESAADAYG DKCAAILLSG ANQDGASGLL KLRNKGALTI VQRPTDAEIG IMPQAAVDIN
     AGEFILTSSE ILKLISASST ETQSS
//
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