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Database: UniProt
Entry: A0A0S2JCL2_9GAMM
LinkDB: A0A0S2JCL2_9GAMM
Original site: A0A0S2JCL2_9GAMM 
ID   A0A0S2JCL2_9GAMM        Unreviewed;       203 AA.
AC   A0A0S2JCL2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=CMT41_02670 {ECO:0000313|EMBL:ALO33738.1};
OS   Colwellia sp. MT41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO33738.1, ECO:0000313|Proteomes:UP000065319};
RN   [1] {ECO:0000313|EMBL:ALO33738.1, ECO:0000313|Proteomes:UP000065319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MT41 {ECO:0000313|EMBL:ALO33738.1,
RC   ECO:0000313|Proteomes:UP000065319};
RA   Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA   Yayanos A., Methe B.A., Bartlett D.H.;
RT   "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT   Colwellia.";
RL   Submitted (NOV-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};
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DR   EMBL; CP013145; ALO33738.1; -; Genomic_DNA.
DR   RefSeq; WP_057179617.1; NZ_CP013145.1.
DR   AlphaFoldDB; A0A0S2JCL2; -.
DR   STRING; 58049.CMT41_02670; -.
DR   KEGG; com:CMT41_02670; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000065319; Chromosome.
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:UP000065319}.
FT   DOMAIN          10..191
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   203 AA;  21830 MW;  1180198E56E8F2EF CRC64;
     MAANNNALYQ ALVIGVSAGG LNALHKILPK LPINFPLAII VLQHRGEIVF EGASHNDFLI
     SYFNNDCAMP VKEAMLGAKI KPGNIYIAPA KYHLLIEKSK IFALSLEPPV NFALPSIDVL
     FDSASACYKN QLIGLILTGA SSDGSIGLKN ISDRAGLTLV QAPRTAEVDF MPKAAIYLHT
     VDHILPLNDI APFLCHLMQG DKG
//
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