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Database: UniProt
Entry: J2VSB5_9BURK
LinkDB: J2VSB5_9BURK
Original site: J2VSB5_9BURK 
ID   J2VSB5_9BURK            Unreviewed;       136 AA.
AC   J2VSB5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
DE   Flags: Fragment;
GN   ORFNames=PMI40_00907 {ECO:0000313|EMBL:EJN09082.1};
OS   Herbaspirillum sp. YR522.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJN09082.1, ECO:0000313|Proteomes:UP000007507};
RN   [1] {ECO:0000313|EMBL:EJN09082.1, ECO:0000313|Proteomes:UP000007507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR522 {ECO:0000313|EMBL:EJN09082.1,
RC   ECO:0000313|Proteomes:UP000007507};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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:EJN09082.1}.
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DR   EMBL; AKJA01000022; EJN09082.1; -; Genomic_DNA.
DR   AlphaFoldDB; J2VSB5; -.
DR   STRING; 1144342.PMI40_00907; -.
DR   PATRIC; fig|1144342.3.peg.835; -.
DR   eggNOG; COG2201; Bacteria.
DR   Proteomes; UP000007507; 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:InterPro.
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: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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007507}.
FT   DOMAIN          1..128
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EJN09082.1"
SQ   SEQUENCE   136 AA;  13984 MW;  6D1E121EECACA851 CRC64;
     PPLPVRLAGE GDLPQAGQVL LAGDNKHLVF RGGGVLGYMA GAASDVYRPS VDMFFHSVVK
     YWQAPAVGIL LTGMGRDGAA GLKAMREHGS HTIAQDQASC AVYGMPKAAV ALDAAVEVLP
     VSGIAARLQG LLATFS
//
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