ID K9DCZ3_9BURK Unreviewed; 339 AA.
AC K9DCZ3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=HMPREF9710_02571 {ECO:0000313|EMBL:EKU82123.1};
OS Massilia timonae CCUG 45783.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU82123.1, ECO:0000313|Proteomes:UP000009874};
RN [1] {ECO:0000313|EMBL:EKU82123.1, ECO:0000313|Proteomes:UP000009874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU82123.1,
RC ECO:0000313|Proteomes:UP000009874};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Massilia timonae CCUG 45783.";
RL Submitted (SEP-2012) 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:EKU82123.1}.
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DR EMBL; AGZI01000030; EKU82123.1; -; Genomic_DNA.
DR RefSeq; WP_005667008.1; NZ_JH992923.1.
DR AlphaFoldDB; K9DCZ3; -.
DR PATRIC; fig|883126.3.peg.2594; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_1_4; -.
DR OrthoDB; 9791760at2; -.
DR Proteomes; UP000009874; 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; IPR011247; Chemotax_prot-Glu_Me-esterase.
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 PIRSF; PIRSF036461; Chmtx_methlestr; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT DOMAIN 1..190
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 10
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 339 AA; 36782 MW; 6CCD1AF166F5D424 CRC64;
MTKIVVIGGS AGALDALKII LPMLPHDFPS AILIVTHIGS QKSIIPDILG RCCAMPVRHA
TDDEPIIPGR VLVAPPDEHL TVVTRDGRSY VRLLHGPREN HCRPAIDPLF RSAATAFLAD
TIGVLLSGYL DDGTVGLQAV KACGGTVIVQ DPLEAKAMDM PASALQHVDV DRVLRTADIA
PALVGLATAS VRPGIRGHDT AVPDVPKWIG VENRIISRDS AMDDLEQIGE PSSLTCPECS
GALWEVGPQA PIRYRCHTGH AFSAKVLETL QRDAVEDAIW GSVRALHEQE RLFSKLSERE
RQTGQMERAA EYQTKAMQAR EHSRILREVV VKRALVVKT
//