ID A0A1W6P0B3_9RHOB Unreviewed; 310 AA.
AC A0A1W6P0B3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN Name=cheB {ECO:0000313|EMBL:ARO14841.1};
GN ORFNames=BVG79_01495 {ECO:0000313|EMBL:ARO14841.1};
OS Ketogulonicigenium robustum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ketogulonicigenium.
OX NCBI_TaxID=92947 {ECO:0000313|EMBL:ARO14841.1, ECO:0000313|Proteomes:UP000242447};
RN [1] {ECO:0000313|EMBL:ARO14841.1, ECO:0000313|Proteomes:UP000242447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPU_B003 {ECO:0000313|EMBL:ARO14841.1,
RC ECO:0000313|Proteomes:UP000242447};
RA Li Y., Liu L., Wang C., Zhang M., Zhang T., Zhang Y.;
RT "Ketogulonicigenium robustum SPU B003 Genome sequencing and assembly.";
RL Submitted (FEB-2017) 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; CP019937; ARO14841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6P0B3; -.
DR STRING; 92947.BVG79_01495; -.
DR KEGG; kro:BVG79_01495; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000242447; 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:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR008248; CheB-like.
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 PIRSF; PIRSF000876; RR_chemtxs_CheB; 2.
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:UP000242447}.
FT DOMAIN 102..303
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 310 AA; 32151 MW; 7170D8D773D4F725 CRC64;
MSEPLLLIVD ADSTRRHHLI RACLLAAPGM RVAGAGHASE AEMLLDARRP QRIAVADGVE
NRASVIAKAR ITGVDCLIFA AGGGSFSEMA QQIISGIRVH PPASVVTYGA AISQLILIGA
STGGIAAIEK ILTTFPADCP PVLLVQHIRD GFAEGFVRRL DQILAPQVRV AAEGVILTPG
TIHVAARSDR HLGVTRRAGV LRSRLLAGPP VAGHSPSVDV LFSDGAALAP EIDVRAALLT
GMGADGANGM CAIYDAGGHT IAQDRDSSVV WGMPRMAVER GGVSEVLPLN RIAAALLRTG
EAARAPAPLR
//
