ID A4BEI3_9GAMM Unreviewed; 342 AA.
AC A4BEI3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000256|HAMAP-Rule:MF_00099};
DE EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099};
DE EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_00099};
GN Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN ORFNames=MED297_02282 {ECO:0000313|EMBL:EAR09410.1};
OS Reinekea blandensis MED297.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR09410.1, ECO:0000313|Proteomes:UP000005953};
RN [1] {ECO:0000313|EMBL:EAR09410.1, ECO:0000313|Proteomes:UP000005953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED297 {ECO:0000313|EMBL:EAR09410.1,
RC ECO:0000313|Proteomes:UP000005953};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC transduction system that modulates chemotaxis in response to various
CC stimuli. Catalyzes the demethylation of specific methylglutamate
CC residues introduced into the chemoreceptors (methyl-accepting
CC chemotaxis proteins or MCP) by CheR. Also mediates the irreversible
CC deamidation of specific glutamine residues to glutamic acid.
CC {ECO:0000256|HAMAP-Rule:MF_00099}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00099};
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, ECO:0000256|HAMAP-
CC Rule:MF_00099};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}.
CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC region which modulates catalytic activity. {ECO:0000256|HAMAP-
CC Rule:MF_00099}.
CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC regulatory domain activates the methylesterase activity.
CC {ECO:0000256|HAMAP-Rule:MF_00099}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000256|HAMAP-
CC Rule:MF_00099}.
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:EAR09410.1}.
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DR EMBL; AAOE01000010; EAR09410.1; -; Genomic_DNA.
DR RefSeq; WP_008047028.1; NZ_CH724153.1.
DR AlphaFoldDB; A4BEI3; -.
DR STRING; 314283.MED297_02282; -.
DR HOGENOM; CLU_000445_51_0_6; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000005953; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR CDD; cd17541; REC_CheB-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR HAMAP; MF_00099; CheB_chemtxs; 1.
DR InterPro; IPR008248; CheB-like.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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 Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW Rule:MF_00099}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005953}.
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 160..342
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 166
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 193
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 286
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 342 AA; 36686 MW; 84A5C920D255AEE9 CRC64;
MGIGVLIVDD SSFFRQQIKA IINAHPQLTV VGEASNGREA IEKAIRLKPS VITMDYEMPM
MDGISAVREI MRQQPTPILM FSSLTLKGAR VTLDALDAGA VDFLPKSYER VSGSNSSLKQ
VLVDKLLTLA KASSAQQTTP AAPPAKSTAS TKRYNQKFDL VLIGTSTGGP VALQKVLTQL
PAGFPSPILL IQHMPGSFTG AFAERLNTQC RIRVKEARDG EVLRAGEAYL APGGMQMMLS
GKGKLKIFEG DARLNYKPSV DLTFGSAVKY YSKHCLALVL TGMGADGREG ARLLKQAGSV
VWAQEGRTCV IDGMPSAVVK ANLADEVVPL PEIAKRLAEV VR
//
