ID W4Q218_9BACI Unreviewed; 347 AA.
AC W4Q218;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=JCM9140_2005 {ECO:0000313|EMBL:GAE25980.1};
OS Halalkalibacter wakoensis JCM 9140.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE25980.1, ECO:0000313|Proteomes:UP000018890};
RN [1] {ECO:0000313|EMBL:GAE25980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE25980.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
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:GAE25980.1}.
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DR EMBL; BAUT01000016; GAE25980.1; -; Genomic_DNA.
DR RefSeq; WP_034745086.1; NZ_BAZN01000016.1.
DR AlphaFoldDB; W4Q218; -.
DR STRING; 1236970.JCM9140_2005; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000018890; 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|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; 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:UP000018890}.
FT DOMAIN 6..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 152..347
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 191
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 289
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 347 AA; 38062 MW; 4615A013AFF358F0 CRC64;
MTKQYGVLVV DDSAFMRKTI SGLIEMSPYL FVIGKARNGI DAIEKIKRLK PAIVTLDIEM
PELNGLSALE KIMEECPVPV VMLSNGADST LEAFELGAVD FLVKETLIKD ITEKALEEVH
NRLVTAANAK LPKIVAVKTK PTILKEDLIL KEQMNKNLLI IGSSTGGPSA LQSILTRFPS
DFSIPIVVIQ HMPPGFTKPL AERFDGLCSL QVKEAEHHDI LEAGTIYIAP AGLQTTIQKT
TSNHYQVKLK ISAPIETLYK PSVDVTLLSV AELSKNQLLT VILTGMGDDG LRGGRKVKQF
GGTLLAESEE TCIVYGMPKV VFEAGLVDKQ VPLPEMYDEI MHFLYLD
//
