AC   MF_00099;
DC   Protein; auto
TR   HAMAP; MF_00099; -; 1; level=0
XX
Names: CheB_chemtxs
XX
ID   CHEB
DE   RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase;
DE            EC=3.1.1.61;
DE            EC=3.5.1.44;
GN   Name=cheB;
XX
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   -!- 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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC       region which modulates catalytic activity.
case <FTTag:phospho>
CC   -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC       regulatory domain activates the methylesterase activity.
end case
CC   -!- SIMILARITY: Belongs to the CheB family.
XX
DR   Pfam; PF01339; CheB_methylest; 1; trigger=no
DR   Pfam; PF00072; Response_reg; 1; trigger=no
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1; trigger=no
DR   PROSITE; PS50122; CHEB; 1; trigger=yes
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1; trigger=yes
XX
KW   Chemotaxis
KW   Cytoplasm
KW   Hydrolase
case <FTTag:phospho>
KW   Phosphoprotein
end case
XX
GO   GO:0008984; F:protein-glutamate methylesterase activity
GO   GO:0050568; F:protein-glutamine glutaminase activity
GO   GO:0006935; P:chemotaxis
GO   GO:0007165; P:signal transduction
GO   GO:0000160; P:phosphorelay signal transduction system
GO   GO:0018277; P:protein deamination
GO   GO:0006482; P:protein demethylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: CHEB_ECOLI (P07330)
FT   ACT_SITE        164
FT   Condition: S
FT   ACT_SITE        190
FT   Condition: H
FT   ACT_SITE        286
FT   Condition: D
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT   Tag: phospho; Condition: D
XX
Size: 334-424;
Related: None;
Template: P07330; P04042; O87125; Q9I6V9;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in KORVE, ANADE, BORA1, BRADU, BURO1, BURTA, CAUVC, CHRVO, DESVH,
 GEOMG, GEOSL, HAHCH, LEPIC, LEPIN, MAGSA, METAC, METHJ, METMA, MYXXD, PSEAE,
 PSEPK, PSESM, CUPMC, RHIJ3, RHIME, ALBFT, RHOPA, RHOPB, RHORT, SACD2, SHEDO,
 SHEON, SHESM, SHESR, SYNAS, SYNWW, VIBCH, VIBVU, VIBVY, XANAC, XANCP, XANOM
Plasmid: in CUPMC, RALN1, RHILO, RHIME
Comments: Gammaproteobacteria gene names for multiple proteins are based on the
 characterized PSEAE genes, see:
 PubMed=12142407;
 Ferrandez A., Hawkins A.C., Summerfield D.T., Harwood C.S.;
 "Cluster II che genes from Pseudomonas aeruginosa are required for an
 optimal chemotactic response.";
 J. Bacteriol. 184:4374-4383(2002).
 Alphaproteobacteria gene names for multiple proteins are based on operon
 organization as discussed in:
 PubMed=11934495;
 Hauwaerts D., Alexandre G., Das S.K., Vanderleyden J., Zhulin I.B.;
 "A major chemotaxis gene cluster in Azospirillum brasilense and
 relationships between chemotaxis operons in alpha-proteobacteria.";
 FEMS Microbiol. Lett. 208:61-67(2002).
 There are cheB-like proteins without the N-terminal regulatory domain in
 MYXXA (frzB), BORBU (BB0415), LEPIC (cheB2) and LEPIN (cheB2).
 CHEB3_RHOSH is missing the conserved D for phosphorylation.
 Possible wrong start in RHOCE
XX
# Revision 1.65 2023/11/28
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