HAMAP

Accession	MF_00099
Dates	1-JUN-2001 (Created) 9-DEC-2011 (Last updated, Version 47)

Data class

Protein

Predictors

HAMAP; MF_00099; [distribution of match scores in UniProtKB];[seed alignment for MF_00099]

Names

CheB_methylest

Identifier

CHEB

Protein name

RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase; EC=3.1.1.61;

Gene name

cheB

FUNCTION: Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR (By similarity).

CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O = protein L-glutamate + methanol.

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

DOMAIN: The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain.

PTM: Phosphorylated by CheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain (By similarity).

SIMILARITY: Contains 1 cheB-type methylesterase domain.

SIMILARITY: Contains 1 response regulatory domain.

Pfam	PF01339; CheB_methylest; 1; PF00072; Response_reg; 1;
PIRSF	PIRSF000876; RR_chemtxs_CheB; 1;
PROSITE	PS50122; CHEB; 1; trigger=PRU00050; PS50110; RESPONSE_REGULATORY; 1; trigger=PRU00169;

Cytoplasm, Hydrolase, Chemotaxis.

Phosphoprotein.

GO:0008984; Molecular function: protein-glutamate methylesterase activity.
GO:0004871; Molecular function: signal transducer activity.
GO:0007606; Biological process: sensory perception of chemical stimulus.
GO:0006935; Biological process: chemotaxis.
GO:0007165; Biological process: signal transduction.
GO:0000160; Biological process: two-component signal transduction system (phosphorelay).
GO:0005737; Cellular component: cytoplasm.

From: CHEB_ECOLI (P07330)
Key		From		To		Description		Condition		FTGroup
ACT_SITE		164		164		By similarity		S
ACT_SITE		190		190		By similarity		H
ACT_SITE		286		286		By similarity		D
MOD_RES		56		56		4-aspartylphosphate (By similarity)		D

Size range:	334-424 amino acids
Related UniRules:	None
Template:	P07330 (CHEB_ECOLI); O87125 (CHEB1_PSEAE); Q9I6V9 (CHEB2_PSEAE); P04042 (CHEB_SALTY): [Recover all]
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	in KORVE, ANADE, BORA1, BRAJA, BURCA, BURTA, CAUCR, CHRVO, DESVH, GEOMG, GEOSL, HAHCH, LEPIC, LEPIN, MAGSA, METAC, METHJ, METMA, MYXXD, PSEAE, PSEPK, PSESM, RALME, RHIL3, RHIME, RHOFD, RHOPA, RHOPB, RHORT, SACD2, SHEDO, SHEON, SHESM, SHESR, SYNAS, SYNWW, VIBCH, VIBVU, VIBVY, XANAC, XANCP, XANOM
Plasmid encoded:	in RALME, RALSO, 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