B0R4K0 · CHEB_HALS3

Function

function

Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the Htr transducer proteins (methyl-accepting chemotaxis proteins) by CheR. Also required for Htr deamidations, at least at a specific glutamine-glutamate pair in HTR-II and a specific aspartate-glutamine pair in Htr4.

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site164
Active site191
Active site288

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionphosphorelay response regulator activity
Molecular Functionprotein-glutamate methylesterase activity
Molecular Functionprotein-glutamine glutaminase activity
Biological Processchemotaxis
Biological Processprotein deamination
Biological Processprotein demethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein-glutamate methylesterase/protein-glutamine glutaminase
  • EC number

Gene names

    • Name
      cheB
    • Ordered locus names
      OE_2416R

Organism names

Accessions

  • Primary accession
    B0R4K0
  • Secondary accessions
    • Q48300
    • Q9HQW6

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Deletion leads to the loss of both chemotactic and phototactic responses. Mutants show increased methylation of the Htr transducer proteins.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004290681-347Protein-glutamate methylesterase/protein-glutamine glutaminase
Modified residue534-aspartylphosphate

Post-translational modification

Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.

Keywords

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain3-119Response regulatory
Region132-154Disordered
Domain152-346CheB-type methylesterase

Domain

Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.

Sequence similarities

Belongs to the CheB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    347
  • Mass (Da)
    36,484
  • Last updated
    2008-04-08 v1
  • Checksum
    9691873DC8EA113B
MTEALVVDDSHFMRTVISDILEDGGVDVVGTAENGARALDAVTDVQPDVITMDVEMPEMDGIEATAEIMREQPTPILMVSALTTEDADATLEAMEKGAIDTFAKPGGTISTELSGHSEELVAAVERVASADPTAGHDVEMEPASPPDATTSEYADNPTLLIGASTGGPNVVESILASLPAEADFRVLIVQHMPDQFTSRFADRLDAASQYDITEAEDGSRIGGGEGLVARGDYHMRVSGYSNGRLRVRLDQSERLHSVRPAIDVTFKSAAERVTDPLVSVVLTGMGSDGADGVRAVKDAGGATLAQNEATSAVFGIPERAIETGCVDDVLPVDQLTEAIADSIRRTT

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict295in Ref. 1; CAA60162

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X86407
EMBL· GenBank· DDBJ
CAA60162.1
EMBL· GenBank· DDBJ
Genomic DNA
AM774415
EMBL· GenBank· DDBJ
CAP13665.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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