A0A8J2Z7E1 · A0A8J2Z7E1_9PROT

  • Protein
    Protein-glutamate methylesterase/protein-glutamine glutaminase
  • Gene
    cheB2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site258
Active site285
Active site383

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
      cheB2
    • Synonyms
      cheB
    • ORF names
      GCM10010964_00310

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CGMCC 1.16330
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Caldovatus

Accessions

  • Primary accession
    A0A8J2Z7E1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue744-aspartylphosphate

Post-translational modification

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

Keywords

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain23-143Response regulatory
Region158-247Disordered
Domain246-441CheB-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    446
  • Mass (Da)
    44,895
  • Last updated
    2022-05-25 v1
  • Checksum
    1D8674E88D043BEF
MSAAEAAGAPAGAAPPAEAEPVRVMLCDDSAVVRGALARLLRADPAIRIVAQVGDGRAALAALADARPEVVLLDLEMPVMDGMTALPLLLRQPAELRPAVIVASALTQRGAAAAMAALRAGAADYLPKPAAAGGGMADPLFRAELLEKVKGWARIRRRQRMPASAPRTADAAAVARRGAGRPGPAPSGRATPRVPAPWPAGPEAATHAAVARRTAALPRAVPPPDRAAPPAAVRPEGTPDRAAAASRTAPRVVVIGASTGGPQALAALVRRLPSAPTVPVLVVQHMPPGFTAMLADHLGRLGGPPAAEAREGEPLRPGRLYLAPGDRHLLVEAGTEGALFARLSDGPAENFCRPALDPLLRSLVAACGGARLLVVVLTGMGQDGLAGCRAVAAAGGQVLAQDEASSVVWGMPGAVARAGLARVVAPPEVLAERIAAALSGPGPRAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BMKS01000001
EMBL· GenBank· DDBJ
GGG15935.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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