A0A0T9PG00 · A0A0T9PG00_9GAMM

  • Protein
    Protein-glutamate methylesterase/protein-glutamine glutaminase
  • Gene
    cheB
  • 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 site164
Active site190
Active site286

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
    • ORF names
      HB980_07110

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SCPM-O-B-8025
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Yersinia

Accessions

  • Primary accession
    A0A0T9PG00

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue564-aspartylphosphate

Post-translational modification

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

Keywords

Family & Domains

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
    349
  • Mass (Da)
    37,977
  • Last updated
    2016-02-17 v1
  • MD5 Checksum
    672426AADE79C2226F8912852C677FDE
MSKIRVLCVDDSALMRQLMTEIINSHPDMEMVAAAPDPLVARDLIKKFNPQVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKNSEITMRALELGAIDFVTKPQLGIREGMLAYSELIAEKIRTAAKARLPQRGPEHAPVMLTHTPLLSSEKLIAIGASTGGTEAIRTVLQPLPPTSPALLITQHMPPGFTRSFAERLNKLCQITVKEAEDGERVLPGHAYIAPGDRHMELARSGANYQVRIHDGPAVNRHRPSVDVLFRSVAQYAGRNAVGVILTGMGNDGAAGLLEMHRAGAYTIAQNEASCVVFGMPREAIGMGGVNEILDLNQISQRMLAQISSGQALRI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAASAN010000002
EMBL· GenBank· DDBJ
NIL26314.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help