A0A0C1YB14 · A0A0C1YB14_9CYAN

  • 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 site179
Active site206
Active site299

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionmethyltransferase activity
Molecular Functionphosphorelay response regulator activity
Molecular Functionprotein-glutamate methylesterase activity
Molecular Functionprotein-glutamine glutaminase activity
Biological Processchemotaxis
Biological Processmethylation

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
      QQ91_001650

Organism names

  • Taxonomic identifier
  • Strain
    • BDU141951
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Oscillatoriales > Oscillatoriaceae > Lyngbya

Accessions

  • Primary accession
    A0A0C1YB14

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue584-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
    362
  • Mass (Da)
    39,112
  • Last updated
    2015-04-01 v1
  • Checksum
    8DEB1F83099C4758
MASRPIRLLLVEDSPVALAILQRLLRDHPAIEIVGIAANGVEALQLIPQVDPQIICTDLHMPKMDGLTLTREVMARFPRPILVVSASVQDEDTQNVFRLLEAGALDIFPKPRTGLAAEYEKVQQELINKIRVLSGVSVFTQHRREVRPTPLPPPPPASAIAASHQLDIRAPRVLAIGASTGGPQALQTILQALPKQFPVPILCVQHISSGFLQGLIDWLNLKSALHIKIAVAGEMPAPGTVYFPPERHHMQIDRYGRFELTQSPPVAGHCPSVTVLLESVAAYYRRSAVGIVLTGMGRDGAEGLHAIALAGGTTIAQDEATCVVFGMPKEAIALNAAQHILPIDNIAPFLLNRVFASALQNF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JTHE02000002
EMBL· GenBank· DDBJ
NEV65816.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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