A0A0C1YB14 · A0A0C1YB14_9CYAN
- ProteinProtein-glutamate methylesterase/protein-glutamine glutaminase
- GenecheB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids362 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4+
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 179 | |||||
Sequence: S | ||||||
Active site | 206 | |||||
Sequence: H | ||||||
Active site | 299 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | methyltransferase activity | |
Molecular Function | phosphorelay response regulator activity | |
Molecular Function | protein-glutamate methylesterase activity | |
Molecular Function | protein-glutamine glutaminase activity | |
Biological Process | chemotaxis | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-glutamate methylesterase/protein-glutamine glutaminase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Oscillatoriales > Oscillatoriaceae > Lyngbya
Accessions
- Primary accessionA0A0C1YB14
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 58 | 4-aspartylphosphate | ||||
Sequence: D |
Post-translational modification
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)39,112
- Last updated2015-04-01 v1
- Checksum8DEB1F83099C4758