A0A8A3S1D6 · A0A8A3S1D6_9EURY
- ProteinProtein-glutamate methylesterase/protein-glutamine glutaminase
- GenecheB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids344 (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
- L-glutaminyl-[protein] + H2O = L-glutamyl-[protein] + NH4+
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 153 | ||||
Active site | 180 | ||||
Active site | 281 | ||||
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 | |
Biological Process | protein deamination | |
Biological Process | protein demethylation |
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 lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanomicrobiales > Methanomicrobiaceae > Methanofollis
Accessions
- Primary accessionA0A8A3S1D6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 54 | 4-aspartylphosphate | |||
Post-translational modification
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-121 | Response regulatory | |||
Domain | 141-339 | CheB-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 statusComplete
- Length344
- Mass (Da)37,107
- Last updated2021-09-29 v1
- ChecksumADC6C465C0E33995
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP036172 EMBL· GenBank· DDBJ | QSZ66287.1 EMBL· GenBank· DDBJ | Genomic DNA |