Q30ZJ5 · CHEB2_OLEA2
- ProteinProtein-glutamate methylesterase/protein-glutamine glutaminase 2
- GenecheB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids356 (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
- [protein]-L-glutamate 5-O-methyl ester + H2O = L-glutamyl-[protein] + methanol + H+
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 177 | ||||
Active site | 203 | ||||
Active site | 299 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | phosphorelay response regulator activity | |
Molecular Function | protein-glutamate methylesterase activity | |
Molecular Function | protein-glutamine glutaminase activity | |
Biological Process | chemotaxis | |
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 2
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Oleidesulfovibrio
Accessions
- Primary accessionQ30ZJ5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000225459 | 1-356 | Protein-glutamate methylesterase/protein-glutamine glutaminase 2 | ||
Modified residue | 57 | 4-aspartylphosphate | |||
Post-translational modification
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 6-123 | Response regulatory | |||
Domain | 165-356 | 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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length356
- Mass (Da)38,050
- Last updated2005-12-06 v1
- MD5 ChecksumB2AF41D464059F53173FC0B723F68A83
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000112 EMBL· GenBank· DDBJ | ABB38901.1 EMBL· GenBank· DDBJ | Genomic DNA |