A0A8J2Z7E1 · A0A8J2Z7E1_9PROT
- ProteinProtein-glutamate methylesterase/protein-glutamine glutaminase
- GenecheB2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids446 (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 | 258 | |||||
Sequence: S | ||||||
Active site | 285 | |||||
Sequence: H | ||||||
Active site | 383 | |||||
Sequence: D |
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
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Caldovatus
Accessions
- Primary accessionA0A8J2Z7E1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 74 | 4-aspartylphosphate | ||||
Sequence: D |
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, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-143 | Response regulatory | ||||
Sequence: RVMLCDDSAVVRGALARLLRADPAIRIVAQVGDGRAALAALADARPEVVLLDLEMPVMDGMTALPLLLRQPAELRPAVIVASALTQRGAAAAMAALRAGAADYLPKPAAAGGGMADPLFRA | ||||||
Region | 158-247 | Disordered | ||||
Sequence: RQRMPASAPRTADAAAVARRGAGRPGPAPSGRATPRVPAPWPAGPEAATHAAVARRTAALPRAVPPPDRAAPPAAVRPEGTPDRAAAASR | ||||||
Domain | 246-441 | CheB-type methylesterase | ||||
Sequence: SRTAPRVVVIGASTGGPQALAALVRRLPSAPTVPVLVVQHMPPGFTAMLADHLGRLGGPPAAEAREGEPLRPGRLYLAPGDRHLLVEAGTEGALFARLSDGPAENFCRPALDPLLRSLVAACGGARLLVVVLTGMGQDGLAGCRAVAAAGGQVLAQDEASSVVWGMPGAVARAGLARVVAPPEVLAERIAAALSGP |
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
- Length446
- Mass (Da)44,895
- Last updated2022-05-25 v1
- Checksum1D8674E88D043BEF
Keywords
- Technical term