A0A1G0M0A4 · A0A1G0M0A4_9BACT
- ProteinProtein-glutamate methylesterase/protein-glutamine glutaminase
- GenecheB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids343 (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 | 166 | |||||
Sequence: S | ||||||
Active site | 193 | |||||
Sequence: H | ||||||
Active site | 285 | |||||
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 |
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
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfuromonadia > Geobacterales > Geobacteraceae
Accessions
- Primary accessionA0A1G0M0A4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 55 | 4-aspartylphosphate | ||||
Sequence: D |
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 | 4-122 | Response regulatory | ||||
Sequence: NILLADDSGLVRQVLTDMLHQSPDIRVVGCACNGSDAVDLTLSLKPDLVIMDLVMPVMDGLAAIEEIMSVAPTPVLVLSAAVEATELSRAFHAIKRGALDVMEKPAVDIPGALDDFRSR | ||||||
Domain | 156-343 | CheB-type methylesterase | ||||
Sequence: PVPKLLAIGASTGGPKAVMSLLKTLPADFPATVFVVQHIADGFAEGFATWLDRECAISVRIAVDGAKYGPGEAVVAPGSSHMTISDGRIRLRDDPPVNCCRPSIDVFFNSLAQTTCNQVVSLLLTGMGKDGAQGLLRIKERGGTTLVQDENSCAVFGMPKEAIKLNAVDRVLPLECMPAAISKLFAVR |
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
- Length343
- Mass (Da)36,577
- Last updated2017-02-15 v1
- ChecksumAF8A11D280ADEF11