P0DMI2 · CHEB_HALSA
- ProteinProtein-glutamate methylesterase/protein-glutamine glutaminase
- GenecheB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids347 (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 | 164 | ||||
Active site | 191 | ||||
Active site | 288 | ||||
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
- Strain
- Taxonomic lineageArchaea > Methanobacteriati > Methanobacteriota > Stenosarchaea group > Halobacteria > Halobacteriales > Halobacteriaceae > Halobacterium > Halobacterium salinarum NRC-34001
Accessions
- Primary accessionP0DMI2
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000158050 | 1-347 | Protein-glutamate methylesterase/protein-glutamine glutaminase | ||
Modified residue | 53 | 4-aspartylphosphate | |||
Post-translational modification
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-119 | Response regulatory | |||
Region | 132-154 | Disordered | |||
Domain | 152-346 | 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
- Length347
- Mass (Da)36,484
- Last updated2014-05-14 v1
- MD5 Checksum62F0A39CEF29D25CE85A46D1BF59B1E2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004437 EMBL· GenBank· DDBJ | AAG19394.1 EMBL· GenBank· DDBJ | Genomic DNA |