A0A2G5X2G5 · A0A2G5X2G5_9BACL
- ProteinProtein-arginine kinase
- GenemcsB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids362 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic activity
- ATP + L-arginyl-[protein] = ADP + H+ + N(omega)-phospho-L-arginyl-[protein]
Activity regulation
Appears to be allosterically activated by the binding of pArg-containing polypeptides to the pArg-binding pocket localized in the C-terminal domain of McsB.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | creatine kinase activity | |
Molecular Function | protein kinase activity | |
Biological Process | phosphocreatine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-arginine kinase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Planococcaceae > Sporosarcina
Accessions
- Primary accessionA0A2G5X2G5
Proteomes
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-252 | Phosphagen kinase C-terminal | ||||
Sequence: IVLSTRIRLARNLQDYLFPISASQEDANRVSEALNQAVKTMQNHHFTGTAMKDLSPLERQILVEKHLVSPQLINPEKHGSVLLSEDETISIMVNEEDHIRIQCIYPGFQIDQAYEQADRVDSELEVNLNYAFDETFGYLTSCPSNTGTGMRASVMMHLPALTITKQIERIIPAISRLGMVVRGSYGEGSEALGNIYQVSNQITLGKSEEEILKDLESISKRLIAHEKKS | ||||||
Motif | 335-340 | RDXXRA motif of the pArg binding pocket involved in allosteric regulation | ||||
Sequence: RDILRA |
Sequence similarities
Belongs to the ATP:guanido phosphotransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)40,812
- Last updated2018-01-31 v1
- Checksum3408045851040DF8