C3LED2 · HPRK_BACAC
- ProteinHPr kinase/phosphorylase
- GenehprK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids309 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on a specific serine residue. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
Miscellaneous
Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.
Catalytic activity
- [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H+
- [HPr protein]-O-phospho-L-serine + H+ + phosphate = [HPr protein]-L-serine + diphosphate
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 138 | |||||
Sequence: H | ||||||
Binding site | 153-160 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GQSGVGKS | ||||||
Active site | 159 | |||||
Sequence: K | ||||||
Binding site | 160 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 177 | Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activity | ||||
Sequence: D | ||||||
Binding site | 202 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 243 | |||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphorelay sensor kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein serine/threonine/tyrosine kinase activity | |
Biological Process | regulation of carbohydrate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHPr kinase/phosphorylase
- EC number
- Short namesHPrK/P
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionC3LED2
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000165067 | 1-309 | HPr kinase/phosphorylase | |||
Sequence: MPKVRTKDLIEQFQLELISGEEGIHRPIDTSDLSRPGIEMAGFFTYYPADRVQLLGKTELTFFDTLTSDQKQERMKALCTEETPCIIVTRNQDVPDELLQASRESGMPLLRSSQTTTRLSSRLTNYLEGKLAPTTAVHGVLVDIYGVGVLITGQSGVGKSETALELVKRGHRLVADDSVEIRQEDEDMLVGSSPDLIEHLLEIRGLGIINVMTLFGAGAVRNYKRITLVINLEIWDQKKNYDRLGLDEEKMKIIDTELTKITLPVRPGRNLAVIIEVAAMNFRLKRMGVNAAQQFSERLMSAIELGNQE |
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 201-210 | Important for the catalytic mechanism of both phosphorylation and dephosphorylation | ||||
Sequence: LEIRGLGIIN | ||||||
Region | 264-269 | Important for the catalytic mechanism of dephosphorylation | ||||
Sequence: PVRPGR |
Domain
The Walker A ATP-binding motif also binds Pi and PPi.
Sequence similarities
Belongs to the HPrK/P family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)34,587
- Last updated2009-06-16 v1
- Checksum4CF32C76AC8BE6E7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001215 EMBL· GenBank· DDBJ | ACP14549.1 EMBL· GenBank· DDBJ | Genomic DNA |