HprK
- Description: HPr kinase/ phosphorylase
| Gene name | hprK |
| Synonyms | ptsK, yvoB |
| Essential | |
| Product | HPr kinase/ phosphorylase |
| Function | phosphorylation of HPr and Crh proteins at Ser46 |
| MW, pI | 34 kDa, 4.906 |
| Gene length, protein length | 930 bp, 310 aa |
| Immediate neighbours | |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
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Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
no carbon catabolite repression
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Josef Deutscher, Paris-Grignon, France
Jörg Stülke, University of Göttingen, Germany Homepage
Wolfgang Hillen, Erlangen University, Germany Homepage
Anne Galinier, University of Marseille, France
Your additional remarks
References
- Reizer, J., Hoischen, C., Titgemeyer, F., Rivolta, C., Rabus, R., Stülke, J., Karamata, D., Saier, M. H., Jr., & Hillen, W. (1998) A novel bacterial protein kinase that controls carbon catabolite repression. Mol. Microbiol. 27: 1157-1169. PubMed
- Hanson K. G., Steinhauer, K., Reizer, J., Hillen, W. & Stülke, J. (2002) HPr kinase/phosphatase of Bacillus subtilis: Expression of the gene and effects of mutations on enzyme activity, growth, and carbon catabolite repression. Microbiology 148: 1805-1811. PubMed
- Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002) Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol. Microbiol. 45: 543-553. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
