HprK

• Description: HPr kinase/ phosphorylase
  
  

Gene name	hprK
Synonyms	ptsK, yvoB
Essential	no
Product	HPr kinase/ phosphorylase
Function	carbon catabolite repression, phosphorylation of HPr and Crh proteins at Ser46
MW, pI	34 kDa, 4.906
Gene length, protein length	930 bp, 310 aa
Immediate neighbours	lgt, nagA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates:

Phenotypes of a mutant

no carbon catabolite repression

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions: HprK- HPr, HprK-Crh PubMed

• Localization:

Database entries

• Structure: 1KKM (complex of Lactobacillus casei HprK with B. subtilis HPr-Ser-P), 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr)

• Swiss prot entry: O34483

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector: pGP642 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab

• 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

References

review

1. Nessler S, Fieulaine S, Poncet S, Galinier A, Deutscher J, Janin J (2003) HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate. J Bacteriol 185:4003-4010. PubMed

general/ physiology

1. 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
2. Galinier A, Kravanja M, Engelmann R, Hengstenberg W, Kilhoffer MC, Deutscher J, Haiech J (1998) New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression. Proc Natl Acad Sci USA 95:1823-1828. PubMed
3. 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
4. Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. PubMed

enzymatic properties, mutation analysis

1. Mijakovic I, Poncet S, Galiner A, Monedero V, Fieulaine S, Janin J, Nessler S, Marquez JA, Scheffzek K, Hasenbein S, Hengstenberg W, Deutscher J: Pyrophosphate-producing protein dephosphorylation by HPr kinase/ phosphorylase: a relic of early life? Proc Natl Acad Sci USA 2002, 99:13442-13447. PubMed
2. Monedero V, Poncet S, Mijakovic I, Fieulaine S, Dossonet V, Martin-Verstraete I, Nessler S, Deutscher J (2001) Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism. EMBO J 20:3928-3937. PubMed
3. 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
4. Jault J M, Fieulaine S, Nessler S, Gonzalo P, Di Pietro A, Deutscher J, Galinier A (2000) The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J Biol Chem 275:1773-1780. PubMed
5. Ramström H, Sanglier S, Leize-Wagner E, Philippe C, van Dorsselaer A, Haiech J (2003) Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis. J Biol Chem 278:1174-1185. PubMed
6. Galinier, A., Lavergne, J.-P., Geourjon, C., Fieulaine, S., Nessler, S. & Jault, J.-M. (2002) A new family of phosphotransferases with a P-loop motif. J. Biol. Chem. 277, 11362-11367. PubMed
7. Lavergne, J.-P., Jault, J.-M. & Galinier, A. (2002) Insights into the functioning of Bacillus subtilis HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate. Biochemistry 41, 6218-6225. PubMed
8. Pompeo, F., Granet, Y., Lavergne, J.-P., Grangeasse, C., Nessler, S., Jault, J.-M. & Galinier, A. (2003) Regulation and mutational analysis of the HPr kinase/phosphorylase from Bacillus subtilis. Biochemistry 42, 6762-6771. PubMed

structure analysis

1. Márquez, J. A., Hasenbein, S., Koch, B., Fieulaine, S., Nessler, S., Russell, R. B., Hengstenberg, W. & Scheffzek, K. (2002) Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: mimicking the product/substrate of the phosphotransfer reactions. Proc. Natl. Acad. Sci. USA 99, 3458-3463. PubMed
2. Allen, G.S., Steinhauer, K., Hillen, W., Stülke, J. & Brennan, R.G. (2003) Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae. J. Mol. Biol. 326, 1203-1217. PubMed
3. Fieulaine, S., Morera, S., Poncet, S., Mijakovic, I., Galinier, A., Janin, J., Deutscher, J., and Nessler, S. (2002) X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc Natl Acad Sci U S A 99: 13437-13441. PubMed

HprK as target for antimicrobial compounds

1. Ramström, H. et al. (2004) Heterocylic bis-cations as starting hits for design of inhibitors of the bifunctional enzyme histidine-containing protein kinase/ phosphatase from Bacillus subtilis. J. Med. Chem. 47, 2264-2275. PubMed

1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed