Difference between revisions of "HprK"

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|style="background:#ABCDEF;" align="center"|'''Function''' || carbon catabolite repression,<br/>phosphorylation of HPr and Crh proteins at Ser46
 
|style="background:#ABCDEF;" align="center"|'''Function''' || carbon catabolite repression,<br/>phosphorylation of HPr and Crh proteins at Ser46
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 34 kDa, 4.906   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 34 kDa, 4.906   

Revision as of 12:31, 11 June 2009

  • 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
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
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
HprK context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU35000

Phenotypes of a mutant

no carbon catabolite repression

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + HPr = ADP + P-Ser-HPr (according to Swiss-Prot)
  • Protein family: HPrK/P family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • 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)
  • KEGG entry: [2]
  • E.C. number:

Additional information

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

Your additional remarks

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