Difference between revisions of "HprK"

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(References)
(References)
Line 128: Line 128:
 
=References=
 
=References=
  
 +
'''review'''
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12837773 PubMed]
 +
 +
'''general/ physiology'''
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/9570401 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/9570401 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/9465101 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/9465101 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
 +
 +
'''enzymatic properties, mutation analysis'''
 
# 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.  [http://www.ncbi.nlm.nih.gov/sites/entrez/12359880 PubMed]
 
# 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.  [http://www.ncbi.nlm.nih.gov/sites/entrez/12359880 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11483496 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11483496 PubMed]
Line 135: Line 143:
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/10636874 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/10636874 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12411438 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12411438 PubMed]
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12837773 PubMed]
+
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11796714 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
+
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12009882 PubMed]
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
+
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12779331 PubMed]
 +
 
 +
'''structure analysis'''
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11904409 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11904409 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12589763 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12589763 PubMed]
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11796714 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12009882 PubMed]
 
# Pompeo, F., Granet, Y., Lavergne, J.-P., Grangeasse, C., Nessler, S., Jault, J.-M. & Galinier, A. (2003) Regulation and mutational of the HPr kinase/phosphorylase from ''Bacillus subtilis''. Biochemistry 42, 6762-6771. [http://www.ncbi.nlm.nih.gov/sites/entrez/12779331 PubMed]
 
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359875 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359875 PubMed]
 +
 +
'''HprK as target for antimicrobial compounds'''
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/15084125 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/15084125 PubMed]
  
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 20:28, 7 February 2009

  • 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
HprK context.gif



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

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