Difference between revisions of "PtsI"

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(Extended information on the protein)
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**pyrophosphate/phosphate carrier histidine (central Domain)
 
**pyrophosphate/phosphate carrier histidine (central Domain)
  
* '''Modification:''' transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-44 or Ser-46
+
* '''Modification:''' transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-44 or Ser-46 [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
  
 
* '''Cofactor(s):''' Magnesium
 
* '''Cofactor(s):''' Magnesium

Revision as of 18:35, 14 January 2009

  • Description: Enzyme I, general (non sugar-specific) component of the PTS. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr)

Gene name ptsI
Synonyms
Essential no
Product phosphotransferase system (PTS) enzyme I
Function PTS-dependent sugar transport
MW, pI 62,9 kDa, 4.59
Gene length, protein length 1710 bp, 570 amino acids
Immediate neighbours pstH, splA
Gene sequence (+200bp) Protein sequence
Genetic context
PtsI context.gif



The gene

Basic information

  • Coordinates: 1458959 - 1460668

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to HPr (His-15)
  • Protein family: PEP-utilizing enzyme family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • HPr binding site (N-Terminal Domain)
    • pyruvate binding site (C-Terminal Domain)
    • pyrophosphate/phosphate carrier histidine (central Domain)
  • Modification: transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-44 or Ser-46 PubMed
  • Cofactor(s): Magnesium
  • Effectors of protein activity:
  • Interactions:
  • Localization: Cytoplasm

Database entries

  • Structure:
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Regulatory mechanism: ptsG: transcriptional antitermination via the GlcT-dependent RNA-switch
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
  2. Pompeo F, Luciano J, Galinier A. (2007) Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in Bacillus subtilis? J Bacteriol. 189(3): 1154-7. PubMed
  3. Arnaud M, Vary P, Zagorec M, Klier A, Débarbouillé M, Postma P, Rapoport G (1992) Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity. J Bacteriol 174:3161-3170. PubMed
  4. Deutscher, J., Kessler, U., Alpert, C. A., and Hengstenberg, W. (1984) Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-ser-HPr and its possible regulatory function. Biochemistry 23: 4455-4460. DOI:10.1021/bi00314a033
  5. Deutscher, J., Küster, E., Bergstedt, U., Charrier, V., and Hillen, W. (1995) Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol. Microbiol. 15: 1049-1053. PubMed
  6. Eisermann, R., Deutscher, J., Gonzy-Tréboul, G., and Hengstenberg, W. (1988) Site-directed mutagenesis with the ptsH gene of Bacillus subtilis. J Biol Chem 263: 17050-17054. PubMed
  7. Frisby, D., and Zuber, P. 1994. Mutations in pts cause catabolite-resistant sporulation and altered regulation of spo0H in Bacillus subtilis. J. Bacteriol. 176: 2587-2595. PubMed
  8. Galinier A, Deutscher J, Martin-Verstraete I: (1999) Phosphorylation of either Crh or HPr mediates binding of CcpA to the Bacillus subtilis xyn cre and catabolite repression of the xyn operon. J Mol Biol , 286:307-314. PubMed
  9. Görke, B., Fraysse, L. & Galinier, A. (2004) Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis. J. Bacteriol. 186, 2992-2995 . PubMed
  10. Lindner, C., Galinier, A., Hecker, M. & Deutscher, J. (1999) Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31, 995-1006 . PubMed
  11. Lindner, C., Hecker, M., Le Coq, D. & Deutscher, J. (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184, 4819-4828 . PubMed
  12. Martin-Verstraete, I., Charrier, V., Stülke, J., Galinier, A., Erni, B., Rapoport, G., & Deutscher, J. (1998) Antagonistic effects of dual PTS catalyzed phosphorylation on the Bacillus subtilis transcriptional activator LevR. Mol. Microbiol. 28: 293-303. PubMed
  13. Martin-Verstraete, I., Deutscher, J., and Galinier, A. (1999) Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon. J Bacteriol 181: 2966-2969. PubMed
  14. Reizer, J., Sutrina, S. L., Saier, Jr., M. H., Stewart, G. C., Peterkofsky, A., and Reddy, P. (1989) Mechanistic and physiological consequences of HPr(Ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: studies with site-specific mutants of HPr. EMBO J 8: 2111-2120. PubMed
  15. Schmalisch, M., Bachem, S. & Stülke, J. (2003) Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation: Elucidation of the phosphorylation chain leading to inactivation of GlcT. J. Biol. Chem. 278: 51108-51115. PubMed
  16. Schumacher, M. A. et al. (2004) Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118, 731-741 . PubMed
  17. Singh, K. D., Halbedel, S., Görke, B. & Stülke, J. (2007) Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: implication of the protein phosphatase PrpC. J. Mol. Microbiol. Biotechnol. 13: 165-171. PubMed
  18. 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
  19. Stülke, J., Martin-Verstraete, I., Charrier, V., Klier, A., Deutscher, J. & Rapoport, G. (1995) The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon. J. Bacteriol. 177: 6928-6936. PubMed
  20. Tortosa, P., Aymerich, S., Lindner, C., Saier, M.H., Jr., Reizer, J. and Le Coq, D. (1997) Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system. J. Biol. Chem. 272, 17230-17237. PubMed