Difference between revisions of "PtsH"

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(Database entries)
(Labs working on this gene/protein)
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
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[[Boris Görke]], University of Göttingen, Germany
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[http://wwwuser.gwdg.de/~genmibio/goerke.html Homepage]
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[[Anne Galinier]], University of Marseille, France
  
 
=Your additional remarks=
 
=Your additional remarks=

Revision as of 16:51, 9 January 2009

  • Description: General component of the sugar phosphotransferase system (PTS).

Gene name ptsH
Synonyms
Essential no
Product histidine-containing phosphocarrier protein of the PTS
Function mediates carbon catabolite repression (CCR)
MW, pI 9,1 kDa, 4.58
Gene length, protein length 264 bp, 88 amino acids
Immediate neighbours ptsG, ptsI
Gene sequence (+200bp) Protein sequence
Genetic context
File:GenE context.gif












The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine
  • Protein family: HPr family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: HPr Domain (2–88)
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: Cytoplasm

Database entries

  • Structure: NCBI, complex of L. Casei HprK with B. Subtilis HPr NCBI, complex of L. Casei HprK with B. Subtilis HPr-Ser-P NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Regulation: induction by glucose (ptsG), constitutive (ptsH)
  • Regulatory mechanism: ptsG: transcriptional antitermination via the GlcT-dependent RNA-switch
  • Additional information:

Biological materials

Labs working on this gene/protein

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

Your additional remarks

References

  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
  2. Macek B, Mijakovic I, Olsen JV (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 6(4): 697-707. PubMed
  3. Mahr K, Esteban CD, Hillen W (2002) Cross communication between components of carbon catabolite repression of Lactobacillus casei and Bacillus megaterium. J Mol Microbiol Biotechnol. 4(5): 489-94. PubMed
  4. Juy M, Penin F, Favier A, Galinier A (2003) Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr J Mol Biol. 332(4): 767-76. PubMed
  5. Müller W, Horstmann N, Hillen W (2006) The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr-Ser46-P in Bacillus subtilis FEBS J. 273(6): 1251-61. PubMed
  6. Lavergne JP, Jault JM, 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(20): 6218-25. PubMed