Difference between revisions of "PtsH"

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(Extended information on the protein)
(Expression and regulation)
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
* '''Additional information:'''  
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* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =

Revision as of 12:21, 6 January 2009

  • Description: General (non sugar-specific) component of the sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.

Gene name ptsH
Synonyms
Essential write here
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

  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation: constitutive expressed
  • Regulatory mechanism:
  • Additional information:

Biological materials

Labs working on this gene/protein

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