PtsI

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  • Description: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar 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 transfers phosphate from PEP to HPr
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:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine
  • 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: phosphorylation (Ser-44 or Ser-46)
  • 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

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