Difference between revisions of "PtsI"

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(Biological materials)
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=Biological materials =
=Biological materials =
* '''Mutant:''' GP864 (ermC), available in [[Stülke]] lab
* '''Mutant:''' GP864 (ermC), GP778 (replacement of glcT and the ptsGHI operon by a spc cassette), available in [[Stülke]] lab
* '''Expression vector:'''  
* '''Expression vector:'''  

Revision as of 13:41, 13 September 2010

  • 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
Essential no
Product phosphotransferase system (PTS) enzyme I
Function PTS-dependent sugar transport
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 62,9 kDa, 4.59
Gene length, protein length 1710 bp, 570 amino acids
Immediate neighbours ptsH, splA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PtsI context.gif
This image was kindly provided by SubtiList

The gene

Basic information

  • Locus tag: BSU13910

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 (according to Swiss-Prot) PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to HPr (His-15)
  • Protein family: PEP-utilizing enzyme family (according to Swiss-Prot) 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-34 or Ser-36 PubMed
  • Cofactor(s): Magnesium
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 2WQD (Enzyme I from Staphylococcus aureus) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expression activated by glucose (2 fold) (GlcT) PubMed
    • the ptsH promoter is constitutive PubMed
    • subject to negative stringent control upon amino acid limitation (due to control of ptsG transcription initiation) PubMed
  • Additional information:

Biological materials

  • Mutant: GP864 (ermC), GP778 (replacement of glcT and the ptsGHI operon by a spc cassette), available in Stülke lab
  • Expression vector:
    • pAG3 (His-tag), available in Galinier lab
    • for expression, purification in E. coli, in pWH844: pGP813 available in Stülke lab
  • 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


Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J. Bacteriol.: 2010, 192(6);1573-85
[PubMed:20081037] [WorldCat.org] [DOI] (I p)

Anselm E Oberholzer, Philipp Schneider, Christian Siebold, Ulrich Baumann, Bernhard Erni
Crystal structure of enzyme I of the phosphoenolpyruvate sugar phosphotransferase system in the dephosphorylated state.
J. Biol. Chem.: 2009, 284(48);33169-76
[PubMed:19801641] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol. Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab. Eng.: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] (P p)

L F Garrity, S L Schiel, R Merrill, J Reizer, M H Saier, G W Ordal
Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC.
J. Bacteriol.: 1998, 180(17);4475-80
[PubMed:9721285] [WorldCat.org] (P p)