PtsI

• 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
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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU13910

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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), Cytoplasm

Database entries

• Structure:

• Swiss prot entry: P08838

• KEGG entry: [3]

• E.C. number: 2.7.3.9 2.7.3.9]

Expression and regulation

• Operon:
  • ptsG-ptsH-ptsI
  • ptsH-ptsI

• Sigma factor: SigA PubMed
• Regulation: expression activated by glucose (4.3 fold) PubMed, induction by glucose (ptsG), constitutive (ptsH)

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

• Additional information:

Biological materials

• Mutant: GP864 (ermC), available in Stülke lab

• Expression vector: pAG3 (His-tag), available in Galinier lab

• lacZ fusion:

• GFP fusion:

• Antibody:

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

References

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] [DOI] (P p)

1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
2. 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
3. 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