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
MW, pI	62,9 kDa, 4.59
Gene length, protein length	1710 bp, 570 amino acids
Immediate neighbours	ptsH, splA
Gene sequence (+200bp)	Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 1458959 - 1460668

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to HPr (His-15)

• 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: 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

Database entries

• Structure:

• Swiss prot entry: [3]

• KEGG entry: [4]

• E.C. number: [5]

Expression and regulation

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

• Sigma factor: SigA PubMed
• Regulation: 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

1. 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
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