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
Gene expression levels in SubtiExpress: ptsI
Interactions involving this protein in SubtInteract: PtsI
Metabolic function and regulation of this protein in SubtiPathways: ptsI
MW, pI	62,9 kDa, 4.59
Gene length, protein length	1710 bp, 570 amino acids
Immediate neighbours	ptsH, splA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

phosphotransferase systems, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

GlcT regulon, stringent response

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

• Cofactors: Magnesium

• Effectors of protein activity:

• Interactions:
  • PtsI-PtsH

• Localization:
  • cytoplasm, even distribution PubMed

Database entries

• Structure: 2WQD (Enzyme I from Staphylococcus aureus) PubMed

• UniProt: P08838

• KEGG entry: [3]

• E.C. number: 2.7.3.9 2.7.3.9]

Expression and regulation

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

• Expression browser: ptsI PubMed

• Sigma factor:
  • ptsG: SigA PubMed
  • ptsH: SigA PubMed

• 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

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

• Additional information:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant: available in Jörg Stülke's lab:
  • GP864 (ermC)
  • GP778 (replacement of glcT and the ptsG-ptsH-ptsI operon by a spc cassette), PubMed

• Expression vector:
  • pAG3 (His-tag) PubMed, available in Galinier lab
  • for expression, purification in E. coli (His-tag), in pWH844: pGP813 available in Jörg Stülke's lab

• lacZ fusion:

• GFP fusion:

• YFP fusion: B. subtilis GP1276 ptsI-yfp ermC, available in Jörg Stülke's lab

• Antibody:

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

References

Sutharsan Govindarajan, Yair Elisha, Keren Nevo-Dinur, Orna Amster-Choder
The general phosphotransferase system proteins localize to sites of strong negative curvature in bacterial cells.
mBio: 2013, 4(5);e00443-13
[PubMed:24129255] [WorldCat.org] [DOI] (I e)

Fabian M Rothe, Christoph Wrede, Martin Lehnik-Habrink, Boris Görke, Jörg Stülke
Dynamic localization of a transcription factor in Bacillus subtilis: the LicT antiterminator relocalizes in response to inducer availability.
J Bacteriol: 2013, 195(10);2146-54
[PubMed:23475962] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)

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] [DOI] (P p)