Difference between revisions of "PtsI"

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=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' available in [[Stülke]] lab
+
* '''Mutant:''' available in [[Jörg Stülke]]'s lab:
 
** GP864 (ermC)
 
** GP864 (ermC)
** GP778 (replacement of ''[[glcT]]'' and the ''[[ptsG]]-[[ptsH]]-[[ptsI]]'' operon by a spc cassette)
+
** GP778 (replacement of ''[[glcT]]'' and the ''[[ptsG]]-[[ptsH]]-[[ptsI]]'' operon by a spc cassette), {{PubMed|22722928}}
  
 
* '''Expression vector:'''  
 
* '''Expression vector:'''  
** pAG3 (His-tag), available in [[Galinier]] lab
+
** pAG3 (His-tag) {{PubMed|9237995}}, available in [[Galinier]] lab
** for expression, purification in ''E. coli'' (His-tag), in [[pWH844]]: pGP813 available in [[Stülke]] lab
+
** for expression, purification in ''E. coli'' (His-tag), in [[pWH844]]: pGP813 available in [[Jörg Stülke]]'s lab
  
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''

Revision as of 08:31, 3 September 2013

  • 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:
Central C-metabolism
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
PtsI context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PtsI expression.png















Categories containing this gene/protein

phosphotransferase systems, phosphoproteins

This gene is a member of the following regulons

GlcT regulon, stringent response

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:

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

  • Expression vector:
  • 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

Your additional remarks

References

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)

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)