Difference between revisions of "PtsI"

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* '''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 ([[PtsH |HPr]])  <br/><br/>
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* '''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 ([[PtsH |HPr]])  <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || phosphotransferase system (PTS) enzyme I  
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|style="background:#ABCDEF;" align="center"| '''Product''' || phosphotransferase system ([[PTS]]) enzyme I  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || PTS-dependent sugar transport
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|style="background:#ABCDEF;" align="center"|'''Function''' || [[PTS]]-dependent sugar transport
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
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**pyrophosphate/phosphate carrier histidine (central Domain)
 
**pyrophosphate/phosphate carrier histidine (central Domain)
  
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* '''Modification:''' transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-34 or Ser-36 [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
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* '''Modification:'''  
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** transient autophosphorylation on His-189
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** ''in vivo'' also phosphorylated on Ser-34 or Ser-36 [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
  
 
* '''Cofactor(s):''' Magnesium
 
* '''Cofactor(s):''' Magnesium
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* '''Interactions:'''
 
* '''Interactions:'''
  
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* '''Localization:''' cytoplasm (according to Swiss-Prot),  Cytoplasm
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* '''Localization:''' cytoplasm (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
 
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
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* '''Regulation:''' expression activated by glucose (4.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose (''[[ptsG]]''), constitutive (''[[ptsH]]'')
 
  
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* '''Regulatory mechanism:''' ''[[ptsG]]'': transcriptional antitermination via the [[GlcT]]-dependent RNA-switch
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* '''Regulation:'''
 +
** expression activated by glucose (4.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose (''[[ptsG]]''), constitutive (''[[ptsH]]'')
 +
 
 +
* '''Regulatory mechanism:'''  
 +
** ''[[ptsG]]'': transcriptional antitermination via the [[GlcT]]-dependent RNA-switch
  
 
* '''Additional information:'''
 
* '''Additional information:'''

Revision as of 19:45, 20 September 2009

  • 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
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: 2HWG (Enzyme I from E. coli)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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
    • 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

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)

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