Difference between revisions of "PtsI"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ptsH]]'', ''[[splA]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ptsH]]'', ''[[splA]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13910 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13910 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13910 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13910 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13910 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13910 DNA_with_flanks]
 
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Revision as of 10:04, 14 May 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

  • Mutant: available in Stülke lab
    • GP864 (ermC)
    • GP778 (replacement of glcT and the ptsG-ptsH-ptsI operon by a spc cassette)
  • Expression vector:
    • pAG3 (His-tag), available in Galinier lab
    • for expression, purification in E. coli (His-tag), in pWH844: pGP813 available in Stülke 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

Your additional remarks

References