Difference between revisions of "PtsG"

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|style="background:#ABCDEF;" align="center"|'''Function''' || glucose transport and phosphorylation, control of [[GlcT]] activity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || glucose transport and phosphorylation, control of [[GlcT]] activity
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|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/carbohydrate_metabolic_pathways.html Sugar catabolism]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 75,3 kDa, 5.40
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 75,3 kDa, 5.40

Revision as of 11:41, 11 June 2009

  • Description: trigger enzyme: major glucose permease of the PTS, EIICBA(Glc) and control of GlcT activity

Gene name ptsG
Synonyms ptsX, crr
Essential no
Product glucose-specific enzyme IICBA component
Function glucose transport and phosphorylation, control of GlcT activity
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 75,3 kDa, 5.40
Gene length, protein length 2097 bp, 699 amino acids
Immediate neighbours glcT, ptsH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PtsG context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU13890

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transport and phosphorylation of glucose, receives a phosphate from HPr at the IIA domain (His-620), the phosphate group is then transferred to the IIB domain (Cys-461) an finally to the incoming glucose. In the absence of glucose, PtsG phosphorylates and thereby inactivates the transcriptional antiterminator GlcT.
  • Protein family: PTS permease, glucose permease (Glc) family PubMed, PTS enzyme II, glucose family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • 11x transmembrane domain (16–36, 89–109, 139–159, 180–200, 233–253, 283–303, 313–333, 338–358, 365–385, 388–408)
    • PTS EIIC domain ( 1-424)
    • PTS EIIB domain (439–520)
    • PTS EIIA domain (568–672)
  • Modification: transient phosphorylation (HPr-dependent) on His-620, then internal phosphotransfer from His-620 to Cys-461
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: membrane protein PubMed

Database entries

  • Structure: 1AX3 (IIA domain), 1GPR (IIA domain), IIA domain NCBI, NMR IIA domain NCBI
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: expression activated by glucose (32 fold) PubMed
  • Regulatory mechanism: transcriptional antitermination via the GlcT-dependent RNA-switch PubMed
  • Additional information:

Biological materials

  • Mutant: GP474 (cat), QB5436 (spc), QB5445 (erm), available in Stülke lab
  • Expression vector: pGP123 (domains BA, in pWH844), pGP123 (domains BA, mut: H620D, in pWH844), pGP428 (EIIB, in pWH844), pGP437(EIIA in pWH844, with thrombin cleavage site), available in Stülke lab
  • lacZ fusion: pGP34 (pAC5), pGP66 (pAC7), pGP606 (mutant terminator, pAC6), pGP532 (pAC7), series of promoter deletions are available in pAC5 and pAC6, series of RAT mutants are available in pAC6, available in Stülke lab
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References


  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed