Difference between revisions of "PtsG"

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(Biological materials)
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=Biological materials =
 
=Biological materials =
  
* '''Mutant:'''
+
* '''Mutant:''' GP474 (cat), QB5436 (spc), QB5445 (erm), available in [[Stülke]] lab
  
* '''Expression vector:'''
+
 
 +
* '''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:'''
+
* '''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:'''
 
* '''GFP fusion:'''

Revision as of 19:35, 14 January 2009

  • Description: Major glucose permease of the PTS, EIICBA(Glc)

Gene name ptsG
Synonyms ptsX, crr
Essential no
Product glucose-specific enzyme IICBA component
Function glucose transport and phosphorylation
MW, pI 75,3 kDa, 5.40
Gene length, protein length 2097 bp, 699 amino acids
Immediate neighbours glcT, ptsH
Gene sequence (+200bp) Protein sequence
Genetic context
PtsG context.gif



The gene

Basic information

  • Coordinates: 1456496 - 1458592

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 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 NCBI

Database entries

  • Structure: IIA domain NCBI, NMR IIA domain NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Regulation: induction by glucose
  • 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. Stülke J, Martin-Verstraete I, Zagorec M (1997) Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT Mol Microbiol. 25: 65-78. PubMed
  2. Bachem S, Stülke J. (1998) Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system. J Bacteriol. 180: 5319-26 PubMed
  3. Bachem, S., Faires, N., & Stülke, J. (1997) Characterization of the presumptive phosphorylation sites of the Bacillus subtilis glucose permease by site-directed mutagenesis: Implication in glucose transport and catabolite repression. FEMS Microbiol. L. 156: 233-238. PubMed
  4. Gonzy-Tréboul, G., de Waard, J. H., Zagorec, M., and Postma, P.W. (1991). The glucose permease of the phosphotransferase system of Bacillus subtilis: Evidence for IIGlc and IIIGlc domains. Mol. Microbiol. 5, 1241-1249. PubMed
  5. Langbein, I., Bachem, S. & Stülke, J. (1999) Specific interaction of the RNA binding domain of the Bacillus subtilis transcriptional antiterminator GlcT with its RNA target, RAT. J. Mol. Biol. 293: 795-805. PubMed
  6. Schilling, O., Herzberg, C., Hertrich, T., Vörsmann, H., Jessen, D., Hübner, S., Titgemeyer, F. & Stülke, J. (2006) Keeping signals straight in transcription regulation: specificity determinants for the interaction of a family of conserved bacterial RNA-protein couples. Nucl. Acids Res. 34: 6102-6115. PubMed
  7. Schilling, O., Langbein, I., Müller, M., Schmalisch, M. & Stülke, J. (2004) A protein-dependent riboswitch controlling ptsGHI operon expression in Bacillus subtilis: RNA structure rather than sequence provides interaction specificity. Nucl. Acids Res. 32: 2853-2864. PubMed
  8. Schmalisch, M., Bachem, S. & Stülke, J. (2003) Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation: Elucidation of the phosphorylation chain leading to inactivation of GlcT. J. Biol. Chem. 278: 51108-51115. PubMed