PtsG

• Description: A major carbohydrate active-transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.
  
  

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 File:GenE context.gif

The gene

Basic information

• Coordinates:

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transport and phosphorylation of glucose

• Protein family: 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:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• 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]

Expression and regulation

• Operon:
  • ptsG-ptsH-ptsI
  • ptsH-ptsI

• Sigma factor: SigA

• Regulation: induction by glucose

• Regulatory mechanism: transcriptional antitermination via the GlcT-dependent RNA-switch PubMed
• Additional information:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

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