PtsG

• 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

The gene

Basic information

• Coordinates: 1456496 - 1458592

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions: PtsG-HPr, PtsG-GlcT (for phosphorylation of GlcT) PubMed

• 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 PubMed

• 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