PtsG

• Description: trigger enzyme: 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, control of GlcT activity
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 This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 1456496 - 1458592

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine (according to Swiss-Prot) 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:

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

• Localization: membrane protein PubMed

Database entries

• Structure: 1AX3 (IIA domain), 1GPR (IIA domain), IIA domain NCBI, NMR IIA domain NCBI

• Swiss prot entry: P20166

• KEGG entry: BSU13890

• E.C. number: 2.7.1.69 9 2.7.1.69]

Expression and regulation

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

• Sigma factor: SigA PubMed

• 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

References

1. Reizer et al. (1999) Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis. Microbiology 145: 3419-3429 PubMed
2. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
3. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
4. 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
5. 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
6. 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
7. 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
8. 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
9. 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
10. 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
11. 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
12. Zagorec, M. & Postma, P. (1992). Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis. Mol Gen Genet 234, 325-328. PubMed
13. Sutrina, S. L., Reddy, P., Saier, M. H., Jr & Reizer, J. (1990). The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease. J Biol Chem 265, 18581-18589. PubMed
14. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed