LicT

• Description: transcriptional antiterminator of the bglPH operon
  
  

Gene name	licT
Synonyms
Essential	no
Product	transcriptional antiterminator (BglG family)
Function	required for substrate-dependent induction of bglPH
MW, pI	32 kDa, 5.944
Gene length, protein length	831 bp, 277 aa
Immediate neighbours	bglS, yxiP
Gene sequence (+200bp)	Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context

The gene

Basic information

• Coordinates:

Phenotypes of a mutant

no expression of the bglP-bglH operon

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: binding to the mRNAs of bglS and the bglP-bglH operon, causes transcription antitermination (in presence of salicin and absence of glucose)

• Protein family: BglG family of antiterminators

• Paralogous protein(s): SacY, GlcT, SacT

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: licT-bglS PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

Josef Deutscher, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

Michael Hecker, Greifswald, Germany Homepage

References

Original description

1. Schnetz, K., Stülke, J., Gertz, S., Krüger, S., Krieg, M., Hecker, M. & Rak, B. (1996) LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family. J. Bacteriol. 178: 1971-1979. PubMed

Control of LicT activity

1. Lindner, C., Galinier, A., Hecker, M. & Deutscher, J. (1999) Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31, 995-1006 . PubMed
2. Lindner, C., Hecker, M., Le Coq, D. & Deutscher, J. (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184, 4819-4828 . PubMed
3. Krüger, S., Gertz, S. & Hecker, M. Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression. J. Bacteriol. 178, 2637-2644 (1996). PubMed
4. Tortosa, P., Declerck, N., Dutartre, H., Lindner, C., Deutscher, J., and Le Coq, D. (2001) Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY. Mol Microbiol 41: 1381-1393. PubMed

Structural analysis of LicT

1. Declerck N, Dutartre H, Receveur V, Dubois V, Royer C, Aymerich S, van Tilbeurgh H (2001) Dimer stabilization upon activation of the transcriptional antiterminator LicT. J Mol Biol 314:671-681. PubMed
2. Graille, M. et al. Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J. Biol. Chem. 280, 14780-14789 (2005). PubMed
3. van Tilbeurgh H, Le Coq D, Declerck N (2001) Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator. EMBO J 20:3789-3799. PubMed
4. Déméné H, Ducat T, De Guillen K, Birck C, Aymerich S, Kochoyan M, Declerck N.(2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.J. Biol. Chem. 283: 30838-30849. PubMed

LicT-RNA interaction

1. Yang Y, Declerck N, Manival X, Aymerich S, Kochoyan M (2002) Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT. EMBO J 21:1987-1997. PubMed
2. Aymerich, S. and Steinmetz, M. (1992) Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family. Proc. Natl. Acad. Sci. USA 89, 10410-10414. PubMed
3. Declerck, N., Vincent, F., Hoh, F., Aymerich, S. and van Tilbeurgh, H. (1999) RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domains from SacY and LicT. J. Mol. Biol. 294, 389-402. PubMed
4. Déméné H, Ducat T, De Guillen K, Birck C, Aymerich S, Kochoyan M, Declerck N.(2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.J. Biol. Chem. 283: 30838-30849. PubMed
5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed