LicT

• Description: transcriptional antiterminator of the bglP-bglH-yxiE operon and the bglS gene
  
  

Gene name	licT
Synonyms
Essential	no
Product	transcriptional antiterminator (BglG family)
Function	control of beta-glucan and beta-glucoside utilization
Gene expression levels in SubtiExpress: licT
Interactions involving this protein in SubtInteract: LicT
Metabolic function and regulation of this protein in SubtiPathways: licT
MW, pI	32 kDa, 5.944
Gene length, protein length	831 bp, 277 aa
Immediate neighbours	bglS, yxiP
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of specific carbon sources, transcription factors and their control, RNA binding regulators, phosphoproteins

The gene

Basic information

• Locus tag: BSU39080

Phenotypes of a mutant

no expression of the bglP-bglH operon

Database entries

• BsubCyc: BSU39080

• 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: transcriptional antiterminator BglG family of antiterminators (according to Swiss-Prot)

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

Extended information on the protein

• Kinetic information:
  • K(D) for the RAT-RNA: 10 nM PubMed
• Domains:
  • N-terminal RNA binding domain Pubmed
  • 2xPRD (PTS regulation domains) PubMed

• Modification:
  • phosphorylation at His-100 in PRD-1 by phosphorylated BglP, inhibits LicT antitermination activity
  • phosphorylation at His-207 and/or His-269 in PRD-2 by His-P-HPr, stimulates LicT antitermination activity

• Cofactor(s):

• Effectors of protein activity:

• Interactions: PtsH-LicT, BglP-LicT

• Localization:
  • cytoplasm, even distribution in the absence of the inducer salicin, subpolar localization in the presence of salicin PubMed

Database entries

• BsubCyc: BSU39080

• Structure: 1L1C (complex with RAT), 1TLV (PRDs)

• UniProt: P39805

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: licT-bglS PubMed

• Expression browser: licT PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP427 (licTS, erm), available in the Stülke lab

• Expression vector:

• • for expression, purification of both PRDs in E. coli with N-terminal His-tag, in pWH844: pGP165, available in Stülke lab
  • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag, in pWH844: pGP315, available in Stülke lab
  • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP572, available in Stülke lab

• lacZ fusion:

• GFP fusion: GP1225 (spc, based on pGP1870), available in the Stülke lab

• YFP fusion: GP1229 (spc, based on pGP1871), available in the Stülke lab

• FLAG-tag construct: GP1221 (spc, based on pGP1331), available in the Stülke lab

• 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

Control of LicT activity

Fabian M Rothe, Christoph Wrede, Martin Lehnik-Habrink, Boris Görke, Jörg Stülke
Dynamic localization of a transcription factor in Bacillus subtilis: the LicT antiterminator relocalizes in response to inducer availability.
J Bacteriol: 2013, 195(10);2146-54
[PubMed:23475962] [WorldCat.org] [DOI] (I p)

Thomas Bahr, Denise Lüttmann, Walter März, Bodo Rak, Boris Görke
Insight into bacterial phosphotransferase system-mediated signaling by interspecies transplantation of a transcriptional regulator.
J Bacteriol: 2011, 193(8);2013-26
[PubMed:21335451] [WorldCat.org] [DOI] (I p)

Cordula Lindner, Michael Hecker, Dominique Le Coq, Josef Deutscher
Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon.
J Bacteriol: 2002, 184(17);4819-28
[PubMed:12169607] [WorldCat.org] [DOI] (P p)

P Tortosa, N Declerck, H Dutartre, C Lindner, J Deutscher, D Le Coq
Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY.
Mol Microbiol: 2001, 41(6);1381-93
[PubMed:11580842] [WorldCat.org] [DOI] (P p)

C Lindner, A Galinier, M Hecker, J Deutscher
Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation.
Mol Microbiol: 1999, 31(3);995-1006
[PubMed:10048041] [WorldCat.org] [DOI] (P p)

S Krüger, S Gertz, M Hecker
Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression.
J Bacteriol: 1996, 178(9);2637-44
[PubMed:8626332] [WorldCat.org] [DOI] (P p)

Structural analysis of LicT

Hélène Déméné, Thierry Ducat, Karine De Guillen, Catherine Birck, Stéphane Aymerich, Michel Kochoyan, Nathalie Declerck
Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.
J Biol Chem: 2008, 283(45);30838-49
[PubMed:18682383] [WorldCat.org] [DOI] (P p)

Marc Graille, Cong-Zhao Zhou, Véronique Receveur-Bréchot, Bruno Collinet, Nathalie Declerck, Herman van Tilbeurgh
Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.
J Biol Chem: 2005, 280(15);14780-9
[PubMed:15699035] [WorldCat.org] [DOI] (P p)

N Declerck, H Dutartre, V Receveur, V Dubois, C Royer, S Aymerich, H van Tilbeurgh
Dimer stabilization upon activation of the transcriptional antiterminator LicT.
J Mol Biol: 2001, 314(4);671-81
[PubMed:11733988] [WorldCat.org] [DOI] (P p)

H van Tilbeurgh, D Le Coq, N Declerck
Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.
EMBO J: 2001, 20(14);3789-99
[PubMed:11447120] [WorldCat.org] [DOI] (P p)

LicT-RNA interaction

Caroline Clerte, Nathalie Declerck, Emmanuel Margeat
Competitive folding of anti-terminator/terminator hairpins monitored by single molecule FRET.
Nucleic Acids Res: 2013, 41(4);2632-43
[PubMed:23303779] [WorldCat.org] [DOI] (I p)

Sebastian Hübner, Nathalie Declerck, Christine Diethmaier, Dominique Le Coq, Stephane Aymerich, Jörg Stülke
Prevention of cross-talk in conserved regulatory systems: identification of specificity determinants in RNA-binding anti-termination proteins of the BglG family.
Nucleic Acids Res: 2011, 39(10);4360-72
[PubMed:21278164] [WorldCat.org] [DOI] (I p)

Hélène Déméné, Thierry Ducat, Karine De Guillen, Catherine Birck, Stéphane Aymerich, Michel Kochoyan, Nathalie Declerck
Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.
J Biol Chem: 2008, 283(45);30838-49
[PubMed:18682383] [WorldCat.org] [DOI] (P p)

Yinshan Yang, Nathalie Declerck, Xavier Manival, Stéphane Aymerich, Michel Kochoyan
Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT.
EMBO J: 2002, 21(8);1987-97
[PubMed:11953318] [WorldCat.org] [DOI] (P p)

N Declerck, F Vincent, F Hoh, S Aymerich, H van Tilbeurgh
RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.
J Mol Biol: 1999, 294(2);389-402
[PubMed:10610766] [WorldCat.org] [DOI] (P p)

S Aymerich, M Steinmetz
Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family.
Proc Natl Acad Sci U S A: 1992, 89(21);10410-4
[PubMed:1279678] [WorldCat.org] [DOI] (P p)