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

K Schnetz, J Stülke, S Gertz, S Krüger, M Krieg, M Hecker, B Rak
LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family.
J Bacteriol: 1996, 178(7);1971-9
[PubMed:8606172] [WorldCat.org] [DOI] (P p)

Control of LicT activity

Structural analysis of LicT

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)