LicT

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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:
Sugar catabolism
MW, pI 32 kDa, 5.944
Gene length, protein length 831 bp, 277 aa
Immediate neighbours bglS, yxiP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LicT context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LicT expression.png




























Categories containing this gene/protein

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

This gene is a member of the following regulons

The LicT regulon: bglP-bglH-yxiE, bglS

The gene

Basic information

  • Locus tag: BSU39080

Phenotypes of a mutant

no expression of the bglP-bglH operon

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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)

Extended information on the protein

  • Kinetic information:
  • 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:

Database entries

  • Structure: 1L1C (complex with RAT), 1TLV (PRDs)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Your additional remarks

References

Additional publications: PubMed

Original description


Control of LicT activity


Structural analysis of LicT


LicT-RNA interaction

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)