Difference between revisions of "LicT"

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(Basic information/ Evolution)
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* '''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)
 
* '''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:''' [[PRD-containing transcription factors|transcriptional antiterminator]] bglG family (according to Swiss-Prot) BglG family of antiterminators
+
* '''Protein family:''' [[PRD-containing transcription factors|transcriptional antiterminator]] BglG family of antiterminators (according to Swiss-Prot)  
  
 
* '''Paralogous protein(s):''' [[SacY]], [[GlcT]], [[SacT]]
 
* '''Paralogous protein(s):''' [[SacY]], [[GlcT]], [[SacT]]

Revision as of 19:56, 20 September 2009

Gene name licT
Synonyms
Essential no
Product transcriptional antiterminator (BglG family)
Function substrate-dependent induction of bglP-bglH
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







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:
  • Localization:

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:
  • 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:
  • 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

Original description


Control of LicT activity


Structural analysis of LicT


LicT-RNA interaction