SacT

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Gene name sacT
Synonyms ipa-47d
Essential no
Product transcriptional antiterminator
Function regulation of sucrose utilization
Gene expression levels in SubtiExpress: sacT
Interactions involving this protein in SubtInteract: SacT
Metabolic function and regulation of this protein in SubtiPathways:
sacT
MW, pI 31 kDa, 5.587
Gene length, protein length 828 bp, 276 aa
Immediate neighbours ywcJ, ywcI
Sequences Protein DNA DNA_with_flanks
Genetic context
SacT context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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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

DnaAregulon

The SacT regulon: sacP-sacA-ywdA

The gene

Basic information

  • Locus tag: BSU38070

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: binding to the mRNA of the sacP-sacA operon, causes transcription antitermination (in presence of sucrose and absence of glucose)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Expression vector:
    • for expression, purification of both PRDs in E. coli with N-terminal His-tag, in pWH844: pGP166, available in Jörg Stülke's lab
    • for expression, purification of PRD-1 in E. coli with N-terminal His-tag, in pWH844: pGP426, available in Jörg Stülke's lab
    • for expression, purification of PRD-2 in E. coli with N-terminal His-tag, in pWH844: pGP427, available in Jörg Stülke's lab
    • for expression, purification of PRD-1 in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP439, available in Jörg Stülke's lab
    • for expression, purification of PRD-2 in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP440, available in Jörg Stülke's lab
    • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP571, available in Jörg Stülke's lab
    • for expression of the RNA-binding domain in B. subtilis, in pBQ200: pGP446, available in Jörg Stülke's lab
    • for expression, purification of sacT-full length in B. subtilis with C-terminal Strep-tag, in pGP382: pGP1064, available in Jörg Stülke's lab
    • for expression, purification of sacT-full length in B. subtilis with N-terminal Strep-tag, in pGP380: pGP1068, available in Jörg Stülke's lab
  • lacZ fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Janet L Smith, Alan D Grossman
In Vitro Whole Genome DNA Binding Analysis of the Bacterial Replication Initiator and Transcription Factor DnaA.
PLoS Genet: 2015, 11(5);e1005258
[PubMed:26020636] [WorldCat.org] [DOI] (I e)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [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)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

M Arnaud, M Débarbouillé, G Rapoport, M H Saier, J Reizer
In vitro reconstitution of transcriptional antitermination by the SacT and SacY proteins of Bacillus subtilis.
J Biol Chem: 1996, 271(31);18966-72
[PubMed:8702561] [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)

M Arnaud, P Vary, M Zagorec, A Klier, M Debarbouille, P Postma, G Rapoport
Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity.
J Bacteriol: 1992, 174(10);3161-70
[PubMed:1577686] [WorldCat.org] [DOI] (P p)

M Debarbouille, M Arnaud, A Fouet, A Klier, G Rapoport
The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators.
J Bacteriol: 1990, 172(7);3966-73
[PubMed:2163394] [WorldCat.org] [DOI] (P p)