CstA

• Description: putative peptide transporter, carbon starvation-induced protein
  
  

Gene name	cstA
Synonyms
Essential	no
Product	putative peptide transporter, carbon starvation-induced protein
Function	uptake of peptides
Gene expression levels in SubtiExpress: cstA
MW, pI	64 kDa, 8.658
Gene length, protein length	1794 bp, 598 aa
Immediate neighbours	ysfE, abfA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed 500px

Categories containing this gene/protein

transporters/ other, Utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU28710

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

Additional information

the E.coli homolog: cstA

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: cstA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • membrane (according to UniProt)

Database entries

• Structure:

• UniProt: P94532

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:
  • cstA-ysfE PubMed

• Expression browser: cstA PubMed

• Sigma factor:

• Regulation: repressed by glucose (3.4-fold) (CcpA) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [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)

Simon Rasmussen, Henrik Bjørn Nielsen, Hanne Jarmer
The transcriptionally active regions in the genome of Bacillus subtilis.
Mol Microbiol: 2009, 73(6);1043-57
[PubMed:19682248] [WorldCat.org] [DOI] (I p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

The E. coli homolog

J E Schultz, A Matin
Molecular and functional characterization of a carbon starvation gene of Escherichia coli.
J Mol Biol: 1991, 218(1);129-40
[PubMed:1848300] [WorldCat.org] [DOI] (P p)