Difference between revisions of "BglS"

From SubtiWiki
Jump to: navigation, search
Line 122: Line 122:
 
=References=
 
=References=
  
 +
<pubmed>18957862 12850135 6087283 8245830 8245831 8606172, </pubmed>
 
# Voigt et al. (2009) Cell physiology and protein secretion of ''Bacillus licheniformis'' compared to ''Bacillus subtilis''. ''J Mol Microbiol Biotechnol.'' '''16:''' 53-68 [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 
# Voigt et al. (2009) Cell physiology and protein secretion of ''Bacillus licheniformis'' compared to ''Bacillus subtilis''. ''J Mol Microbiol Biotechnol.'' '''16:''' 53-68 [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 
# Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in ''Bacillus subtilis'': regulation of the central metabolic pathways. ''Metab Eng.'' '''5:''' 133-149 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
 
# Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in ''Bacillus subtilis'': regulation of the central metabolic pathways. ''Metab Eng.'' '''5:''' 133-149 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]

Revision as of 20:52, 8 June 2009

  • Description: endo-beta-1,3-1,4 glucanase

Gene name bglS
Synonyms bgl, licS
Essential no
Product endo-beta-1,3-1,4 glucanase
Function lichenan degradation
MW, pI 27 kDa, 6.482
Gene length, protein length 726 bp, 242 aa
Immediate neighbours citH, licT
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
BglS context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU39070

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds (according to Swiss-Prot)
  • Protein family: glycosyl hydrolase 16 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: extracellular (signal peptide) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: repressed by glucose (3.1-fold) (CcpA) PubMed1 PubMed2, expressed in the stationary phase (temporal activation), weak induction by ß-glucosides (LicT) PubMed
  • Regulatory mechanism:
    • CcpA: transcription repression PubMed
    • LicT: binding to an RNA switch results in transcriptional antitermination PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

  1. Voigt et al. (2009) Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis. J Mol Microbiol Biotechnol. 16: 53-68 PubMed
  2. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
  1. Murphy ND, McConnell DJ, Cantwell BA. 1984. The DNA sequence of the gene and genetic control sites for the excreted Bacillus subtilis enzyme β-glucanase. Nucl. Acids Res. 12:5355-5367. PubMed
  2. Stülke, J., Hanschke, R. & Hecker, M. (1993) Temporal activation of ß-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool. J. Gen. Microbiol. 139: 2041-2045. PubMed
  3. Krüger, S., Stülke, J. & Hecker, M. (1993) Carbon catabolite repression of ß-glucanase synthesis in Bacillus subtilis. J. Gen. Microbiol. 139: 2047-2054. PubMed
  4. Schnetz, K., Stülke, J., Gertz, S., Krüger, S., Krieg, M., Hecker, M. & Rak, B. (1996) LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family. J. Bacteriol. 178: 1971-1979. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed