Difference between revisions of "AraE"

From SubtiWiki
Jump to: navigation, search
(Expression and regulation)
Line 93: Line 93:
 
* '''Sigma factor:'''  
 
* '''Sigma factor:'''  
  
* '''Regulation:''' repressed by glucose [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induced by arabinose [http://www.ncbi.nlm.nih.gov/sites/entrez/9620981 PubMed]
+
* '''Regulation:''' repressed by glucose,  induced by arabinose [http://www.ncbi.nlm.nih.gov/sites/entrez/9620981 PubMed]
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
Line 119: Line 119:
 
=References=
 
=References=
  
# 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]
 
 
# Krispin, O., and R. Allmansberger. (1998) The ''Bacillus subtilis'' AraE protein displays a broad substrate specificity for several different sugars. ''J. Bacteriol.'' '''180:''' 3250-3252. [http://www.ncbi.nlm.nih.gov/sites/entrez/9620981 PubMed]
 
# Krispin, O., and R. Allmansberger. (1998) The ''Bacillus subtilis'' AraE protein displays a broad substrate specificity for several different sugars. ''J. Bacteriol.'' '''180:''' 3250-3252. [http://www.ncbi.nlm.nih.gov/sites/entrez/9620981 PubMed]
 
# Sá-Nogueira I, Ramos SS. (1997) Cloning, functional analysis, and transcriptional regulation of the Bacillus subtilis araE gene involved in L-arabinose utilization. ''J Bacteriol. '' '''Dec;179(24):''' 7705-11. [http://www.ncbi.nlm.nih.gov/sites/entrez/9401028 PubMed]
 
# Sá-Nogueira I, Ramos SS. (1997) Cloning, functional analysis, and transcriptional regulation of the Bacillus subtilis araE gene involved in L-arabinose utilization. ''J Bacteriol. '' '''Dec;179(24):''' 7705-11. [http://www.ncbi.nlm.nih.gov/sites/entrez/9401028 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 00:22, 3 April 2009

  • Description: L-arabinose permease

Gene name araE
Synonyms yvbR
Essential no
Product L-arabinose permease
Function uptake of arabinose, galactose and xylose
MW, pI 50 kDa, 9.259
Gene length, protein length 1392 bp, 464 aa
Immediate neighbours cggR, araR
Gene sequence (+200bp) Protein sequence
Genetic context
AraE context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transports arabinose, and also xylose and galactose PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation: repressed by glucose, induced by arabinose PubMed
  • Regulatory mechanism:
  • 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. Krispin, O., and R. Allmansberger. (1998) The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars. J. Bacteriol. 180: 3250-3252. PubMed
  2. Sá-Nogueira I, Ramos SS. (1997) Cloning, functional analysis, and transcriptional regulation of the Bacillus subtilis araE gene involved in L-arabinose utilization. J Bacteriol. Dec;179(24): 7705-11. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed