AraE

• Description: L-arabinose permease
  
  

Gene name	araE
Synonyms	yvbR
Essential	no
Product	L-arabinose permease
Function	uptake of arabinose, galactose and xylose
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	50 kDa, 9.259
Gene length, protein length	1392 bp, 464 aa
Immediate neighbours	cggR, araR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU33960

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P96710

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: araE PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by arabinose (AraR) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression
  • AraR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

L J Mota, P Tavares, I Sá-Nogueira
Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis.
Mol Microbiol: 1999, 33(3);476-89
[PubMed:10417639] [WorldCat.org] [DOI] (P p)

O Krispin, R Allmansberger
The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars.
J Bacteriol: 1998, 180(12);3250-2
[PubMed:9620981] [WorldCat.org] [DOI] (P p)

I Sá-Nogueira, S S Ramos
Cloning, functional analysis, and transcriptional regulation of the Bacillus subtilis araE gene involved in L-arabinose utilization.
J Bacteriol: 1997, 179(24);7705-11
[PubMed:9401028] [WorldCat.org] [DOI] (P p)