FrlB

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  • Description: fructoselysine-6-P-glycosidase

Gene name frlB
Synonyms yurP
Essential no
Product fructoselysine-6-P-glycosidase
Function metabolism of aminoacylated fructose
Gene expression levels in SubtiExpress: frlB
Metabolic function and regulation of this protein in SubtiPathways:
Alternative nitrogen sources
MW, pI 36 kDa, 5.442
Gene length, protein length 984 bp, 328 aa
Immediate neighbours frlO, yurQ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YurP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FrlB expression.png















Categories containing this gene/protein

utilization of specific carbon sources, utilization of nitrogen sources other than amino acids, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CodY regulon, FrlR regulon

The gene

Basic information

  • Locus tag: BSU32610

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-48 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation


  • Sigma factor:
  • Regulation:
    • frlB: repressed during growth in the presence of branched chain amino acids (CodY) PubMed
    • frlB: induced in the presence of fructosamine (FrlR) PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Additional references: PubMed

Martin Lehnik-Habrink, Leonie Rempeters, Ákos T Kovács, Christoph Wrede, Claudia Baierlein, Heike Krebber, Oscar P Kuipers, Jörg Stülke
DEAD-Box RNA helicases in Bacillus subtilis have multiple functions and act independently from each other.
J Bacteriol: 2013, 195(3);534-44
[PubMed:23175651] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947