FrlB

• 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: frlB
MW, pI	36 kDa, 5.442
Gene length, protein length	984 bp, 328 aa
Immediate neighbours	frlO, yurQ
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

This gene is a member of the following regulons

CodY regulon, FrlR regulon

The gene

Basic information

• Locus tag: BSU32610

Database entries

• BsubCyc: BSU32610

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization: membrane associated PubMed

Database entries

• BsubCyc: BSU32610

• Structure: 3EUA

• UniProt: O32157

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • frlB-frlO-frlN-frlM-frlD PubMed
  • frlB-frlO PubMed
  • frlB PubMed

• Expression browser: frlB PubMed

• 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

• Regulatory mechanism:
  • CodY: transcription repression PubMed1, PubMed2
  • FrlR: transcription repression PubMed

• Additional information:
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
  • the frlB-frlO-frlN-frlM-frlD operon is not expressed in a cshA mutant PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 3695 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Veronika Maria Deppe, Stephanie Klatte, Johannes Bongaerts, Karl-Heinz Maurer, Timothy O'Connell, Friedhelm Meinhardt
Genetic control of amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR.
Appl Environ Microbiol: 2011, 77(9);2839-46
[PubMed:21398478] [WorldCat.org] [DOI] (I p)

Veronika Maria Deppe, Johannes Bongaerts, Timothy O'Connell, Karl-Heinz Maurer, Friedhelm Meinhardt
Enzymatic deglycation of Amadori products in bacteria: mechanisms, occurrence and physiological functions.
Appl Microbiol Biotechnol: 2011, 90(2);399-406
[PubMed:21347729] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Boris R Belitsky, Abraham L Sonenshein
Genetic and biochemical analysis of CodY-binding sites in Bacillus subtilis.
J Bacteriol: 2008, 190(4);1224-36
[PubMed:18083814] [WorldCat.org] [DOI] (I p)

Elsa Wiame, Armelle Duquenne, Ghislain Delpierre, Emile Van Schaftingen
Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis.
FEBS Lett: 2004, 577(3);469-72
[PubMed:15556630] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)