FrlD

• Description: fructosamine kinase
  
  

Gene name	frlD
Synonyms	yurL
Essential	no
Product	fructosamine kinase
Function	metabolism of sugar amines
Gene expression levels in SubtiExpress: frlD
Metabolic function and regulation of this protein in SubtiPathways: Alternative nitrogen sources
MW, pI	30 kDa, 4.909
Gene length, protein length	852 bp, 284 aa
Immediate neighbours	frlR, frlM
Get the DNA and protein sequences (Barbe et al., 2009)
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

This gene is a member of the following regulons

CodY regulon, FrlR regulon

The gene

Basic information

• Locus tag: BSU32570

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: carbohydrate kinase pfkB 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:

Database entries

• Structure:

• UniProt: O32153

• KEGG entry: [3]

• E.C. number:

Expression and regulation

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

• Expression browser: frlD 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

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

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

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)

Elsa Wiame, Pedro Lamosa, Helena Santos, Emile Van Schaftingen
Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine.
Biochem J: 2005, 392(Pt 2);263-9
[PubMed:16153181] [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)

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)