Difference between revisions of "FrlD"
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<big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
− | <pubmed>15556630,16153181, 21347729,12618455, 12823818 </pubmed> | + | <pubmed>15556630,16153181, 21347729,12618455, 12823818, 21398478</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:42, 20 April 2012
- Description: fructosamine kinase
Gene name | frlD |
Synonyms | yurL |
Essential | no |
Product | fructosamine kinase |
Function | metabolism of sugar amines |
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
|
Contents
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
The gene
Basic information
- Locus tag: BSU32570
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: 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:
Database entries
- Structure:
- UniProt: O32153
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
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
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)
Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818]
[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)