Difference between revisions of "YkuP"
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** [[Des]]-[[YkuP]] (electron transfer to [[Des]]) {{PubMed|21665975}}  | ** [[Des]]-[[YkuP]] (electron transfer to [[Des]]) {{PubMed|21665975}}  | ||
| − | * '''Localization:'''  | + | * '''[[Localization]]:'''  | 
=== Database entries ===  | === Database entries ===  | ||
Revision as of 11:59, 8 November 2011
-  Description: flavodoxin, binds FMN, replaces ferredoxin under conditions of iron limitation 
 
| Gene name | ykuP | 
| Synonyms | |
| Essential | no | 
| Product | flavodoxin | 
| Function | electron transfer | 
| Interactions involving this protein in SubtInteract: YkuP | |
|  Metabolic function and regulation of this protein in SubtiPathways:  Lys, Thr  | |
| MW, pI | 20 kDa, 4.098 | 
| Gene length, protein length | 534 bp, 178 aa | 
| Immediate neighbours | ykuO, ykuQ | 
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14170
 
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: flavodoxin-like domain (according to Swiss-Prot)
 
- Paralogous protein(s): YkuN
 
Extended information on the protein
- Kinetic information:
 
- Domains:
 
- Modification:
 
- Cofactor(s):
 
- Effectors of protein activity:
 
Database entries
- Structure:
 
- UniProt: O34589
 
- KEGG entry: [3]
 
- E.C. number:
 
Additional information
Expression and regulation
- Regulation:
 
- Additional information:
 
Biological materials
- Mutant:
 
- Expression vector:
 
- lacZ fusion:
 
- GFP fusion:
 
- two-hybrid system:
 
- Antibody:
 
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
Marco Girhard, Tobias Klaus, Yogan Khatri, Rita Bernhardt, Vlada B Urlacher  
Characterization of the versatile monooxygenase CYP109B1 from Bacillus subtilis. 
Appl Microbiol Biotechnol: 2010, 87(2);595-607 
[PubMed:20186410]
  [WorldCat.org]
 [DOI]
 (I p)
Zhi-Qiang Wang, Rachel J Lawson, Madhavan R Buddha, Chin-Chuan Wei, Brian R Crane, Andrew W Munro, Dennis J Stuehr  
Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase. 
J Biol Chem: 2007, 282(4);2196-202 
[PubMed:17127770]
  [WorldCat.org]
 [DOI]
 (P p)
Rachel J Lawson, Claes von Wachenfeldt, Ihtshamul Haq, John Perkins, Andrew W Munro  
Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI. 
Biochemistry: 2004, 43(39);12390-409 
[PubMed:15449930]
  [WorldCat.org]
 [DOI]
 (P p)
Noel Baichoo, Tao Wang, Rick Ye, John D Helmann  
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. 
Mol Microbiol: 2002, 45(6);1613-29 
[PubMed:12354229]
  [WorldCat.org]
 [DOI]
 (P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker  
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability. 
J Bacteriol: 2002, 184(15);4288-95 
[PubMed:12107147]
  [WorldCat.org]
 [DOI]
 (P p)
