Difference between revisions of "YkuP"

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(Extended information on the protein)
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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
YkuP context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

electron transport/ other

This gene is a member of the following regulons

Fur regulon

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:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed unless the cells enter an iron starvation (Fur) PubMed
    • repressed by casamino acids PubMed
  • Regulatory mechanism:
  • 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)