YkuP

• Description: flavodoxin, binds FMN, replaces ferredoxin under conditions of iron limitation
  
  

Gene name	ykuP
Synonyms
Essential	no
Product	flavodoxin
Function	electron transfer
Gene expression levels in SubtiExpress: ykuP
Interactions involving this protein in SubtInteract: YkuP
Metabolic function and regulation of this protein in SubtiPathways: ykuP
MW, pI	20 kDa, 4.098
Gene length, protein length	534 bp, 178 aa
Immediate neighbours	ykuO, ykuQ
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

electron transport/ other

This gene is a member of the following regulons

Fur regulon

The gene

Basic information

• Locus tag: BSU14170

Database entries

• BsubCyc: BSU14170

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • YkuP-BioI PubMed
  • YjiB-YkuP PubMed
  • Des-YkuP (electron transfer to Des) PubMed

• Localization:

Database entries

• BsubCyc: BSU14170

• Structure:

• UniProt: O34589

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ykuN-ykuO-ykuP PubMed

• Expression browser: ykuP PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced upon iron starvation (Fur) PubMed
  • repressed by casamino acids PubMed

• Regulatory mechanism:
  • Fur: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 4675 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1156 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)