Difference between revisions of "YkuP"

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Line 83: Line 83:
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:''' FMN
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
Line 118: Line 118:
 
** induced upon iron starvation ([[Fur]]) {{PubMed|12354229}}  
 
** induced upon iron starvation ([[Fur]]) {{PubMed|12354229}}  
 
** repressed by casamino acids [http://www.ncbi.nlm.nih.gov/pubmed/12107147 PubMed]
 
** repressed by casamino acids [http://www.ncbi.nlm.nih.gov/pubmed/12107147 PubMed]
 +
** expressed under anaerobic conditions ([[ResD]]) {{PubMed|24214949}}
 +
** induced by nitric oxide under anaerobic conditions ([[NsrR]]) {{PubMed|24214949}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 
** [[Fur]]: transcription repression {{PubMed|12354229}}  
 
** [[Fur]]: transcription repression {{PubMed|12354229}}  
 +
** [[ResD]]: transcription activation {{PubMed|24214949}}
 +
** [[NsrR]]: transcription repression {{PubMed|24214949}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
Line 145: Line 149:
  
 
=References=
 
=References=
'''Additional publications:''' {{PubMed|21665975}}
+
<pubmed>15449930,17127770 ,12354229,12107147, 20186410 24214949 21665975</pubmed>
<pubmed>15449930,17127770 ,12354229,12107147, 20186410</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:33, 26 May 2014

  • 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
YkuP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YkuP expression.png















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:
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • induced upon iron starvation (Fur) PubMed
    • repressed by casamino acids PubMed
    • expressed under anaerobic conditions (ResD) PubMed
    • induced by nitric oxide under anaerobic conditions (NsrR) 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:

Labs working on this gene/protein

Your additional remarks

References

Bernadette Henares, Sushma Kommineni, Onuma Chumsakul, Naotake Ogasawara, Shu Ishikawa, Michiko M Nakano
The ResD response regulator, through functional interaction with NsrR and fur, plays three distinct roles in Bacillus subtilis transcriptional control.
J Bacteriol: 2014, 196(2);493-503
[PubMed:24214949] [WorldCat.org] [DOI] (I p)

Lorena Chazarreta-Cifre, Leticia Martiarena, Diego de Mendoza, Silvia G Altabe
Role of ferredoxin and flavodoxins in Bacillus subtilis fatty acid desaturation.
J Bacteriol: 2011, 193(16);4043-8
[PubMed:21665975] [WorldCat.org] [DOI] (I p)

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)