Difference between revisions of "HypO"

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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
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* Haike Antelmann, University of Greifswald, Germany
  
 
=Your additional remarks=
 
=Your additional remarks=

Revision as of 19:53, 16 January 2012

  • Description: NAD(P)H-flavin nitroreductase

Gene name hypO
Synonyms yfkO
Essential no
Product NAD(P)H-flavin nitroreductase
Function probably involved in NaOCl and diamide detoxification
MW, pI 25 kDa, 5.667
Gene length, protein length 663 bp, 221 aa
Immediate neighbours treR, yfkN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YfkO context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

electron transport/ other, resistance against oxidative and electrophile stress

This gene is a member of the following regulons

HypR regulon


The gene

Basic information

  • Locus tag: BSU07830

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

Additional information

Expression and regulation

  • Operon: hypO (according to DBTBS)
  • Regulation:
    • induced under disulfide stress conditions (diamide, NaOCl) (HypR) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

  • Haike Antelmann, University of Greifswald, Germany

Your additional remarks

References

Original articles

G A Prosser, A V Patterson, D F Ackerley
uvrB gene deletion enhances SOS chromotest sensitivity for nitroreductases that preferentially generate the 4-hydroxylamine metabolite of the anti-cancer prodrug CB1954.
J Biotechnol: 2010, 150(1);190-4
[PubMed:20727918] [WorldCat.org] [DOI] (I p)


Palm GJ, Khanh Chi B, Waack P, Gronau K, Becher D, Albrecht D, Hinrichs W, Read RJ, Antelmann H.
Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.
Nucleic Acids Res. 2012, Jan 11. [Epub ahead of print]
PubMed