Difference between revisions of "AhpF"

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* '''Operon:''' ''[[ahpC]]-[[ahpF]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed]
 
* '''Operon:''' ''[[ahpC]]-[[ahpF]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed]
  
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ahpF_4119527_4121056_1 ahpF] {{PubMed|22383849}}
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* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed]
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 10:19, 17 April 2012

  • Description: alkyl hydroperoxide reductase (large subunit) / NADH dehydrogenase

Gene name ahpF
Synonyms ndh
Essential no
Product alkyl hydroperoxide reductase (large subunit) /
NADH dehydrogenase
Function resistance against peroxide stres
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 54 kDa, 4.705
Gene length, protein length 1527 bp, 509 aa
Immediate neighbours ahpC, bglA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AhpF context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

resistance against oxidative and electrophile stress, membrane proteins, phosphoproteins

This gene is a member of the following regulons

PerR regulon

The gene

Basic information

  • Locus tag: BSU40100

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: NADH + acceptor = NAD+ + reduced acceptor (according to Swiss-Prot)
  • Protein family: class-II pyridine nucleotide-disulfide oxidoreductase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on (Ser-48 OR Ser-49) PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1HYU (from Salmonella typhimurium, 52% identity, 69% similarity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

A Sakai, K Katayama, T Katsuragi, Y Tani
Glycolaldehyde-forming route in Bacillus subtilis in relation to vitamin B6 biosynthesis.
J Biosci Bioeng: 2001, 91(2);147-52
[PubMed:16232966] [WorldCat.org] [DOI] (P p)

A F Herbig, J D Helmann
Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA.
Mol Microbiol: 2001, 41(4);849-59
[PubMed:11532148] [WorldCat.org] [DOI] (P p)

N Bsat, L Chen, J D Helmann
Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes.
J Bacteriol: 1996, 178(22);6579-86
[PubMed:8932315] [WorldCat.org] [DOI] (P p)

H Antelmann, S Engelmann, R Schmid, M Hecker
General and oxidative stress responses in Bacillus subtilis: cloning, expression, and mutation of the alkyl hydroperoxide reductase operon.
J Bacteriol: 1996, 178(22);6571-8
[PubMed:8932314] [WorldCat.org] [DOI] (P p)