AhpF

• 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
Gene expression levels in SubtiExpress: ahpF
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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
  • phosphorylated on Arg-457 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure: 1HYU (from Salmonella typhimurium, 52% identity, 69% similarity) PubMed

• UniProt: P42974

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ahpC-ahpF PubMed

• Expression browser: ahpF PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by H2O2 (PerR) PubMed

• Regulatory mechanism:
  • PerR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

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)