AhpC

• Description: alkyl hydroperoxide reductase (small subunit)
  
  

Gene name	ahpC
Synonyms	perR
Essential	no
Product	alkyl hydroperoxide reductase (small subunit)
Function	resistance against peroxide stres
Gene expression levels in SubtiExpress: ahpC
Metabolic function and regulation of this protein in SubtiPathways: ahpC
MW, pI	20 kDa, 4.283
Gene length, protein length	561 bp, 187 aa
Immediate neighbours	gntZ, ahpF
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

resistance against oxidative and electrophile stress, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

PerR regulon

The gene

Basic information

• Locus tag: BSU40090

Database entries

• BsubCyc: BSU40090

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH (according to Swiss-Prot)

• Protein family: ahpC/TSA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU40090

• Structure: 1WE0 (from Amphibacillus xylanus, 78% identity, 88% similarity) PubMed

• UniProt: P80239

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ahpC-ahpF PubMed

• Expression browser: ahpC PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by H2O2 (PerR) PubMed

• Regulatory mechanism:
  • PerR: transcription repression PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 69388 PubMed

• • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 43066 PubMed

• • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 62318 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)