Difference between revisions of "AhpC"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 24849 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 24849 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 44043 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 44043 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 43066 {{PubMed|21395229}}
 +
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 62318 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:32, 17 April 2014

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















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

Phenotypes of a mutant

Database entries

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

Additional information

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:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1WE0 (from Amphibacillus xylanus, 78% identity, 88% similarity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 24849 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 44043 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:

Labs working on this gene/protein

Your additional remarks

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)