KatA

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  • Description: main vegetative catalase 1

Gene name katA
Synonyms kat-19
Essential no
Product vegetative catalase
Function detoxification (degradation) of hydrogen peroxide
Gene expression levels in SubtiExpress: katA
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 54 kDa, 6.151
Gene length, protein length 1449 bp, 483 aa
Immediate neighbours senS, ssuB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
KatA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
KatA expression.png




























Categories containing this gene/protein

resistance against oxidative and electrophile stress, phosphoproteins

This gene is a member of the following regulons

PerR regulon

The gene

Basic information

  • Locus tag: BSU08820

Phenotypes of a mutant

  • increased sensitivity to oxidative stress PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 H2O2 = O2 + 2 H2O (according to Swiss-Prot)
  • Protein family: catalase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-366 PubMed
  • Cofactor(s): contains an iron-sulfur cluster, heme
  • Effectors of protein activity:

Database entries

  • Structure: 1SI8 (enzyme from Enterococcus faecalis, 68% identity)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • induced in the presence of hydrogen peroxide and paraquat (PerR) PubMed
  • 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

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)

Melinda J Faulkner, Zhen Ma, Mayuree Fuangthong, John D Helmann
Derepression of the Bacillus subtilis PerR peroxide stress response leads to iron deficiency.
J Bacteriol: 2012, 194(5);1226-35
[PubMed:22194458] [WorldCat.org] [DOI] (I p)

Wang Yung Tu, Susanne Pohl, Pijug Summpunn, Silvio Hering, Sandra Kerstan, Colin R Harwood
Comparative analysis of the responses of related pathogenic and environmental bacteria to oxidative stress.
Microbiology (Reading): 2012, 158(Pt 3);636-647
[PubMed:22174384] [WorldCat.org] [DOI] (I 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)

L Casillas-Martinez, P Setlow
Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents.
J Bacteriol: 1997, 179(23);7420-5
[PubMed:9393707] [WorldCat.org] [DOI] (P p)

S Engelmann, M Hecker
Impaired oxidative stress resistance of Bacillus subtilis sigB mutants and the role of katA and katE.
FEMS Microbiol Lett: 1996, 145(1);63-9
[PubMed:8931328] [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)

L Chen, L Keramati, J D Helmann
Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions.
Proc Natl Acad Sci U S A: 1995, 92(18);8190-4
[PubMed:7667267] [WorldCat.org] [DOI] (P p)