KatA

• Description: main vegetative catalase 1
  
  

Gene name	katA
Synonyms	kat-19
Essential	no
Product	vegetative catalase
Function	detoxification (degradation) of hydrogen peroxide
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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:

• Cofactor(s): contains an iron-sulfur cluster, heme

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1SI8 (enzyme from Enterococcus faecalis, 68% identity)

• UniProt: P26901

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: katA PubMed

• Expression browser: katA PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • PerR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)