SodA

• Description: superoxide dismutase, general stress protein, important for survival of ethanol and paraquat stresses and at low temperatures
  
  

Gene name	sodA
Synonyms	yqgD
Essential	no
Product	superoxide dismutase
Function	detoxification of oxygen radicals
Gene expression levels in SubtiExpress: sodA
MW, pI	22 kDa, 5.203
Gene length, protein length	606 bp, 202 aa
Immediate neighbours	yqgE, yqgC
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

general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress, membrane proteins, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

SigB regulon

The gene

Basic information

• Locus tag: BSU25020

Database entries

• BsubCyc: BSU25020

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2 superoxide + 2 H⁺ = O₂ + H₂O₂ (according to Swiss-Prot)

• Protein family: iron/manganese superoxide dismutase family (according to Swiss-Prot)

• Paralogous protein(s): SodF

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on Thr-34 AND Thr-70 PubMed

• Cofactors: manganese

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm PubMed

Database entries

• BsubCyc: BSU25020

• Structure: 2RCV

• UniProt: P54375

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: sodA PubMed

• Sigma factor: SigB PubMed

• Regulation:
  • induced by stress (SigB) PubMed
  • constitutive expression PubMed

• Regulatory mechanism:

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 5124 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 25098 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 36093 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 14195 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 29664 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alexander Reder, Dirk Höper, Ulf Gerth, Michael Hecker
Contributions of individual σB-dependent general stress genes to oxidative stress resistance of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3601-10
[PubMed:22582280] [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)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [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)

Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528] [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)

T Inaoka, Y Matsumura, T Tsuchido
SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of Bacillus subtilis.
J Bacteriol: 1999, 181(6);1939-43
[PubMed:10074093] [WorldCat.org] [DOI] (P p)

T Inaoka, Y Matsumura, T Tsuchido
Molecular cloning and nucleotide sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis.
J Bacteriol: 1998, 180(14);3697-703
[PubMed:9658017] [WorldCat.org] [DOI] (P p)

A O Henriques, L R Melsen, C P Moran
Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis.
J Bacteriol: 1998, 180(9);2285-91
[PubMed:9573176] [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)