QcrA

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  • Description: menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit), component of the cytochrome bc complex

Gene name qcrA
Synonyms bfcA, petC
Essential no
Product menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit)
Function respiration
Gene expression levels in SubtiExpress: qcrA
Interactions involving this protein in SubtInteract: QcrA
MW, pI 18 kDa, 6.078
Gene length, protein length 501 bp, 167 aa
Immediate neighbours qcrB, ypiF
Sequences Protein DNA DNA_with_flanks
Genetic context
QcrA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
QcrA expression.png















Categories containing this gene/protein

respiration, membrane proteins

This gene is a member of the following regulons

AbrB regulon, CcpA regulon, ResD regulon

The gene

Basic information

  • Locus tag: BSU22560

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: accD/PCCB family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • 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

Reviews

Original publications

Pedro M F Sousa, Marco A M Videira, Filipe A S Santos, Brian L Hood, Thomas P Conrads, Ana M P Melo
The bc:caa3 supercomplexes from the Gram positive bacterium Bacillus subtilis respiratory chain: a megacomplex organization?
Arch Biochem Biophys: 2013, 537(1);153-60
[PubMed:23880299] [WorldCat.org] [DOI] (I p)

Vivianne J Goosens, Andreas Otto, Corinna Glasner, Carmine C Monteferrante, René van der Ploeg, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
Novel twin-arginine translocation pathway-dependent phenotypes of Bacillus subtilis unveiled by quantitative proteomics.
J Proteome Res: 2013, 12(2);796-807
[PubMed:23256564] [WorldCat.org] [DOI] (I p)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

G Sun, E Sharkova, R Chesnut, S Birkey, M F Duggan, A Sorokin, P Pujic, S D Ehrlich, F M Hulett
Regulators of aerobic and anaerobic respiration in Bacillus subtilis.
J Bacteriol: 1996, 178(5);1374-85
[PubMed:8631715] [WorldCat.org] [DOI] (P p)

J Yu, L Hederstedt, P J Piggot
The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization.
J Bacteriol: 1995, 177(23);6751-60
[PubMed:7592464] [WorldCat.org] [DOI] (P p)