Difference between revisions of "QcrA"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[respiration]]}}, | ||
| + | {{SubtiWiki category|[[membrane proteins]]}} | ||
| + | |||
| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[CcpA regulon]]}}, | ||
| + | {{SubtiWiki regulon|[[ResD regulon]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 20:48, 8 December 2010
- 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 |
| MW, pI | 18 kDa, 6.078 |
| Gene length, protein length | 501 bp, 167 aa |
| Immediate neighbours | qcrB, ypiF |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
respiration, membrane proteins
This gene is a member of the following regulons
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:
- Domains:
- Modification:
- Cofactor(s): contains an iron-sulfur cluster
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P46911
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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
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)
