Difference between revisions of "QcrA"
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| − | * '''Description:''' menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit), component of the cytochrome | + | * '''Description:''' Rieske factor, menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit), component of the cytochrome bc1 complex<br/><br/> |
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
** cell membrane {{PubMed|23880299}} | ** cell membrane {{PubMed|23880299}} | ||
| − | ** delivered to the membrane by the [[TatAY]]-[[TatCY]] [[protein secretion]] system {{PubMed|23256564}} | + | ** delivered to the membrane by the [[TatAY]]-[[TatCY]] [[protein secretion]] system, this depends on prior dusulfide bond formation and co-factor insertion {{PubMed|24652282,23256564}} |
=== Database entries === | === Database entries === | ||
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<pubmed> 24140208 </pubmed> | <pubmed> 24140208 </pubmed> | ||
== Original publications == | == Original publications == | ||
| − | <pubmed>8631715,7592464, 23880299,12850135 12107147, 20817675 23256564 </pubmed> | + | <pubmed>8631715,7592464, 23880299,12850135 12107147, 20817675 23256564 24652282</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 09:17, 22 March 2014
- Description: Rieske factor, menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit), component of the cytochrome bc1 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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:
- Cofactors: contains an iron-sulfur cluster
- Effectors of protein activity:
- Localization:
- cell membrane PubMed
- delivered to the membrane by the TatAY-TatCY protein secretion system, this depends on prior dusulfide bond formation and co-factor insertion PubMed
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
Reviews
Original publications
Vivianne J Goosens, Carmine G Monteferrante, Jan Maarten van Dijl
Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.
J Biol Chem: 2014, 289(19);13124-31
[PubMed:24652282]
[WorldCat.org]
[DOI]
(I p)
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)
