Difference between revisions of "QoxB"
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=== Additional information=== | === Additional information=== | ||
− | + | * A mutation was found in this gene after evolution under relexed selection for sporulation {{PubMed|21821766}} | |
− | |||
− | |||
=The protein= | =The protein= | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' cell | + | * '''[[Localization]]:''' cell membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] |
=== Database entries === | === Database entries === | ||
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=References= | =References= | ||
− | <pubmed> 11073895 1316894 20351111,10551842,18763711, </pubmed> | + | <pubmed> 11073895 1316894 20351111,10551842,18763711, 21821766</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:35, 15 August 2011
- Description: cytochrome aa3 quinol oxidase (subunit I)
Gene name | qoxB |
Synonyms | ipa-38d |
Essential | no |
Product | cytochrome aa3 quinol oxidase (subunit I) |
Function | respiration |
MW, pI | 73 kDa, 8.848 |
Gene length, protein length | 1947 bp, 649 aa |
Immediate neighbours | qoxC, qoxA |
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: BSU38160
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
- A mutation was found in this gene after evolution under relexed selection for sporulation PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Ubiquinol-8 + O2 = Ubiquinone-8 + H2O (according to Swiss-Prot)
- Protein family: heme-copper respiratory oxidase family (according to Swiss-Prot)
- Paralogous protein(s): CtaD
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane PubMed
Database entries
- Structure:
- UniProt: P34956
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and 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
Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766]
[WorldCat.org]
[DOI]
(I p)
Sophia M Yi, Kuppala V Narasimhulu, Rimma I Samoilova, Robert B Gennis, Sergei A Dikanov
Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis.
J Biol Chem: 2010, 285(24);18241-51
[PubMed:20351111]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
L Winstedt, C von Wachenfeldt
Terminal oxidases of Bacillus subtilis strain 168: one quinol oxidase, cytochrome aa(3) or cytochrome bd, is required for aerobic growth.
J Bacteriol: 2000, 182(23);6557-64
[PubMed:11073895]
[WorldCat.org]
[DOI]
(P p)
N Azarkina, S Siletsky, V Borisov, C von Wachenfeldt, L Hederstedt, A A Konstantinov
A cytochrome bb'-type quinol oxidase in Bacillus subtilis strain 168.
J Biol Chem: 1999, 274(46);32810-7
[PubMed:10551842]
[WorldCat.org]
[DOI]
(P p)
M Santana, F Kunst, M F Hullo, G Rapoport, A Danchin, P Glaser
Molecular cloning, sequencing, and physiological characterization of the qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase.
J Biol Chem: 1992, 267(15);10225-31
[PubMed:1316894]
[WorldCat.org]
(P p)