Difference between revisions of "AzoR2"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[sporulation proteins]]}}, | ||
| + | {{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[MhqR regulon]]}}, | ||
| + | {{SubtiWiki regulon|[[SigG regulon]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 23:22, 8 December 2010
- Description: similar to NAD(P)H dehydrogenase (quinone)
| Gene name | azoR2 |
| Synonyms | yvaB |
| Essential | no |
| Product | azoreductase |
| Function | resistance to 2-methylhydroquinone |
| MW, pI | 23 kDa, 5.114 |
| Gene length, protein length | 633 bp, 211 aa |
| Immediate neighbours | yvaA, yvaC |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
sporulation proteins, resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU33540
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: azoreductase type 1 family (according to Swiss-Prot)
- Paralogous protein(s): AzoR1
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 3P0R (from B. anthracis, 43% identity, 61% similarity)
- UniProt: O32224
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: azoR2 PubMed
- 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
Montira Leelakriangsak, Nguyen Thi Thu Huyen, Stefanie Töwe, Nguyen van Duy, Dörte Becher, Michael Hecker, Haike Antelmann, Peter Zuber
Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis.
Mol Microbiol: 2008, 67(5);1108-24
[PubMed:18208493]
[WorldCat.org]
[DOI]
(I p)
Stefanie Töwe, Montira Leelakriangsak, Kazuo Kobayashi, Nguyen Van Duy, Michael Hecker, Peter Zuber, Haike Antelmann
The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis.
Mol Microbiol: 2007, 66(1);40-54
[PubMed:17725564]
[WorldCat.org]
[DOI]
(P p)
Stephanie T Wang, Barbara Setlow, Erin M Conlon, Jessica L Lyon, Daisuke Imamura, Tsutomu Sato, Peter Setlow, Richard Losick, Patrick Eichenberger
The forespore line of gene expression in Bacillus subtilis.
J Mol Biol: 2006, 358(1);16-37
[PubMed:16497325]
[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)
