Difference between revisions of "AdhR"
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− | * '''Description:''' transcriptional activator of ''[[adhA]]-[[yraA]]'' <br/><br/> | + | * '''Description:''' transcriptional activator ([[transcription factors of the MerR family|MerR family]]) of ''[[adhA]]-[[yraA]]'', responsive to formaldehyde and methylglyoxal <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional activator ([[MerR family]]) | + | |style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional activator ([[transcription factors of the MerR family|MerR family]]) |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || regulation of the protective response to formaldehyde | + | |style="background:#ABCDEF;" align="center"|'''Function''' || regulation of the protective response to formaldehyde and methylglyoxal |
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU27000 adhR] | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 9.637 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 9.637 | ||
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 420 bp, 140 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 420 bp, 140 aa | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yraD]]'', ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yraD]]'', ''[[yrzP]]'' |
|- | |- | ||
− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27000 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27000 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27000 DNA_with_flanks] |
|- | |- | ||
|- | |- | ||
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|colspan="2" | '''Genetic context''' <br/> [[Image:yraB_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:yraB_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yraB_2755382_2755804_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:adhR_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU27000]] | ||
|- | |- | ||
|} | |} | ||
__TOC__ | __TOC__ | ||
− | + | <br/><br/><br/><br/> | |
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
<br/><br/> | <br/><br/> | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU27000&redirect=T BSU27000] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
− | |||
=The protein= | =The protein= | ||
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* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
− | * '''Protein family:''' | + | * '''Protein family:''' [[transcription factors of the MerR family|MerR family]] |
* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' | ||
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* '''Domains:''' | * '''Domains:''' | ||
− | * '''Modification:''' activity probably controlled via thiol-(S)-alkylation | + | * '''Modification:''' activity probably redox-controlled via thiol-(S)-alkylation at Cys-52 by aldehydes {{PubMed|19170879}} |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
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* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
− | * '''Localization:''' | + | * '''[[Localization]]:''' cytoplasmic |
− | |||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU27000&redirect=T BSU27000] | ||
* '''Structure:''' | * '''Structure:''' | ||
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* '''Operon:''' | * '''Operon:''' | ||
− | * ''' | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yraB_2755382_2755804_-1 adhR] {{PubMed|22383849}} |
− | * '''Regulation:''' | + | * '''Sigma factor:''' |
+ | |||
+ | * '''Regulation:''' | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = | ||
Line 124: | Line 130: | ||
=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
+ | |||
+ | [[Haike Antelmann]],University of Greifswald, Germany | ||
=Your additional remarks= | =Your additional remarks= | ||
Line 129: | Line 137: | ||
=References= | =References= | ||
− | <pubmed> | + | =Reviews= |
+ | |||
+ | <pubmed>21722790</pubmed> | ||
+ | Antelmann H, Helmann JD. | ||
+ | Thiol-based redox switches and gene regulation. | ||
+ | Antioxid Redox Signal. 2011,14:1049-63. | ||
+ | {{PubMed|20626317}} | ||
+ | |||
+ | =Original articles= | ||
+ | |||
+ | <pubmed>19170879</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Latest revision as of 13:14, 22 June 2014
- Description: transcriptional activator (MerR family) of adhA-yraA, responsive to formaldehyde and methylglyoxal
Gene name | adhR |
Synonyms | yraB |
Essential | no |
Product | transcriptional activator (MerR family) |
Function | regulation of the protective response to formaldehyde and methylglyoxal |
Gene expression levels in SubtiExpress: adhR | |
MW, pI | 16 kDa, 9.637 |
Gene length, protein length | 420 bp, 140 aa |
Immediate neighbours | yraD, yrzP |
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
transcription factors and their control, resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27000
Phenotypes of a mutant
Database entries
- BsubCyc: BSU27000
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: MerR family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: activity probably redox-controlled via thiol-(S)-alkylation at Cys-52 by aldehydes PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasmic
Database entries
- BsubCyc: BSU27000
- Structure:
- UniProt: O06008
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Haike Antelmann,University of Greifswald, Germany
Your additional remarks
References
Reviews
Alastair G McEwan, Karrera Y Djoko, Nathan H Chen, Rafael L M Couñago, Stephen P Kidd, Adam J Potter, Michael P Jennings
Novel bacterial MerR-like regulators their role in the response to carbonyl and nitrosative stress.
Adv Microb Physiol: 2011, 58;1-22
[PubMed:21722790]
[WorldCat.org]
[DOI]
(I p)
Antelmann H, Helmann JD. Thiol-based redox switches and gene regulation. Antioxid Redox Signal. 2011,14:1049-63. PubMed
Original articles
Thi Thu Huyen Nguyen, Warawan Eiamphungporn, Ulrike Mäder, Manuel Liebeke, Michael Lalk, Michael Hecker, John D Helmann, Haike Antelmann
Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR).
Mol Microbiol: 2009, 71(4);876-94
[PubMed:19170879]
[WorldCat.org]
[DOI]
(I p)