Difference between revisions of "AhpC"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}}, | {{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}}, | ||
− | {{SubtiWiki category|[[phosphoproteins]]}} | + | {{SubtiWiki category|[[phosphoproteins]]}}, |
+ | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed] | * '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed] | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ahpC_4118950_4119513_1 ahpC] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ahpC_4118950_4119513_1 ahpC] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed] | + | * '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed] |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
− | <pubmed>11532148,,8932314,8932315,11532148,16493705, </pubmed> | + | <pubmed>11532148,15378759,8932314,8932315,11532148,16493705, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:19, 5 March 2014
- Description: alkyl hydroperoxide reductase (small subunit)
Gene name | ahpC |
Synonyms | perR |
Essential | no |
Product | alkyl hydroperoxide reductase (small subunit) |
Function | resistance against peroxide stres |
Gene expression levels in SubtiExpress: ahpC | |
Metabolic function and regulation of this protein in SubtiPathways: ahpC | |
MW, pI | 20 kDa, 4.283 |
Gene length, protein length | 561 bp, 187 aa |
Immediate neighbours | gntZ, ahpF |
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
resistance against oxidative and electrophile stress, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU40090
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH (according to Swiss-Prot)
- Protein family: ahpC/TSA family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Effectors of protein activity:
Database entries
- UniProt: P80239
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
A F Herbig, J D Helmann
Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA.
Mol Microbiol: 2001, 41(4);849-59
[PubMed:11532148]
[WorldCat.org]
[DOI]
(P p)
N Bsat, L Chen, J D Helmann
Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes.
J Bacteriol: 1996, 178(22);6579-86
[PubMed:8932315]
[WorldCat.org]
[DOI]
(P p)
H Antelmann, S Engelmann, R Schmid, M Hecker
General and oxidative stress responses in Bacillus subtilis: cloning, expression, and mutation of the alkyl hydroperoxide reductase operon.
J Bacteriol: 1996, 178(22);6571-8
[PubMed:8932314]
[WorldCat.org]
[DOI]
(P p)