Difference between revisions of "HypR"
Line 73: | Line 73: | ||
=== Extended information on the protein === | === Extended information on the protein === | ||
− | * '''Kinetic information:''' Cys14 redox sensing Cys, has lower pKa of 6.36 | + | * '''Kinetic information:''' Cys14 redox sensing Cys, has lower pKa of 6.36 {{PubMed|22238377}} |
− | * '''Domains:''' 5 alpha helices, 2 beta sheets, MarR-fold with wHTH motif, alpha4 major groove recognition helix, beta2 and 3 form the wing; alpha5 dimer interface | + | * '''Domains:''' 5 alpha helices, 2 beta sheets, MarR-fold with wHTH motif, alpha4 major groove recognition helix, beta2 and 3 form the wing; alpha5 dimer interface {{PubMed|22238377}} |
− | + | * '''Modification:''' oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress {{PubMed|22238377}} | |
− | * '''Modification:''' oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
Line 105: | Line 104: | ||
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
− | * '''Regulation:''' activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro | + | * '''Regulation:''' activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro {{PubMed|22238377}} |
+ | |||
+ | * '''Regulatory mechanism:''' redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo {{PubMed|22238377}} | ||
− | |||
− | * '''Additional information:''' Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha4 helices of the HypR dimer about 4 Angstroem towards each other that leads to activation of HypR | + | * '''Additional information:''' Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha4 helices of the HypR dimer about 4 Angstroem towards each other that leads to activation of HypR {{PubMed|22238377}} |
=Biological materials = | =Biological materials = |
Revision as of 08:52, 13 January 2012
- Description: MarR/DUF24-family transcription regulator, positively controls the nitroreductase gene yfkO (hypO) in response to disulfide stress
Gene name | yybR (hypR) |
Synonyms | hypR |
Essential | no |
Product | MarR/DUF24-family transcription regulator HypR |
Function | positively controls nitroreductase gene yfkO (hypO) in response to disulfide stress (diamide, NaOCl) |
MW, pI | 14 kDa, 8.415 |
Gene length, protein length | 375 bp, 125 aa |
Immediate neighbours | cotF, ppaC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
- 1 Categories containing this gene/protein
- 2 This gene is a member of the following regulons
- 3 This gene is a member of the following regulons
- 4 The YybR (HypR) regulon:
- 5 The gene
- 6 The protein
- 7 Expression and regulation
- 8 Biological materials
- 9 Labs working on this gene/protein
- 10 Your additional remarks
- 11 References
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
This gene is a member of the following regulons
The YybR (HypR) regulon:
The gene
Basic information
- Locus tag: BSU40540
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
hypR autoregulated by disulfide stress
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: MarR/DUF24-family regulator
- Paralogous protein(s): YdeP,YkvN
Extended information on the protein
- Kinetic information: Cys14 redox sensing Cys, has lower pKa of 6.36 PubMed
- Domains: 5 alpha helices, 2 beta sheets, MarR-fold with wHTH motif, alpha4 major groove recognition helix, beta2 and 3 form the wing; alpha5 dimer interface PubMed
- Modification: oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasmic
Database entries
- Structure: tba
- UniProt: P37486
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: yybR (hypR)(according to DBTBS)
- Regulation: activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro PubMed
- Regulatory mechanism: redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo PubMed
- Additional information: Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha4 helices of the HypR dimer about 4 Angstroem towards each other that leads to activation of HypR PubMed
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