Difference between revisions of "BrxA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || de-bacillithiolation of S-bacillithiolated [[OhrR]] and [[MetE]] | |style="background:#ABCDEF;" align="center"|'''Function''' || de-bacillithiolation of S-bacillithiolated [[OhrR]] and [[MetE]] | ||
|- | |- | ||
− | |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=BSU21860 | + | |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=BSU21860 brxA] |
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=BrxA BrxA] | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 15 kDa, 4.619 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 15 kDa, 4.619 | ||
Line 64: | Line 66: | ||
* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
+ | ** de-bacillithiolation of S-bacillithiolated [[OhrR]] and [[MetE]] {{PubMed|24313874}} | ||
* '''Protein family:''' scpA family (according to Swiss-Prot) | * '''Protein family:''' scpA family (according to Swiss-Prot) | ||
Line 83: | Line 86: | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
+ | ** [[BrxA]]-[[MetE]] {{PubMed|24313874}} | ||
+ | ** [[BrxA]]-[[OhrR]] {{PubMed|24313874}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
Line 102: | Line 107: | ||
* '''Operon:''' ''brxA'' (according to [http://dbtbs.hgc.jp/COG/prom/yphP.html DBTBS]) | * '''Operon:''' ''brxA'' (according to [http://dbtbs.hgc.jp/COG/prom/yphP.html DBTBS]) | ||
− | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yphP_2300221_2300655_-1 | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yphP_2300221_2300655_-1 brxA] {{PubMed|22383849}} |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' |
Revision as of 19:17, 13 December 2013
- Description: bacilliredoxin
Gene name | brxA |
Synonyms | yphP |
Essential | no |
Product | bacilliredoxin |
Function | de-bacillithiolation of S-bacillithiolated OhrR and MetE |
Gene expression levels in SubtiExpress: brxA | |
Interactions involving this protein in SubtInteract: BrxA | |
MW, pI | 15 kDa, 4.619 |
Gene length, protein length | 432 bp, 144 aa |
Immediate neighbours | ypiP, ilvD |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU21860
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: scpA family (according to Swiss-Prot)
- Paralogous protein(s): BrxB
Extended information on the protein
- Kinetic information:
- Modification:
- S-bacillithiolation upon hypochlorite stress on Cys-53 PubMed
- Effectors of protein activity:
Database entries
- UniProt: P54170
- KEGG entry: [4]
- E.C. number:
Additional information
Expression and regulation
- Operon: brxA (according to DBTBS)
- 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
YpdA, BrxA, BrxB and YtxJ co-occur in those species predicted to synthesize bacillithiol.
References
Ahmed Gaballa, Bui Khanh Chi, Alexandra A Roberts, Dörte Becher, Chris J Hamilton, Haike Antelmann, John D Helmann
Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE.
Antioxid Redox Signal: 2014, 21(3);357-67
[PubMed:24313874]
[WorldCat.org]
[DOI]
(I p)
Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038]
[WorldCat.org]
[DOI]
(I p)
Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987]
[WorldCat.org]
[DOI]
(I p)
Ahmed Gaballa, Gerald L Newton, Haike Antelmann, Derek Parsonage, Heather Upton, Mamta Rawat, Al Claiborne, Robert C Fahey, John D Helmann
Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli.
Proc Natl Acad Sci U S A: 2010, 107(14);6482-6
[PubMed:20308541]
[WorldCat.org]
[DOI]
(I p)
Urszula Derewenda, Tomasz Boczek, Kelly L Gorres, Minmin Yu, Li-wei Hung, David Cooper, Andrzej Joachimiak, Ronald T Raines, Zygmunt S Derewenda
Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .
Biochemistry: 2009, 48(36);8664-71
[PubMed:19653655]
[WorldCat.org]
[DOI]
(I p)