Difference between revisions of "BrxA"
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* '''Protein family:''' scpA family (according to Swiss-Prot) | * '''Protein family:''' scpA family (according to Swiss-Prot) | ||
− | * '''Paralogous protein(s):''' [[ | + | * '''Paralogous protein(s):''' [[BrxB]] |
=== Extended information on the protein === | === Extended information on the protein === | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' contains an CxC redox motif [http://www.ncbi.nlm.nih.gov/pubmed/20308541] | + | * '''[[Domains]]:''' contains an CxC redox motif [http://www.ncbi.nlm.nih.gov/pubmed/20308541] |
* '''Modification:''' | * '''Modification:''' | ||
** S-bacillithiolation upon hypochlorite stress on Cys-53 {{PubMed|21749987}} | ** S-bacillithiolation upon hypochlorite stress on Cys-53 {{PubMed|21749987}} | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
Line 100: | Line 100: | ||
=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' '' | + | * '''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 yphP] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yphP_2300221_2300655_-1 yphP] {{PubMed|22383849}} | ||
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=Your additional remarks= | =Your additional remarks= | ||
− | [[YpdA]], [[ | + | [[YpdA]], [[BrxA]], [[BrxB]] and [[YtxJ]] co-occur in those species predicted to synthesize bacillithiol. |
=References= | =References= | ||
− | <pubmed> 22938038,19653655 20308541 21749987</pubmed> | + | <pubmed> 22938038,19653655 20308541 21749987 24313874 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:56, 13 December 2013
- Description: disulfide isomerase, bacilliredoxin
Gene name | brxA |
Synonyms | yphP |
Essential | no |
Product | disulfide isomerase, bacilliredoxin |
Function | de-bacillithiolation of S-bacillithiolated OhrR and MetE |
Gene expression levels in SubtiExpress: yphP | |
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)