Difference between revisions of "BrxA"
| Line 1: | Line 1: | ||
| − | * '''Description:''' disulfide isomerase <br/><br/> | + | * '''Description:''' disulfide isomerase, putative bacilliredoxin <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 10: | Line 10: | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || disulfide isomerase | + | |style="background:#ABCDEF;" align="center"| '''Product''' || disulfide isomerase, putative bacilliredoxin |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown | |style="background:#ABCDEF;" align="center"|'''Function''' || unknown | ||
| Line 52: | Line 52: | ||
=== Additional information=== | === Additional information=== | ||
| − | |||
| − | |||
| − | |||
=The protein= | =The protein= | ||
| Line 72: | Line 69: | ||
* '''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}} | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
| Line 78: | Line 76: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
* '''Localization:''' | * '''Localization:''' | ||
| Line 126: | Line 124: | ||
=References= | =References= | ||
| − | <pubmed> 19653655 20308541</pubmed> | + | <pubmed> 19653655 20308541 21749987</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 08:27, 14 July 2011
- Description: disulfide isomerase, putative bacilliredoxin
| Gene name | yphP |
| Synonyms | |
| Essential | no |
| Product | disulfide isomerase, putative bacilliredoxin |
| Function | unknown |
| MW, pI | 15 kDa, 4.619 |
| Gene length, protein length | 432 bp, 144 aa |
| Immediate neighbours | ypiP, ilvD |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
poorly characterized/ putative enzymes
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): yqiW
Extended information on the protein
- Kinetic information:
- Domains: contains an CxC redox motif [3]
- Modification:
- S-bacillithiolation upon hypochlorite stress on Cys-53 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- UniProt: P54170
- KEGG entry: [4]
- E.C. number:
Additional information
Expression and regulation
- Operon: yphP (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, YqiW, YphP and YtxJ cooccur in those species predicted to synthesize bacillithiol.
References
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)
