Difference between revisions of "BshA"
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= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[Spx regulon]]}} | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| + | ** subject to feedback inhibition by bacillithiol {{PubMed|22569254}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ypjH_2357078_2358211_-1 bshA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ypjH_2357078_2358211_-1 bshA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|23894131}} |
* '''Regulation:''' | * '''Regulation:''' | ||
| + | ** induced by diamide stess (thiol depletion) ([[Spx]]) {{PubMed|23894131}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[Spx]]: transcription activation {{PubMed|23894131}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
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=Biological materials = | =Biological materials = | ||
| − | * '''Mutant:''' ''bshA::mls'' available in [[John_Helmann]] lab | + | * '''Mutant:''' |
| − | ** GP88 ('' | + | ** ''bshA::mls'' available in [[John_Helmann]] lab |
| + | ** GP88 (''bshA''::''pX2''(''cat'')), available in [[Jörg Stülke]]'s lab | ||
* '''Expression vector:''' | * '''Expression vector:''' | ||
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=References= | =References= | ||
| − | + | <pubmed> 20308541 19578333 22569254 20799687 23894131</pubmed> | |
| − | <pubmed> 20308541 19578333 22569254 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:13, 1 August 2013
- Description: L-malic acid glycosyltransferase, involved in bacillithiol synthesis
| Gene name | bshA |
| Synonyms | jojH, ypjH |
| Essential | no |
| Product | L-malic acid glycosyltransferase |
| Function | biosynthesis of bacillithiol |
| Gene expression levels in SubtiExpress: bshA | |
| MW, pI | 41 kDa, 6.149 |
| Gene length, protein length | 1131 bp, 377 aa |
| Immediate neighbours | cca, bshB1 |
| 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
miscellaneous metabolic pathways, resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU22460
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: UDP-GlcNAc + L-malate = GlcNAc(α1→2)L-malate PubMed; also uses D-malate as a substrate, but with much lower affinity PubMed
- Protein family: NamA subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- subject to feedback inhibition by bacillithiol PubMed
Database entries
- UniProt: P42982
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- bshA::mls available in John_Helmann lab
- GP88 (bshA::pX2(cat)), available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Ahmed Gaballa, Haike Antelmann, Chris J Hamilton, John D Helmann
Regulation of Bacillus subtilis bacillithiol biosynthesis operons by Spx.
Microbiology (Reading): 2013, 159(Pt 10);2025-2035
[PubMed:23894131]
[WorldCat.org]
[DOI]
(I p)
Heather Upton, Gerald L Newton, Melissa Gushiken, Kelly Lo, Dhiraj Holden, Robert C Fahey, Mamta Rawat
Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis.
FEBS Lett: 2012, 586(7);1004-8
[PubMed:22569254]
[WorldCat.org]
[DOI]
(I p)
Derek Parsonage, Gerald L Newton, Robert C Holder, Bret D Wallace, Carleitta Paige, Chris J Hamilton, Patricia C Dos Santos, Matthew R Redinbo, Sean D Reid, Al Claiborne
Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis .
Biochemistry: 2010, 49(38);8398-414
[PubMed:20799687]
[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)
Gerald L Newton, Mamta Rawat, James J La Clair, Vishnu Karthik Jothivasan, Tanya Budiarto, Chris J Hamilton, Al Claiborne, John D Helmann, Robert C Fahey
Bacillithiol is an antioxidant thiol produced in Bacilli.
Nat Chem Biol: 2009, 5(9);625-7
[PubMed:19578333]
[WorldCat.org]
[DOI]
(I p)
