Difference between revisions of "BshA"
Line 121: | Line 121: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
** number of protein molecules per cell (complex medium with amino acids, without glucose): 168 {{PubMed|24696501}} | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 168 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 443 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 291 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 366 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
** ''bshA::mls'' available in [[John_Helmann]] lab | ** ''bshA::mls'' available in [[John_Helmann]] lab |
Revision as of 14:20, 17 April 2014
- 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
- BsubCyc: BSU22460
- 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
- BsubCyc: BSU22460
- UniProt: P42982
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
- number of protein molecules per cell (complex medium with amino acids, without glucose): 168 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 443 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 291 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 366 PubMed
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)