Difference between revisions of "BshA"

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* '''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
YpjH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BshA expression.png















Categories containing this gene/protein

miscellaneous metabolic pathways, resistance against oxidative and electrophile stress

This gene is a member of the following regulons

Spx regulon


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

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • induced by diamide stess (thiol depletion) (Spx) PubMed
  • Regulatory mechanism:
  • 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

  • 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)