Difference between revisions of "MrpA"

From SubtiWiki
Jump to: navigation, search
Line 60: Line 60:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU31600&redirect=T BSU31600]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mrpABCDEFG.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mrpABCDEFG.html]
Line 96: Line 97:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU31600&redirect=T BSU31600]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 14:38, 2 April 2014

  • Description: Na+ transporter subunit of the Na+/H+ antiporter, multiple resistance and pH homeostasis

Gene name mrpA
Synonyms yufT, shaA, ntrA
Essential yes PubMed
Product Na+/H+ antiporter subunit
Function sodium export
Gene expression levels in SubtiExpress: mrpA
Interactions involving this protein in SubtInteract: MrpA
MW, pI 86 kDa, 9.519
Gene length, protein length 2322 bp, 774 aa
Immediate neighbours yufS, mrpB
Sequences Protein DNA DNA_with_flanks
Genetic context
MrpA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MrpA expression.png















Categories containing this gene/protein

transporters/ other, metal ion homeostasis (K, Na, Ca, Mg), essential genes, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU31600

Phenotypes of a mutant

  • essential PubMed
  • a mrpA mutant is viable at pH7.4 and sodium concentrations below 80 mM PubMed
  • the mrpA mutant accumulates internal sodium PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Na+ transporter subunit of the Na+/H+ antiporter PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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

References

Kamil Górecki, Cecilia Hägerhäll, Torbjörn Drakenberg
The Na+ transport in gram-positive bacteria defect in the Mrp antiporter complex measured with 23Na nuclear magnetic resonance.
Anal Biochem: 2014, 445;80-6
[PubMed:24139955] [WorldCat.org] [DOI] (I p)

Vamsi K Moparthi, Brijesh Kumar, Yusra Al-Eryani, Eva Sperling, Kamil Górecki, Torbjörn Drakenberg, Cecilia Hägerhäll
Functional role of the MrpA- and MrpD-homologous protein subunits in enzyme complexes evolutionary related to respiratory chain complex I.
Biochim Biophys Acta: 2014, 1837(1);178-85
[PubMed:24095649] [WorldCat.org] [DOI] (P p)

Egle Virzintiene, Vamsi K Moparthi, Yusra Al-Eryani, Leonard Shumbe, Kamil Górecki, Cecilia Hägerhäll
Structure and function of the C-terminal domain of MrpA in the Bacillus subtilis Mrp-antiporter complex--the evolutionary progenitor of the long horizontal helix in complex I.
FEBS Lett: 2013, 587(20);3341-7
[PubMed:24021651] [WorldCat.org] [DOI] (I p)

Vamsi K Moparthi, Brijesh Kumar, Cecilie Mathiesen, Cecilia Hägerhäll
Homologous protein subunits from Escherichia coli NADH:quinone oxidoreductase can functionally replace MrpA and MrpD in Bacillus subtilis.
Biochim Biophys Acta: 2011, 1807(4);427-36
[PubMed:21236240] [WorldCat.org] [DOI] (P p)

Yusuke Kajiyama, Masato Otagiri, Junichi Sekiguchi, Toshiaki Kudo, Saori Kosono
The MrpA, MrpB and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues.
Microbiology (Reading): 2009, 155(Pt 7);2137-2147
[PubMed:19389778] [WorldCat.org] [DOI] (P p)

Yusuke Kajiyama, Masato Otagiri, Junichi Sekiguchi, Saori Kosono, Toshiaki Kudo
Complex formation by the mrpABCDEFG gene products, which constitute a principal Na+/H+ antiporter in Bacillus subtilis.
J Bacteriol: 2007, 189(20);7511-4
[PubMed:17693497] [WorldCat.org] [DOI] (P p)

Saori Kosono, Yusuke Kajiyama, Shin Kawasaki, Toko Yoshinaka, Koki Haga, Toshiaki Kudo
Functional involvement of membrane-embedded and conserved acidic residues in the ShaA subunit of the multigene-encoded Na+/H+ antiporter in Bacillus subtilis.
Biochim Biophys Acta: 2006, 1758(5);627-35
[PubMed:16730649] [WorldCat.org] [DOI] (P p)

Saori Kosono, Kei Asai, Yoshito Sadaie, Toshiaki Kudo
Altered gene expression in the transition phase by disruption of a Na+/H+ antiporter gene (shaA) in Bacillus subtilis.
FEMS Microbiol Lett: 2004, 232(1);93-9
[PubMed:15019740] [WorldCat.org] [DOI] (P p)

M Ito, A A Guffanti, W Wang, T A Krulwich
Effects of nonpolar mutations in each of the seven Bacillus subtilis mrp genes suggest complex interactions among the gene products in support of Na(+) and alkali but not cholate resistance.
J Bacteriol: 2000, 182(20);5663-70
[PubMed:11004162] [WorldCat.org] [DOI] (P p)

M Ito, A A Guffanti, B Oudega, T A Krulwich
mrp, a multigene, multifunctional locus in Bacillus subtilis with roles in resistance to cholate and to Na+ and in pH homeostasis.
J Bacteriol: 1999, 181(8);2394-402
[PubMed:10198001] [WorldCat.org] [DOI] (P p)