MleN

From SubtiWiki
Revision as of 09:28, 2 November 2012 by Fmeyer (talk | contribs) (Biological materials)
Jump to: navigation, search
  • Description: malate-H+/Na+-lactate antiporter

Gene name mleN
Synonyms yqkI
Essential no
Product malate-H+/Na+-lactate antiporter
Function malate uptake
Gene expression levels in SubtiExpress: mleN
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 50 kDa, 7.249
Gene length, protein length 1404 bp, 468 aa
Immediate neighbours mleA, ansB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MleN context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MleN expression.png



















Categories containing this gene/protein

transporters/ other, utilization of specific carbon sources, membrane proteins

This gene is a member of the following regulons

AnsR regulon, CcpA regulon

The gene

Basic information

  • Locus tag: BSU23560

Phenotypes of a mutant

abrupt arrest in the mid-logarithmic phase of growth on malate when low concentrations of protonophore were present PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: nhaC Na(+)/H(+) antiporter family (according to Swiss-Prot)
  • Paralogous protein(s): NhaC

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:GP1460 (mleN::spc), available in Stülke lab
  • Expression vector:
  • lacZ fusion: pGP388 (in pAC7), available in Stülke lab
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Susan H Fisher, Lewis V Wray
Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase.
J. Bacteriol.: 2002, 184(8);2148-54
[PubMed:11914346] [WorldCat.org] [DOI] (P p)

Y Wei, A A Guffanti, M Ito, T A Krulwich
Bacillus subtilis YqkI is a novel malic/Na+-lactate antiporter that enhances growth on malate at low protonmotive force.
J. Biol. Chem.: 2000, 275(39);30287-92
[PubMed:10903309] [WorldCat.org] [DOI] (P p)

D X Sun, P Setlow
Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase.
J. Bacteriol.: 1991, 173(12);3831-45
[PubMed:1711029] [WorldCat.org] [DOI] (P p)