MleN
- 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 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
transporters/ other, utilization of specific carbon sources, membrane proteins
This gene is a member of the following regulons
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:
- Localization:
- membrane associated PubMed
Database entries
- Structure:
- UniProt: P54571
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- 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)
