GltT

• Description: major H+/Na+-glutamate symport protein
  
  

Gene name	gltT
Synonyms	yhfG
Essential	no
Product	major H+/Na+-glutamate symport protein
Function	glutamate and aspartate uptake
Gene expression levels in SubtiExpress: gltT
Metabolic function and regulation of this protein in SubtiPathways: gltT
MW, pI	45 kDa, 9.029
Gene length, protein length	1287 bp, 429 aa
Immediate neighbours	yhfF, yhfH
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transporters/ other, biosynthesis/ acquisition of amino acids, glutamate metabolism, utilization of amino acids, membrane proteins

The gene

Basic information

• Locus tag: BSU10220

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: View classification (according to Swiss-Prot)

• Paralogous protein(s): GltP, DctP

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization: cell membrane PubMed

Database entries

• Structure:
  • 4IZM (the protein from Pyrococcus horikoshii, 35% identity, 73% similarity) PubMed
  • 4KY0 (the glutamate transporter of Thermococcus kodakarensis, 35% identity, 72% similarity) PubMed

• UniProt: O07605

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: gltT PubMed

• Expression browser: gltT PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Sonja Jensen, Albert Guskov, Stephan Rempel, Inga Hänelt, Dirk Jan Slotboom
Crystal structure of a substrate-free aspartate transporter.
Nat Struct Mol Biol: 2013, 20(10);1224-6
[PubMed:24013209] [WorldCat.org] [DOI] (I p)

Nicolas Reyes, SeCheol Oh, Olga Boudker
Binding thermodynamics of a glutamate transporter homolog.
Nat Struct Mol Biol: 2013, 20(5);634-40
[PubMed:23563139] [WorldCat.org] [DOI] (I p)

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)