Difference between revisions of "GltT"
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=== Additional information=== | === Additional information=== | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' [http://www.pdb.org/pdb/explore/remediatedSequence.do?structureId=4IZM 4IZM] (the protein from ''Pyrococcus horikoshii'', 35% identity, 73% similarity) {{PubMed|23563139}} | + | * '''Structure:''' |
| + | ** [http://www.pdb.org/pdb/explore/remediatedSequence.do?structureId=4IZM 4IZM] (the protein from ''Pyrococcus horikoshii'', 35% identity, 73% similarity) {{PubMed|23563139}} | ||
| + | ** [http://pdb.org/pdb/explore/explore.do?structureId=4KY0 4KY0] (the glutamate transporter of ''Thermococcus kodakarensis'', 35% identity, 72% similarity) {{PubMed|24013209}} | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/O07605 O07605] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O07605 O07605] | ||
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=References= | =References= | ||
| − | <pubmed>18763711, 23563139 22383849</pubmed> | + | <pubmed>18763711, 23563139 22383849 24013209</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:05, 27 December 2013
- 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: Ammonium/ glutamate | |
| 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
| |
Contents
Categories containing this gene/protein
transporters/ other, biosynthesis/ acquisition of amino acids, glutamate metabolism, utilization of amino acids, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU10220
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: View classification (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cell membrane PubMed
Database entries
- Structure:
- UniProt: O07605
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon: gltT PubMed
- 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
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)
