Difference between revisions of "SteT"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU12860&redirect=T BSU12860] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU12860&redirect=T BSU12860] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 13:30, 2 April 2014
- Description: serine/ threonine exchanger transporter
Gene name | steT |
Synonyms | ykbA |
Essential | no |
Product | serine/ threonine exchanger transporter |
Function | exchange of serine and threonine |
Gene expression levels in SubtiExpress: steT | |
MW, pI | 46 kDa, 9.184 |
Gene length, protein length | 1314 bp, 438 aa |
Immediate neighbours | ykaA, mhqA |
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, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU12860
Phenotypes of a mutant
Database entries
- BsubCyc: BSU12860
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: membrane
Database entries
- BsubCyc: BSU12860
- Structure:
- UniProt: O34739
- KEGG entry: [2]
- T.C. number: 2.A.3.8.12
Additional information
Expression and regulation
- Operon: steT
- Regulation: expression activated by glucose (4.2 fold) PubMed
- 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
Paola Bartoccioni, César Del Rio, Merce Ratera, Lukasz Kowalczyk, Jocelyn M Baldwin, Antonio Zorzano, Matthias Quick, Stephen A Baldwin, José Luis Vázquez-Ibar, Manuel Palacín
Role of transmembrane domain 8 in substrate selectivity and translocation of SteT, a member of the L-amino acid transporter (LAT) family.
J Biol Chem: 2010, 285(37);28764-76
[PubMed:20610400]
[WorldCat.org]
[DOI]
(I p)
Christian A Bippes, Antra Zeltina, Fabio Casagrande, Merce Ratera, Manuel Palacin, Daniel J Muller, Dimitrios Fotiadis
Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter.
J Biol Chem: 2009, 284(28);18651-63
[PubMed:19419962]
[WorldCat.org]
[DOI]
(P p)
Núria Reig, César del Rio, Fabio Casagrande, Mercè Ratera, Josep Lluís Gelpí, David Torrents, Peter J F Henderson, Hao Xie, Stephen A Baldwin, Antonio Zorzano, Dimitrios Fotiadis, Manuel Palacín
Functional and structural characterization of the first prokaryotic member of the L-amino acid transporter (LAT) family: a model for APC transporters.
J Biol Chem: 2007, 282(18);13270-81
[PubMed:17344220]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)