Difference between revisions of "ThiU"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13240&redirect=T BSU13240] | ||
* '''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=BSU13240&redirect=T BSU13240] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1SBR 1SBR] (complex with thiamine), [http://www.rcsb.org/pdb/explore.do?structureId=1S99 1S99] | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1SBR 1SBR] (complex with thiamine), [http://www.rcsb.org/pdb/explore.do?structureId=1S99 1S99] | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 257 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 745 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1463 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 433 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 540 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
Latest revision as of 14:18, 17 April 2014
- Description: thiamine ABC transporter (binding protein)
Gene name | thiU |
Synonyms | ykoF |
Essential | no |
Product | thiamine ABC transporter (binding protein) |
Function | thiamine uptake |
Gene expression levels in SubtiExpress: thiU | |
Interactions involving this protein in SubtInteract: ThiU | |
Metabolic function and regulation of this protein in SubtiPathways: thiU | |
MW, pI | 21 kDa, 6.046 |
Gene length, protein length | 600 bp, 200 aa |
Immediate neighbours | thiV, ykoG |
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
ABC transporters, biosynthesis of cofactors, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13240
Phenotypes of a mutant
Database entries
- BsubCyc: BSU13240
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: membrane associated (via ThiV-ThiX) PubMed
Database entries
- BsubCyc: BSU13240
- UniProt: O34911
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 257 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 745 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1463 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 433 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 540 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Ghislain Schyns, Sébastien Potot, Yi Geng, Teresa M Barbosa, Adriano Henriques, John B Perkins
Isolation and characterization of new thiamine-deregulated mutants of Bacillus subtilis.
J Bacteriol: 2005, 187(23);8127-36
[PubMed:16291685]
[WorldCat.org]
[DOI]
(P p)
Yancho Devedjiev, Yogesh Surendranath, Urszula Derewenda, Alexandra Gabrys, David R Cooper, Rong-guang Zhang, Lour Lezondra, Andrzej Joachimiak, Zygmunt S Derewenda
The structure and ligand binding properties of the B. subtilis YkoF gene product, a member of a novel family of thiamin/HMP-binding proteins.
J Mol Biol: 2004, 343(2);395-406
[PubMed:15451668]
[WorldCat.org]
[DOI]
(P p)
Dmitry A Rodionov, Alexey G Vitreschak, Andrey A Mironov, Mikhail S Gelfand
Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms.
J Biol Chem: 2002, 277(50);48949-59
[PubMed:12376536]
[WorldCat.org]
[DOI]
(P p)