Difference between revisions of "RibU"
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=== Additional information=== | === Additional information=== | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' membrane | + | * '''[[Localization]]:''' membrane |
=== Database entries === | === Database entries === | ||
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' there is a promoter directly in front of ''ribU'' {{PubMed|17693491}} | + | * '''Operon:''' ''[[ribU]]'' {{PubMed|21815947}} |
+ | ** there is a promoter directly in front of ''[[ribU]]'' {{PubMed|17693491}} | ||
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
=Biological materials = | =Biological materials = | ||
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<pubmed> 20497229 </pubmed> | <pubmed> 20497229 </pubmed> | ||
==Original publications== | ==Original publications== | ||
+ | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
+ | <big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> | ||
+ | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
+ | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
<pubmed>12456892, 20972419,17693491, </pubmed> | <pubmed>12456892, 20972419,17693491, </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:50, 19 November 2011
- Description: riboflavin transporter
Gene name | ribU |
Synonyms | ypaA |
Essential | no |
Product | riboflavin transporter |
Function | riboflavin uptake |
Metabolic function and regulation of this protein in SubtiPathways: Riboflavin / FAD | |
MW, pI | 20 kDa, 10.12 |
Gene length, protein length | 570 bp, 190 aa |
Immediate neighbours | fer, ypzE |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
transporters/ other, biosynthesis of cofactors, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU23050
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: membrane
Database entries
- Structure: 3P5N (RibU from Staphylococcus aureus)
- UniProt: P50726
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism: FMN-box: riboswitch, controls access of the ribosome to the Shine-Dalgarno sequence PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Thomas Eitinger, Dmitry A Rodionov, Mathias Grote, Erwin Schneider
Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
FEMS Microbiol Rev: 2011, 35(1);3-67
[PubMed:20497229]
[WorldCat.org]
[DOI]
(I p)
Original publications
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947
Peng Zhang, Jiawei Wang, Yigong Shi
Structure and mechanism of the S component of a bacterial ECF transporter.
Nature: 2010, 468(7324);717-20
[PubMed:20972419]
[WorldCat.org]
[DOI]
(I p)
Christian Vogl, Simon Grill, Oliver Schilling, Jörg Stülke, Matthias Mack, Jürgen Stolz
Characterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum.
J Bacteriol: 2007, 189(20);7367-75
[PubMed:17693491]
[WorldCat.org]
[DOI]
(P p)
Wade C Winkler, Smadar Cohen-Chalamish, Ronald R Breaker
An mRNA structure that controls gene expression by binding FMN.
Proc Natl Acad Sci U S A: 2002, 99(25);15908-13
[PubMed:12456892]
[WorldCat.org]
[DOI]
(P p)