Difference between revisions of "YqfG"
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=The protein= | =The protein= | ||
Revision as of 23:02, 30 November 2010
- Description: required for rRNA maturation
Gene name | yqfG |
Synonyms | |
Essential | no |
Product | unknown |
Function | rRNA maturation |
MW, pI | 17 kDa, 4.193 |
Gene length, protein length | 471 bp, 157 aa |
Immediate neighbours | dgkA, yqfF |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU25320
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
Categories containing this gene/protein
translation, membrane proteins
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: UPF0054 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- UniProt: P46347
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
This protein family is highly conserved in bacteria. In E. coli, its orthologe YbeY is involved in maturation of rRNA. PubMed
References
Bryan W Davies, Caroline Köhrer, Asha I Jacob, Lyle A Simmons, Jianyu Zhu, Lourdes M Aleman, Uttam L Rajbhandary, Graham C Walker
Role of Escherichia coli YbeY, a highly conserved protein, in rRNA processing.
Mol Microbiol: 2010, 78(2);506-18
[PubMed:20807199]
[WorldCat.org]
[DOI]
(I p)
Catherine Hervé du Penhoat, Zhaohui Li, Hanudatta S Atreya, Seho Kim, Adelinda Yee, Rong Xiao, Diana Murray, Cheryl H Arrowsmith, Thomas Szyperski
NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure.
J Struct Funct Genomics: 2005, 6(1);51-62
[PubMed:15965736]
[WorldCat.org]
[DOI]
(P p)