Difference between revisions of "YqfG"

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(Database entries)
(References)
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<pubmed> 20807199 </pubmed>
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<pubmed> 20807199, 15965736</pubmed>
  
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:43, 4 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
YqfG context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU25320

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: 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

  • Structure: 1TVI orthologue from T. maritima (38% identity) PubMed
  • 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)