YqfG

• 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

Categories containing this gene/protein

translation, membrane proteins

The gene

Basic information

• Locus tag: BSU25320

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• UniProt: P46347

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Your additional remarks

This protein family is highly conserved in bacteria. In E. coli, its orthologe YbeY is involved in maturation of rRNA. PubMed In S. meliloti, the protein affects sRNA regulation in a similar way as Hfq 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)