YvyD

• Description: general stress protein, required for ribosome dimerization in the stationary phase
  
  

Gene name	yvyD
Synonyms	yviI
Essential	no
Product	unknown
Function	dimerization of ribosomes in the stationary phase
Gene expression levels in SubtiExpress: yvyD
MW, pI	21 kDa, 5.184
Gene length, protein length	567 bp, 189 aa
Immediate neighbours	secA, smiA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

general stress proteins (controlled by SigB), membrane proteins, phosphoproteins

This gene is a member of the following regulons

SigB regulon, SigH regulon

The gene

Basic information

• Locus tag: BSU35310

Phenotypes of a mutant

• the mutant is cold-sensitive
• delayed recovery from stationary phase and delayed germination

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein S30Ae family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-6 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • YvyD-ribosome (for ribosome dimerization) PubMed
• Localization:
  • membrane protein

Database entries

• Structure:

• UniProt: P28368

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: yvyD PubMed

• Expression browser: yvyD PubMed

• Sigma factor: SigB PubMed, SigH PubMed

• Regulation:
  • repressed by casamino acids PubMed
  • induced by stress (SigB) PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

Publications on the homologous E. coli proteins Hpf and YfiA

Yury S Polikanov, Gregor M Blaha, Thomas A Steitz
How hibernation factors RMF, HPF, and YfiA turn off protein synthesis.
Science: 2012, 336(6083);915-8
[PubMed:22605777] [WorldCat.org] [DOI] (I p)