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P0AD49 · YFIA_ECOLI

Function

function

During stationary phase prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases (PubMed:16324148).
During environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S ribosome against dissociation, inhibits translation elongation and increases translation accuracy (PubMed:11375931, PubMed:15219834).
When normal growth conditions are restored, is quickly released from the ribosome (PubMed:11375931).
Has been suggested to inhibit translation elongation by blocking the A-site (aminoacyl-tRNA site) (PubMed:11375931).
Has also been suggested to inhibit translation initiation by blocking the A-site and P-site (peptidyl-tRNA site) of the ribosome (PubMed:15502846, PubMed:23420694).
At 15 degrees Celsius binds 30S subunits and stimulates their association with 50S subunits into idle 70S ribosomes (PubMed:23420694).
Crystallization with T.thermophilus 70S ribosomes shows it binds in the channel between the head and body of the 30S subunit, where mRNA, tRNAs, initiation factors IF1 and IF3 and elongation factor G would bind; this protein's extended tail follows the mRNA channel and probably prevents RMF binding, which would prevent ribosome dimerization (PubMed:22605777).
This protein also stabilizes the 30S head relative to the rest of the ribosome, which may also prevent dimerization (PubMed:22605777).
Counteracts miscoding (translation errors) particularly efficiently at magnesium concentrations close to those observed in vivo but less efficiently at higher concentrations (PubMed:15219834).
Counteraction of miscoding was shown to be stronger than inhibition of translation, suggesting that the former activity could be the main function of this protein in vivo (PubMed:15219834).

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentcytosolic small ribosomal subunit
Molecular Functionribosomal small subunit binding
Molecular FunctionrRNA binding
Biological Processdormancy process
Biological Processnegative regulation of translational elongation
Biological Processnegative regulation of translational initiation
Biological Processresponse to cold

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribosome-associated inhibitor A
  • Alternative names
    • Protein Y
      (pY
      )
    • Ribosome associated factor Y
    • Spot Y

Gene names

    • Name
      raiA
    • Synonyms
      yfiA
    • Ordered locus names
      b2597, JW2578

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
    • MRE-600
    • K12 / EMG2
    • K12 / MC4100 / AD202
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AD49
  • Secondary accessions
    • P11285

Proteomes

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Non-essential gene, increased formation of inactive 100S ribosomes in stationary phase, which persist longer than in wild-type. Double hpr-yfiA deletion mutants form 90S ribosomes (PubMed:16324148).
A quadruple yfiA-hpf-rmf-sra knockout strain is significantly outcompeted by wild-type after 4 days growth (PubMed:17277072).
No visible effect on viability or growth rate at 37 or 10 degrees Celsius, slight effect on bulk translation and timing of expression of some cold-shock proteins (PubMed:23420694).

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

Type
IDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001692612-113Ribosome-associated inhibitor A
Modified residue66N6-acetyllysine

Keywords

Proteomic databases

PTM databases

Expression

Induction

During stationary phase (at protein level) (PubMed:11168583, PubMed:11375931).
Also by cold stress, remains ribosome-associated for the 4 hours tested, then disappears when cells are warmed (at protein level) (PubMed:11375931, PubMed:23420694).

Interaction

Subunit

Associates mainly with 70S ribosomes (PubMed:11168583, PubMed:11375931).
Localized at the surface of the 30S ribosomal subunit, at the interface with the 50S subunit (PubMed:10535924, PubMed:15502846, PubMed:22605777).
Binds across the channel in the 30S subunit where tRNAs and mRNA interact during protein biosynthesis (PubMed:15502846, PubMed:22605777).
Can also associate with 100S ribosomes, which are inactive dimers of 70S ribosomes (PubMed:11168583).
Contacts modifed methylated residues of 16S rRNA (in complex with T.thermophilus ribosome, 2/3 residues are also modified in E.coli) (PubMed:25775268).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P0AD49frr P0A8054EBI-1129692, EBI-1114349

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region23-26Interaction with 16S rRNA
Region83-91Interaction with 16S rRNA
Region91-113Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    113
  • Mass (Da)
    12,785
  • Last updated
    2007-01-23 v2
  • MD5 Checksum
    56A38EA72F0BE578BFEF7F17B93BD275
MTMNITSKQMEITPAIRQHVADRLAKLEKWQTHLINPHIILSKEPQGFVADATINTPNGVLVASGKHEDMYTAINELINKLERQLNKLQHKGEARRAATSVKDANFVEEVEEE

Mass Spectrometry

Molecular mass is 12,640 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M10431
EMBL· GenBank· DDBJ
AAA24328.1
EMBL· GenBank· DDBJ
Genomic DNA
Z70523
EMBL· GenBank· DDBJ
CAA94436.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC75646.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA16481.1
EMBL· GenBank· DDBJ
Genomic DNA
M58024
EMBL· GenBank· DDBJ
AAA62782.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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