P0ADY3 · RL14_ECOLI

Function

function

This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609).
Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117).
Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentcytosolic large ribosomal subunit
Molecular Functionlarge ribosomal subunit rRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processcytoplasmic translation

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Large ribosomal subunit protein uL14
  • Alternative names
    • 50S ribosomal protein L14

Gene names

    • Name
      rplN
    • Ordered locus names
      b3310, JW3272

Organism names

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

Accessions

  • Primary accession
    P0ADY3
  • Secondary accessions
    • P02411
    • Q2M6X5

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis97Reduced RsfS binding.
Mutagenesis98Reduced RsfS binding.
Mutagenesis114Reduced RsfS binding.
Mutagenesis117No change in RsfS binding.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001285401-123Large ribosomal subunit protein uL14

Proteomic databases

Interaction

Subunit

Part of the 50S ribosomal subunit (PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:24844575, PubMed:25310980, PubMed:2665813, PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:352727, PubMed:7556101).
Contacts L19 (PubMed:16272117, PubMed:2665813).
Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the universal ribosomal protein uL14 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    123
  • Mass (Da)
    13,541
  • Last updated
    1988-04-01 v1
  • Checksum
    192ACB1623979510
MIQEQTMLNVADNSGARRVMCIKVLGGSHRRYAGVGDIIKITIKEAIPRGKVKKGDVLKAVVVRTKKGVRRPDGSVIRFDGNACVLLNNNSEQPIGTRIFGPVTRELRSEKFMKIISLAPEVL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict63in Ref. 1; AA sequence
Sequence conflict84in Ref. 1; AA sequence
Sequence conflict90-91in Ref. 1; AA sequence
Sequence conflict97in Ref. 1; AA sequence
Sequence conflict115in Ref. 1; AA sequence
Sequence conflict123in Ref. 1; AA sequence

Mass Spectrometry

Molecular mass is 13,540.2 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X01563
EMBL· GenBank· DDBJ
CAA25715.1
EMBL· GenBank· DDBJ
Genomic DNA
U18997
EMBL· GenBank· DDBJ
AAA58107.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76335.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77981.1
EMBL· GenBank· DDBJ
Genomic DNA
V00357
EMBL· GenBank· DDBJ
CAA23653.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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