P60723 · RL4_ECOLI

Function

function

One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA (PubMed:3298242).
It is important during the early stages of 50S assembly (PubMed:3298242).
It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (PubMed:6170935, PubMed:7556101).
Protein uL4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which uL4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. uL4 controls the translation of the S10 operon by binding to its mRNA. The regions of uL4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).
Forms part of the polypeptide exit tunnel.
Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.

Miscellaneous

The erythromycin sensitive allele is dominant over the resistant allele.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentcytosolic large ribosomal subunit
Cellular Componentlarge ribosomal subunit
Molecular FunctionDNA binding
Molecular Functionendoribonuclease inhibitor activity
Molecular FunctionmRNA 5'-UTR binding
Molecular FunctionRNA-binding transcription regulator activity
Molecular FunctionrRNA binding
Molecular Functionstructural constituent of ribosome
Molecular Functiontranslation repressor activity
Biological Processcytoplasmic translation
Biological ProcessDNA-templated transcription termination
Biological Processnegative regulation of cytoplasmic translation
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of translation
Biological Processresponse to antibiotic
Biological Processribosome assembly
Biological Processtranscriptional attenuation

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Large ribosomal subunit protein uL4
  • Alternative names
    • 50S ribosomal protein L4

Gene names

    • Name
      rplD
    • Synonyms
      eryA
    • Ordered locus names
      b3319, JW3281

Organism names

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

Accessions

  • Primary accession
    P60723
  • Secondary accessions
    • P02388
    • Q2M6Y4

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis40-88Regulates the S10 operon normally. Assembles into ribosomes in vivo.
Natural variant63in strain: N282; confers erythromycin resistance. Ribosomes bind erythromycin poorly and have reduced peptidyltransferase activity. 50S subunits assemble normally, even in the presence of drug, but assembly is cold-sensitive at 20 degrees Celsius
Mutagenesis67-103Regulates the S10 operon normally. Does not assemble into ribosomes in vivo.
Mutagenesis93-101Regulates the S10 operon normally. Not stably associated with the ribosome in vivo.
Mutagenesis131Does not regulate the S10 operon; assembles into ribosomes in vivo.
Mutagenesis134Does not regulate the S10 operon in vivo.
Mutagenesis160Does not regulate the S10 operon; assembles into ribosomes in vivo.
Mutagenesis167Does not regulate the S10 operon in vivo.
Mutagenesis171-201Loss of S10 operon regulation. Assembles into ribosomes in vivo.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001292151-201Large ribosomal subunit protein uL4

Proteomic databases

Interaction

Subunit

Part of the 50S ribosomal subunit (PubMed:10094780, PubMed:11511371, PubMed:12809609, PubMed:16272117, PubMed:24844575, PubMed:25310980, PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:3298242, PubMed:34403461, PubMed:34504068, PubMed:7556101, Ref.1). In TnaC-stalled ribosomes forms part of the binding pocket for L-Trp with the leader peptide and uL22 (PubMed:34403461, PubMed:34504068).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P60723coaD P0A6I62EBI-545597, EBI-553173
BINARY P60723def P0A6K34EBI-545597, EBI-548913

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region44-71Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    201
  • Mass (Da)
    22,087
  • Last updated
    1986-07-21 v1
  • Checksum
    3A953206B0F083B5
MELVLKDAQSALTVSETTFGRDFNEALVHQVVVAYAAGARQGTRAQKTRAEVTGSGKKPWRQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKVNKKMYRGALKSILSELVRQDRLIVVEKFSVEAPKTKLLAQKLKDMALEDVLIITGELDENLFLAARNLHKVDVRDATGIDPVSLIAFDKVVMTADAVKQVEEMLA

Mass Spectrometry

Molecular mass is 22,086.2 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X02613
EMBL· GenBank· DDBJ
CAA26461.1
EMBL· GenBank· DDBJ
Genomic DNA
U18997
EMBL· GenBank· DDBJ
AAA58116.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76344.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77972.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp