RL4_CAMJE
ID RL4_CAMJE Reviewed; 204 AA.
AC Q9PLX2; Q0P7S5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=50S ribosomal protein L4;
GN Name=rplD; OrderedLocusNames=Cj1706c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000305}.
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DR EMBL; AL111168; CAL35800.1; -; Genomic_DNA.
DR PIR; F81268; F81268.
DR RefSeq; WP_002851146.1; NC_002163.1.
DR RefSeq; YP_002345072.1; NC_002163.1.
DR AlphaFoldDB; Q9PLX2; -.
DR SMR; Q9PLX2; -.
DR IntAct; Q9PLX2; 10.
DR STRING; 192222.Cj1706c; -.
DR PaxDb; Q9PLX2; -.
DR PRIDE; Q9PLX2; -.
DR EnsemblBacteria; CAL35800; CAL35800; Cj1706c.
DR GeneID; 905980; -.
DR KEGG; cje:Cj1706c; -.
DR PATRIC; fig|192222.6.peg.1680; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_7; -.
DR OMA; PQVHILE; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR013005; Ribosomal_uL4/L1e.
DR PANTHER; PTHR10746; PTHR10746; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03953; rplD_bact; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..204
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000129198"
FT REGION 49..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 22230 MW; B6CD85C218419429 CRC64;
MSKVVVLNDK LEKAGELDLP SKYAEVNPHN LYLYVKSYLA SLRANTAHTK GRSDVSGGGK
KPWRQKGRGG ARAGSTRTNV WVGGAVAFGP TNERNYFQKV NKKQKRLALE RALADKAAKG
VLFTADSLAI ESGKTKDANA VIKKLGVKDA LIVKDLLDEK TLLAYRNLAN CYVVDVTEVN
AYLVSVFNAV IMEKSVLESI TKEG