ID   RL4_MYCCT               Reviewed;         208 AA.
AC   P10135; Q2SRF4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=MCAP_0695;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3481422; DOI=10.1007/bf00325700;
RA   Ohkubo S., Muto A., Kawauchi Y., Yamao F., Osawa S.;
RT   "The ribosomal protein gene cluster of Mycoplasma capricolum.";
RL   Mol. Gen. Genet. 210:314-322(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01328}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR   EMBL; X06414; CAA29705.1; -; Genomic_DNA.
DR   EMBL; CP000123; ABC01153.1; -; Genomic_DNA.
DR   PIR; S02832; R5YM4C.
DR   RefSeq; WP_011387543.1; NC_007633.1.
DR   AlphaFoldDB; P10135; -.
DR   SMR; P10135; -.
DR   EnsemblBacteria; ABC01153; ABC01153; MCAP_0695.
DR   GeneID; 23778351; -.
DR   KEGG; mcp:MCAP_0695; -.
DR   HOGENOM; CLU_041575_5_2_14; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
DR   PhylomeDB; P10135; -.
DR   Proteomes; UP000001928; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..208
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000129237"
FT   REGION          50..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        71
FT                   /note="R -> L (in Ref. 1; CAA29705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="G -> E (in Ref. 1; CAA29705)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  23080 MW;  521DBC03B01CB723 CRC64;
     MKLQVLDTKG NEIKEIALND YVWGIEPHQQ AIYDTVISQQ AALRQGTKKV KTRAEVSGGG
     RKPWKQKGTG RARQGSIRAP QWKGGGVTFG PTPDINYKKS VNKKVRALAF RSVLSLKVKE
     NNLVIVDKFD FAKPSTKEMV VVMKNLKIDD QKTLIVTKEK EELVVKSSNN ITGVKTISAN
     QLNVFDLLNA TKLLITEEAA IAVEEVYA