ID   RL4_MESH2               Reviewed;         214 AA.
AC   Q601L4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=mhp188;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27445.1; -; Genomic_DNA.
DR   RefSeq; WP_011206025.1; NC_006360.1.
DR   AlphaFoldDB; Q601L4; -.
DR   SMR; Q601L4; -.
DR   STRING; 295358.mhp188; -.
DR   EnsemblBacteria; AAV27445; AAV27445; mhp188.
DR   KEGG; mhy:mhp188; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_2_1_14; -.
DR   OMA; PQVHILE; -.
DR   PhylomeDB; Q601L4; -.
DR   Proteomes; UP000006822; 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..214
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242396"
FT   REGION          56..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  24055 MW;  FAC3699AFF73D87F CRC64;
     MNKISEISIQ SQKTENLVKF NANDDLPKSL FEQKEPHFQA IFDSILSERA SKRLSTHKVK
     NRAEVSGTGK KPWKQKSTGK ARAGSKRSPI FVGGGRAFGP TTQRNYNLKV NKKVKKLAFI
     SALSQLAQNQ QILVNDFSMN KISTKLLVDQ LKIFKIDQLR HILIASSDPN LFLSARNLPN
     VELVKTNSLT VESLIKADLL IISKNEITNL EKRI