ID A0A7U4NSG4_MYCPM Unreviewed; 212 AA. AC A0A7U4NSG4; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. DE RecName: Full=50S ribosomal protein L4 {ECO:0000256|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328}; GN ORFNames=F537_00975 {ECO:0000313|EMBL:ALA34277.1}; OS Mycoplasma pneumoniae 85084. OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=1263762 {ECO:0000313|EMBL:ALA34277.1, ECO:0000313|Proteomes:UP000057765}; RN [1] {ECO:0000313|EMBL:ALA34277.1, ECO:0000313|Proteomes:UP000057765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85084 {ECO:0000313|EMBL:ALA34277.1, RC ECO:0000313|Proteomes:UP000057765}; RX PubMed=26275904; DOI=10.1186/s12864-015-1801-0; RA Xiao L., Ptacek T., Osborne J.D., Crabb D.M., Simmons W.L., Lefkowitz E.J., RA Waites K.B., Atkinson T.P., Dybvig K.; RT "Comparative genome analysis of Mycoplasma pneumoniae."; RL BMC Genomics 16:610-610(2015). CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000256|HAMAP-Rule:MF_01328}. 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:0000256|HAMAP-Rule:MF_01328}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP- CC Rule:MF_01328}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family. CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP010544; ALA34277.1; -; Genomic_DNA. DR RefSeq; WP_010874523.1; NZ_CP010544.1. DR SMR; A0A7U4NSG4; -. DR Proteomes; UP000057765; Chromosome. 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_01328}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP- KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}. FT REGION 55..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 161..181 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 212 AA; 23590 MW; 58421C03A2754D0B CRC64; MAKLKLIKID GSFETEPVKL SPGLIAKELK QQPVFDAVLV EQASWRQGTH SILTKGEVRG GGKKPYKQKH TGKARQGSTR NPHFVGGGIV FGPKPNRNYS LKLNKKAHTA ALHTVWSEKL ASDNTHLVDQ NLFNKTEGKT KVMMQFLKSA KLLDKNVLFV VNTLNTNLEQ STSNIKNVQV KHLDKVSVRD LMLANALLVE KEVLKALEGK FK //