ID A0A7U9CU50_KLEPN Unreviewed; 201 AA. AC A0A7U9CU50; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-AUG-2022, entry version 5. DE RecName: Full=50S ribosomal protein L4 {ECO:0000256|ARBA:ARBA00019302, ECO:0000256|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328}; GN ORFNames=B819_28528 {ECO:0000313|EMBL:EKF76906.1}; OS Klebsiella pneumoniae subsp. pneumoniae KpQ3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=1226115 {ECO:0000313|EMBL:EKF76906.1, ECO:0000313|Proteomes:UP000011948}; RN [1] {ECO:0000313|Proteomes:UP000011948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KpQ3 {ECO:0000313|Proteomes:UP000011948}; RX PubMed=23469341; RA Tobes R., Codoner F.M., Lopez-Camacho E., Salanueva I.J., Manrique M., RA Brozynska M., Gomez-Gil R., Martinez-Blanch J.F., Alvarez-Tejado M., RA Pareja E., Mingorance J.; RT "Genome Sequence of Klebsiella pneumoniae KpQ3, a DHA-1 beta-Lactamase- RT Producing Nosocomial Isolate."; RL Genome Announc. 1:E00167-E00112(2013). 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; JH930400; EKF76906.1; -; Genomic_DNA. DR RefSeq; WP_002919794.1; NZ_JH930400.1. DR SMR; A0A7U9CU50; -. DR GeneID; 64293226; -. DR Proteomes; UP000011948; Unassembled WGS sequence. 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 {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 46..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 201 AA; 22114 MW; 6B7A32185AB6A49C CRC64; MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA EITGSGKKPW RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM YRGALKSILS ELVRQDRLIV VEKFSVEAPK TKLLAQKLKD MALEDVLIIT GELDENLFLA ARNLHKVDVR DANGIDPVSL IAFDKVVMTA DAVKQVEEML A //