ID A0A811D2K3_9ENTR Unreviewed; 201 AA. AC A0A811D2K3; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. 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 ECO:0000313|EMBL:BCU53818.1}; GN ORFNames=ENKO_04120 {ECO:0000313|EMBL:BCU53818.1}; OS Enterobacter kobei. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=208224 {ECO:0000313|EMBL:BCU53818.1}; RN [1] {ECO:0000313|EMBL:BCU53818.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM 8580 {ECO:0000313|EMBL:BCU53818.1}; RA Maeda T., Shibai A., Kawada K., Kotani H., Tarusawa Y., Tanabe K., RA Furusawa C.; RT "Difference and commonality of drug resistance evolution in various RT bacteria. and drug sensitivity profiles."; RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases. 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; AP024590; BCU53818.1; -; Genomic_DNA. DR RefSeq; WP_072571573.1; NZ_FYBC01000011.1. DR GeneID; 66622919; -. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. 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 43..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 201 AA; 22042 MW; AAD6EA2CC4A1C8CB CRC64; MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA EVTGSGKKPW RQKGTGRARS GSVKSPIWRS GGVTFAARPQ DHSQKVNKKM YRGALKSILS ELVRQDRLIV VEQFSVEAPK TKLLAQKLKD MALEDVLIIT GELDENLFLA ARNLHKVDVR DAAGIDPVSL IAFDKVVMTA DAVKQVEEML A //