ID A0A1Q6N7D3_9CLOT Unreviewed; 122 AA. AC A0A1Q6N7D3; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 11-DEC-2019, entry version 9. DE RecName: Full=50S ribosomal protein L18 {ECO:0000256|HAMAP-Rule:MF_01337}; GN Name=rplR {ECO:0000256|HAMAP-Rule:MF_01337}; GN ORFNames=BHW11_07815 {ECO:0000313|EMBL:OLA01573.1}; OS Clostridium sp. CAG:62_40_43. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1896990 {ECO:0000313|EMBL:OLA01573.1, ECO:0000313|Proteomes:UP000187212}; RN [1] {ECO:0000313|EMBL:OLA01573.1, ECO:0000313|Proteomes:UP000187212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAG:62_40_43 {ECO:0000313|EMBL:OLA01573.1}; RX PubMed=27819664; DOI=10.1038/nbt.3704; RA Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.; RT "Measurement of bacterial replication rates in microbial communities."; RL Nat. Biotechnol. 34:1256-1263(2016). CC -!- FUNCTION: This is one of the proteins that binds and probably mediates CC the attachment of the 5S RNA into the large ribosomal subunit, where it CC forms part of the central protuberance. {ECO:0000256|HAMAP- CC Rule:MF_01337}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. CC {ECO:0000256|HAMAP-Rule:MF_01337}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family. CC {ECO:0000256|HAMAP-Rule:MF_01337}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OLA01573.1}. 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; MNSA01000012; OLA01573.1; -; Genomic_DNA. DR Proteomes; UP000187212; Unassembled WGS sequence. 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 HAMAP; MF_01337_B; Ribosomal_L18_B; 1. DR InterPro; IPR005484; Ribosomal_L18. DR InterPro; IPR004389; Ribosomal_L18_bac-type. DR PANTHER; PTHR12899; PTHR12899; 1. DR Pfam; PF00861; Ribosomal_L18p; 1. DR TIGRFAMs; TIGR00060; L18_bact; 1. PE 3: Inferred from homology; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01337}; KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01337, KW ECO:0000313|EMBL:OLA01573.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01337}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01337}. FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 122 AA; 13356 MW; 62700FDEDBB92E78 CRC64; MVSKKNRSEV RVNKHRRIRS RLSGTPEQPR LAVFRSNNHM YAQIIDDVAG NTIVSASTVQ ADVKEGLTKT NNTEAAAKLG EVIAKKALDN GIKTVVFDRG GYIYQGKVKA LAEAAREAGL EF //