ID RL11_ALIF1 Reviewed; 142 AA. AC Q5E232; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 02-DEC-2020, entry version 88. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=VF_2419; OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Aliivibrio. OX NCBI_TaxID=312309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with RT pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP- CC Rule:MF_00736}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC Interacts with L10 and the large rRNA to form the base of the stalk. CC L10 forms an elongated spine to which L12 dimers bind in a sequential CC fashion forming a multimeric L10(L12)X complex. {ECO:0000255|HAMAP- CC Rule:MF_00736}. CC -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP- CC Rule:MF_00736}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family. CC {ECO:0000255|HAMAP-Rule:MF_00736}. 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; CP000020; AAW86914.1; -; Genomic_DNA. DR RefSeq; WP_005421326.1; NC_006840.2. DR RefSeq; YP_205802.1; NC_006840.2. DR SMR; Q5E232; -. DR STRING; 312309.VF_2419; -. DR EnsemblBacteria; AAW86914; AAW86914; VF_2419. DR GeneID; 54165133; -. DR KEGG; vfi:VF_2419; -. DR PATRIC; fig|312309.11.peg.2451; -. DR eggNOG; COG0080; Bacteria. DR HOGENOM; CLU_074237_2_0_6; -. DR OMA; CKQFNAK; -. DR OrthoDB; 1702697at2; -. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit 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 CDD; cd00349; Ribosomal_L11; 1. DR Gene3D; 1.10.10.250; -; 1. DR Gene3D; 3.30.1550.10; -; 1. DR HAMAP; MF_00736; Ribosomal_L11; 1. DR InterPro; IPR000911; Ribosomal_L11/L12. DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf. DR InterPro; IPR006519; Ribosomal_L11_bac-typ. DR InterPro; IPR020783; Ribosomal_L11_C. DR InterPro; IPR036769; Ribosomal_L11_C_sf. DR InterPro; IPR020785; Ribosomal_L11_CS. DR InterPro; IPR020784; Ribosomal_L11_N. DR PANTHER; PTHR11661; PTHR11661; 1. DR Pfam; PF00298; Ribosomal_L11; 1. DR Pfam; PF03946; Ribosomal_L11_N; 1. DR SMART; SM00649; RL11; 1. DR SUPFAM; SSF46906; SSF46906; 1. DR SUPFAM; SSF54747; SSF54747; 1. DR TIGRFAMs; TIGR01632; L11_bact; 1. DR PROSITE; PS00359; RIBOSOMAL_L11; 1. PE 3: Inferred from homology; KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding. FT CHAIN 1..142 FT /note="50S ribosomal protein L11" FT /id="PRO_0000258238" SQ SEQUENCE 142 AA; 14787 MW; 0C9EF92D2B76E0A8 CRC64; MAKKVEAYIK LQVAAGMANP SPPVGPALGQ HGVNIMEFCK AFNAKTESIE KGLPIPVVIS VYNDRSFTFV TKTPPAAVLL KKAAGVKSGS GRPNTEKVGT VTDAQLQEIA ETKAADMTGA DIEAMKRSIA GTARSMGLVV EG //