ID A0A1B4HPZ2_9BURK Unreviewed; 143 AA. AC A0A1B4HPZ2; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-NOV-2016, entry version 2. DE RecName: Full=50S ribosomal protein L11 {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|SAAS:SAAS00635419}; GN Name=rplK {ECO:0000256|HAMAP-Rule:MF_00736}; GN ORFNames=WJ16_01310 {ECO:0000313|EMBL:AOJ30239.1}; OS Burkholderia metallica. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=488729 {ECO:0000313|EMBL:AOJ30239.1}; RN [1] {ECO:0000313|EMBL:AOJ30239.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FL-6-5-30-S1-D7 {ECO:0000313|EMBL:AOJ30239.1}; RA Sahl J., Wagner D., Keim P.; RT "Diversity of Burkholderia near neighbor genomes."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. CC {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|RuleBase:RU003979, CC ECO:0000256|SAAS:SAAS00635423}. 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 CC stalk. L10 forms an elongated spine to which L12 dimers bind in a CC sequential fashion forming a multimeric L10(L12)X complex. CC {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|SAAS:SAAS00635425}. CC -!- PTM: One or more lysine residues are methylated. CC {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|RuleBase:RU003979}. CC -!- SIMILARITY: Belongs to the ribosomal protein L11P family. CC {ECO:0000256|HAMAP-Rule:MF_00736, ECO:0000256|RuleBase:RU003978, CC ECO:0000256|SAAS:SAAS00635430}. 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; CP013401; AOJ30239.1; -; Genomic_DNA. DR RefSeq; WP_006477201.1; NZ_CP013401.1. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. 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; IPR006519; Ribosomal_L11_bac-typ. DR InterPro; IPR020783; Ribosomal_L11_C. 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 {ECO:0000256|HAMAP-Rule:MF_00736, KW ECO:0000256|RuleBase:RU003979}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00736, KW ECO:0000256|RuleBase:RU003978, ECO:0000256|SAAS:SAAS00635422}; KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_00736, KW ECO:0000256|RuleBase:RU003978, ECO:0000256|SAAS:SAAS00635421, KW ECO:0000313|EMBL:AOJ30239.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00736, KW ECO:0000256|RuleBase:RU003979, ECO:0000256|SAAS:SAAS00635426}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00736, KW ECO:0000256|RuleBase:RU003979, ECO:0000256|SAAS:SAAS00635428}. SQ SEQUENCE 143 AA; 14916 MW; 425A7B98E29A08C7 CRC64; MAKKIIGFIK LQIPAGKANP SPPVGPALGQ RGLNIMEFCK AFNAQTQGME PGLPVPVVIT AFADKSFTFV MKTPPATVLI KKAAKVDKGS SKPHTDKVGS ITRAQAEEIA KTKMPDLTAA DLDAAVRTIA GSARSMGITV EGV //