ID RL6_GEOSE Reviewed; 178 AA. AC P02391; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 131. DE RecName: Full=Large ribosomal subunit protein uL6 {ECO:0000255|HAMAP-Rule:MF_01365}; DE AltName: Full=50S ribosomal protein L6 {ECO:0000305}; DE AltName: Full=BL10; GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1985969; DOI=10.1016/s0021-9258(17)35255-9; RA Ramakrishnan V., Gerchman S.E.; RT "Cloning, sequencing, and overexpression of genes for ribosomal proteins RT from Bacillus stearothermophilus."; RL J. Biol. Chem. 266:880-885(1991). RN [2] RP PROTEIN SEQUENCE OF 2-178. RA Kimura M., Rawlings N., Appelt K.; RT "The amino acid sequence of protein BL10 from the 50S subunit of the RT Bacillus stearothermophilus ribosome."; RL FEBS Lett. 136:58-64(1981). RN [3] RP PROTEIN SEQUENCE OF 150-164, AND CROSS-LINKING TO RRNA. RC STRAIN=799; RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x; RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.; RT "Protein-rRNA binding features and their structural and functional RT implications in ribosomes as determined by cross-linking studies."; RL EMBO J. 14:4578-4588(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=8262035; DOI=10.1002/j.1460-2075.1993.tb06184.x; RA Golden B.L., Ramakrishnan V., White S.W.; RT "Ribosomal protein L6: structural evidence of gene duplication from a RT primitive RNA binding protein."; RL EMBO J. 12:4901-4908(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=9642068; DOI=10.1006/jmbi.1998.1780; RA Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., RA White S.W.; RT "Ribosomal proteins S5 and L6: high-resolution crystal structures and roles RT in protein synthesis and antibiotic resistance."; RL J. Mol. Biol. 279:873-888(1998). RN [6] RP 3D-STRUCTURE MODELING ONTO THE H.MARISMORTUI 50S RIBOSOME. RX PubMed=10476961; DOI=10.1038/23641; RA Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.; RT "Placement of protein and RNA structures into a 5 A-resolution map of the RT 50S ribosomal subunit."; RL Nature 400:841-847(1999). CC -!- FUNCTION: It is located near the subunit interface in the base of the CC L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase CC center (By similarity). This protein binds to the 23S rRNA, and is CC important in its secondary structure. {ECO:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family. CC {ECO:0000255|HAMAP-Rule:MF_01365}. 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; M57622; AAA22700.1; ALT_SEQ; Genomic_DNA. DR PIR; A02766; R5BS0F. DR RefSeq; WP_011229634.1; NZ_RCTK01000011.1. DR PDB; 1ML5; EM; 14.00 A; h=2-178. DR PDB; 1RL6; X-ray; 2.00 A; A=2-178. DR PDB; 4V4T; X-ray; 6.46 A; H=2-178. DR PDBsum; 1ML5; -. DR PDBsum; 1RL6; -. DR PDBsum; 4V4T; -. DR AlphaFoldDB; P02391; -. DR SMR; P02391; -. DR IntAct; P02391; 1. DR GeneID; 69835477; -. DR OrthoDB; 9805007at2; -. DR EvolutionaryTrace; P02391; -. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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; 3.90.930.12; Ribosomal protein L6, alpha-beta domain; 2. DR HAMAP; MF_01365_B; Ribosomal_uL6_B; 1. DR InterPro; IPR000702; Ribosomal_uL6-like. DR InterPro; IPR036789; Ribosomal_uL6-like_a/b-dom_sf. DR InterPro; IPR020040; Ribosomal_uL6_a/b-dom. DR InterPro; IPR019906; Ribosomal_uL6_bac-type. DR InterPro; IPR002358; Ribosomal_uL6_CS. DR NCBIfam; TIGR03654; L6_bact; 1. DR PANTHER; PTHR11655:SF14; 54S RIBOSOMAL PROTEIN L6, MITOCHONDRIAL; 1. DR PANTHER; PTHR11655; 60S/50S RIBOSOMAL PROTEIN L6/L9; 1. DR Pfam; PF00347; Ribosomal_L6; 2. DR PIRSF; PIRSF002162; Ribosomal_L6; 1. DR PRINTS; PR00059; RIBOSOMALL6. DR SUPFAM; SSF56053; Ribosomal protein L6; 2. DR PROSITE; PS00525; RIBOSOMAL_L6_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.2" FT CHAIN 2..178 FT /note="Large ribosomal subunit protein uL6" FT /id="PRO_0000131037" FT STRAND 16..20 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 23..28 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 31..36 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:1RL6" FT HELIX 59..80 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 83..91 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 102..111 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 121..127 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:1RL6" FT HELIX 138..149 FT /evidence="ECO:0007829|PDB:1RL6" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:1RL6" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:1RL6" SQ SEQUENCE 178 AA; 19299 MW; C9D83BA8F35DB4FA CRC64; MSRVGKKPIE IPAGVTVTVN GNTVTVKGPK GELTRTFHPD MTITVEGNVI TVTRPSDEKH HRALHGTTRS LLANMVEGVS KGYEKALELV GVGYRASKQG KKLVLSVGYS HPVEIEPEEG LEIEVPSQTK IIVKGADKQR VGELAANIRA VRPPEPYKGK GIRYEGELVR LKEGKTGK //