ID RL14_THET2 Reviewed; 122 AA. AC Q72I14; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Large ribosomal subunit protein uL14 {ECO:0000255|HAMAP-Rule:MF_01367}; DE AltName: Full=50S ribosomal protein L14 {ECO:0000305}; GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=TT_C1318; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in CC the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and CC together make contacts with the 16S rRNA in bridges B5 and B8. CC {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family. CC {ECO:0000255|HAMAP-Rule:MF_01367}. 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; AE017221; AAS81660.1; -; Genomic_DNA. DR RefSeq; WP_003043914.1; NZ_CP133179.1. DR PDB; 4V4I; X-ray; 3.71 A; I=1-122. DR PDB; 4V4J; X-ray; 3.83 A; I=1-122. DR PDB; 4V63; X-ray; 3.21 A; BO/DO=1-122. DR PDB; 4V67; X-ray; 3.00 A; BO/DO=1-122. DR PDB; 4V7P; X-ray; 3.62 A; BK/CK=1-122. DR PDB; 4V83; X-ray; 3.50 A; BK/DK=1-122. DR PDB; 4V84; X-ray; 3.40 A; BK/DK=1-122. DR PDB; 4V9J; X-ray; 3.86 A; BO/DO=1-122. DR PDB; 4V9K; X-ray; 3.50 A; BO/DO=1-122. DR PDB; 4V9L; X-ray; 3.50 A; BO/DO=1-122. DR PDB; 4V9M; X-ray; 4.00 A; BO/DO=1-122. DR PDB; 4V9N; X-ray; 3.40 A; BO/DO=1-122. DR PDB; 4V9Q; X-ray; 3.40 A; AK/CK=1-122. DR PDB; 4W29; X-ray; 3.80 A; BO/DO=1-122. DR PDB; 4XEJ; X-ray; 3.80 A; AL14/BL14=1-122. DR PDB; 5J4D; X-ray; 3.10 A; L/QB=1-122. DR PDB; 5V8I; X-ray; 3.25 A; 1O/2O=1-122. DR PDB; 6B4V; X-ray; 3.40 A; L/PB=1-122. DR PDB; 6BOH; X-ray; 3.40 A; L/QB=1-122. DR PDB; 6BOK; X-ray; 3.55 A; L/OB=1-122. DR PDB; 6N1D; X-ray; 3.20 A; AL14/BL14=1-122. DR PDBsum; 4V4I; -. DR PDBsum; 4V4J; -. DR PDBsum; 4V63; -. DR PDBsum; 4V67; -. DR PDBsum; 4V7P; -. DR PDBsum; 4V83; -. DR PDBsum; 4V84; -. DR PDBsum; 4V9J; -. DR PDBsum; 4V9K; -. DR PDBsum; 4V9L; -. DR PDBsum; 4V9M; -. DR PDBsum; 4V9N; -. DR PDBsum; 4V9Q; -. DR PDBsum; 4W29; -. DR PDBsum; 4XEJ; -. DR PDBsum; 5J4D; -. DR PDBsum; 5V8I; -. DR PDBsum; 6B4V; -. DR PDBsum; 6BOH; -. DR PDBsum; 6BOK; -. DR PDBsum; 6N1D; -. DR AlphaFoldDB; Q72I14; -. DR SMR; Q72I14; -. DR IntAct; Q72I14; 4. DR KEGG; tth:TT_C1318; -. DR eggNOG; COG0093; Bacteria. DR HOGENOM; CLU_095071_2_1_0; -. DR OrthoDB; 9806379at2; -. DR EvolutionaryTrace; Q72I14; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. 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; 2.40.150.20; Ribosomal protein L14; 1. DR HAMAP; MF_01367; Ribosomal_uL14; 1. DR InterPro; IPR000218; Ribosomal_uL14. DR InterPro; IPR005745; Ribosomal_uL14_bac-type. DR InterPro; IPR019972; Ribosomal_uL14_CS. DR InterPro; IPR036853; Ribosomal_uL14_sf. DR NCBIfam; TIGR01067; rplN_bact; 1. DR PANTHER; PTHR11761; 50S/60S RIBOSOMAL PROTEIN L14/L23; 1. DR PANTHER; PTHR11761:SF3; 54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL; 1. DR Pfam; PF00238; Ribosomal_L14; 1. DR SMART; SM01374; Ribosomal_L14; 1. DR SUPFAM; SSF50193; Ribosomal protein L14; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT CHAIN 1..122 FT /note="Large ribosomal subunit protein uL14" FT /id="PRO_0000266574" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 15..24 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 38..46 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:4V9K" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:4V9L" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:4V9L" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:4V84" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:4V9K" FT HELIX 105..109 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 112..117 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:4V9K" SQ SEQUENCE 122 AA; 13289 MW; 7C1AB92EBABC9001 CRC64; MIQPQTYLEV ADNTGARKIM CIRVLKGSNA KYATVGDVIV ASVKEAIPRG AVKEGDVVKA VVVRTKKEVK RPDGSAIRFD DNAAVIINNQ LEPRGTRVFG PVARELREKG FMKIVSLAPE VL //