ID RL1_THET8 Reviewed; 229 AA. AC Q5SLP7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 138. DE RecName: Full=Large ribosomal subunit protein uL1 {ECO:0000305}; DE AltName: Full=50S ribosomal protein L1; GN Name=rplA; OrderedLocusNames=TTHA0246; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-26. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=11154066; DOI=10.1515/bc.2000.133; RA Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., RA Choli-Papadopoulou T.; RT "Identification of the 50S ribosomal proteins from the eubacterium Thermus RT thermophilus."; RL Biol. Chem. 381:1079-1087(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-181. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=1447157; DOI=10.1128/jb.174.23.7859-7863.1992; RA Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.; RT "Identification of the gene encoding transcription factor NusG of Thermus RT thermophilus."; RL J. Bacteriol. 174:7859-7863(1992). RN [4] RP MASS SPECTROMETRY. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=16287167; DOI=10.1002/pmic.200402111; RA Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.; RT "Extending ribosomal protein identifications to unsequenced bacterial RT strains using matrix-assisted laser desorption/ionization mass RT spectrometry."; RL Proteomics 5:4818-4831(2005). RN [5] RP X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME. RX PubMed=11511350; DOI=10.1016/s0092-8674(01)00435-4; RA Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.; RT "The path of messenger RNA through the ribosome."; RL Cell 106:233-241(2001). RN [6] RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME. RX PubMed=11283358; DOI=10.1126/science.1060089; RA Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., RA Cate J.H.D., Noller H.F.; RT "Crystal structure of the ribosome at 5.5 A resolution."; RL Science 292:883-896(2001). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH RF2, RP AND SUBUNIT. RX PubMed=18988853; DOI=10.1126/science.1164840; RA Weixlbaumer A., Jin H., Neubauer C., Voorhees R.M., Petry S., Kelley A.C., RA Ramakrishnan V.; RT "Insights into translational termination from the structure of RF2 bound to RT the ribosome."; RL Science 322:953-956(2008). RN [8] RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH RF2, RP AND SUBUNIT. RX PubMed=20421507; DOI=10.1073/pnas.1003995107; RA Jin H., Kelley A.C., Loakes D., Ramakrishnan V.; RT "Structure of the 70S ribosome bound to release factor 2 and a substrate RT analog provides insights into catalysis of peptide release."; RL Proc. Natl. Acad. Sci. U.S.A. 107:8593-8598(2010). CC -!- FUNCTION: Directly binds to 23S rRNA. Forms what is known as the L1 CC stalk, which protrudes beyond the 70S ribosome surface. The stalk is CC preferentially stabilized in 70S versus 50S crystals. Interacts with CC the E site tRNA, blocking the exit path. This blockage implies that CC this section of the ribosome must be able to move to release the CC deacetylated tRNA. CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it CC controls the translation of the L11 operon by binding to its mRNA. CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- MASS SPECTROMETRY: Mass=24698; Method=MALDI; CC Evidence={ECO:0000269|PubMed:16287167}; CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family. CC {ECO:0000305}. 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; AP008226; BAD70069.1; -; Genomic_DNA. DR RefSeq; WP_011227804.1; NC_006461.1. DR RefSeq; YP_143512.1; NC_006461.1. DR PDB; 1ML5; EM; 14.00 A; c=2-229. DR PDB; 2OM7; EM; 7.30 A; K=1-229. DR PDB; 3TG8; X-ray; 1.95 A; A=1-229. DR PDB; 4V42; X-ray; 5.50 A; BC=2-229. DR PDB; 4V4P; X-ray; 5.50 A; AC=2-229. DR PDB; 4V4X; X-ray; 5.00 A; BC=1-229. DR PDB; 4V4Y; X-ray; 5.50 A; BC=1-229. DR PDB; 4V4Z; X-ray; 4.51 A; BC=1-229. DR PDB; 4V51; X-ray; 2.80 A; BC/DC=2-229. DR PDB; 4V5A; X-ray; 3.50 A; BC/DC=2-229. DR PDB; 4V5C; X-ray; 3.30 A; BC/DC=1-229. DR PDB; 4V5D; X-ray; 3.50 A; BC/DC=1-229. DR PDB; 4V5E; X-ray; 3.45 A; BC/DC=1-229. DR PDB; 4V5F; X-ray; 3.60 A; BC/DC=1-229. DR PDB; 4V5G; X-ray; 3.60 A; BC/DC=1-229. DR PDB; 4V5J; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V5K; X-ray; 3.20 A; BC/DC=1-229. DR PDB; 4V5L; X-ray; 3.10 A; BC=1-229. DR PDB; 4V5M; EM; 7.80 A; BC=1-229. DR PDB; 4V5N; EM; 7.60 A; BC=1-229. DR PDB; 4V5P; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V5Q; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V5R; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V5S; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V68; EM; 6.40 A; BC=19-225. DR PDB; 4V6A; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V7J; X-ray; 3.30 A; AC/BC=1-229. DR PDB; 4V7K; X-ray; 3.60 A; AC/BC=1-229. DR PDB; 4V7L; X-ray; 3.00 A; BC/DC=1-229. DR PDB; 4V7M; X-ray; 3.45 A; BC/DC=1-229. DR PDB; 4V8J; X-ray; 3.90 A; BC/DC=1-229. DR PDB; 4V8N; X-ray; 3.10 A; BC/DC=1-229. DR PDB; 4V8O; X-ray; 3.80 A; BC=1-229. DR PDB; 4V8Q; X-ray; 3.10 A; AC=1-229. DR PDB; 4V8U; X-ray; 3.70 A; BC/DC=1-229. DR PDB; 4V8X; X-ray; 3.35 A; BC/DC=1-229. DR PDB; 4V90; X-ray; 2.95 A; BC=2-229. DR PDB; 4V97; X-ray; 3.52 A; BC/DC=1-229. DR PDB; 4V9H; X-ray; 2.86 A; BC=1-229. DR PDB; 4WF1; X-ray; 3.09 A; B5=19-225. DR PDB; 4WPO; X-ray; 2.80 A; AC/CC=2-229. DR PDB; 4WQF; X-ray; 2.80 A; AC/CC=2-229. DR PDB; 4WQU; X-ray; 2.80 A; AC/CC=2-229. DR PDB; 4WQY; X-ray; 2.80 A; AC/CC=2-229. DR PDB; 4WT8; X-ray; 3.40 A; CA/DA=19-111. DR PDB; 4WU1; X-ray; 3.20 A; 71/79=1-229. DR PDB; 4WZD; X-ray; 3.10 A; 71/79=1-229. DR PDB; 4WZO; X-ray; 3.30 A; 71=1-229. DR PDB; 5A9Z; EM; 4.70 A; AC=2-229. DR PDB; 5AA0; EM; 5.00 A; AC=2-229. DR PDB; 5E7K; X-ray; 3.20 A; 71/79=1-229. DR PDB; 5E81; X-ray; 2.95 A; 71/79=1-229. DR PDB; 5EL4; X-ray; 3.15 A; 71=1-229. DR PDB; 5EL5; X-ray; 3.15 A; 71=1-229. DR PDB; 5EL6; X-ray; 3.10 A; 71/79=1-229. DR PDB; 5EL7; X-ray; 3.15 A; 71/79=1-229. DR PDB; 5HAU; X-ray; 3.00 A; 1C/2C=1-229. DR PDB; 5NPM; X-ray; 2.70 A; A=10-229. DR PDB; 5OT7; EM; 3.80 A; f=3-229. DR PDB; 5UQ7; EM; 3.50 A; C=3-229. DR PDB; 5UQ8; EM; 3.20 A; C=3-229. DR PDB; 5ZLU; EM; 3.60 A; Y=1-229. DR PDB; 6C5L; X-ray; 3.20 A; BC/DC=1-229. DR PDB; 6GSL; X-ray; 3.16 A; 71/79=1-229. DR PDB; 6Q95; EM; 3.70 A; A=1-229. DR PDB; 6QNQ; X-ray; 3.50 A; 71=1-229. DR PDB; 6QNR; X-ray; 3.10 A; 71/79=1-229. DR PDB; 7LH5; X-ray; 3.27 A; BC/DC=1-229. DR PDBsum; 1ML5; -. DR PDBsum; 2OM7; -. DR PDBsum; 3TG8; -. DR PDBsum; 4V42; -. DR PDBsum; 4V4P; -. DR PDBsum; 4V4X; -. DR PDBsum; 4V4Y; -. DR PDBsum; 4V4Z; -. DR PDBsum; 4V51; -. DR PDBsum; 4V5A; -. DR PDBsum; 4V5C; -. DR PDBsum; 4V5D; -. DR PDBsum; 4V5E; -. DR PDBsum; 4V5F; -. DR PDBsum; 4V5G; -. DR PDBsum; 4V5J; -. DR PDBsum; 4V5K; -. DR PDBsum; 4V5L; -. DR PDBsum; 4V5M; -. DR PDBsum; 4V5N; -. DR PDBsum; 4V5P; -. DR PDBsum; 4V5Q; -. DR PDBsum; 4V5R; -. DR PDBsum; 4V5S; -. DR PDBsum; 4V68; -. DR PDBsum; 4V6A; -. DR PDBsum; 4V7J; -. DR PDBsum; 4V7K; -. DR PDBsum; 4V7L; -. DR PDBsum; 4V7M; -. DR PDBsum; 4V8J; -. DR PDBsum; 4V8N; -. DR PDBsum; 4V8O; -. DR PDBsum; 4V8Q; -. DR PDBsum; 4V8U; -. DR PDBsum; 4V8X; -. DR PDBsum; 4V90; -. DR PDBsum; 4V97; -. DR PDBsum; 4V9H; -. DR PDBsum; 4WF1; -. DR PDBsum; 4WPO; -. DR PDBsum; 4WQF; -. DR PDBsum; 4WQU; -. DR PDBsum; 4WQY; -. DR PDBsum; 4WT8; -. DR PDBsum; 4WU1; -. DR PDBsum; 4WZD; -. DR PDBsum; 4WZO; -. DR PDBsum; 5A9Z; -. DR PDBsum; 5AA0; -. DR PDBsum; 5E7K; -. DR PDBsum; 5E81; -. DR PDBsum; 5EL4; -. DR PDBsum; 5EL5; -. DR PDBsum; 5EL6; -. DR PDBsum; 5EL7; -. DR PDBsum; 5HAU; -. DR PDBsum; 5NPM; -. DR PDBsum; 5OT7; -. DR PDBsum; 5UQ7; -. DR PDBsum; 5UQ8; -. DR PDBsum; 5ZLU; -. DR PDBsum; 6C5L; -. DR PDBsum; 6GSL; -. DR PDBsum; 6Q95; -. DR PDBsum; 6QNQ; -. DR PDBsum; 6QNR; -. DR PDBsum; 7LH5; -. DR AlphaFoldDB; Q5SLP7; -. DR EMDB; EMD-3852; -. DR EMDB; EMD-4475; -. DR EMDB; EMD-8596; -. DR EMDB; EMD-8597; -. DR SMR; Q5SLP7; -. DR IntAct; Q5SLP7; 9. DR EnsemblBacteria; BAD70069; BAD70069; BAD70069. DR GeneID; 3168861; -. DR KEGG; ttj:TTHA0246; -. DR PATRIC; fig|300852.9.peg.246; -. DR eggNOG; COG0081; Bacteria. DR HOGENOM; CLU_062853_0_0_0; -. DR PhylomeDB; Q5SLP7; -. DR EvolutionaryTrace; Q5SLP7; -. DR Proteomes; UP000000532; 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:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd00403; Ribosomal_L1; 1. DR Gene3D; 3.30.190.20; -; 1. DR Gene3D; 3.40.50.790; -; 1. DR HAMAP; MF_01318_B; Ribosomal_uL1_B; 1. DR InterPro; IPR005878; Ribosom_uL1_bac-type. DR InterPro; IPR002143; Ribosomal_uL1. DR InterPro; IPR023674; Ribosomal_uL1-like. DR InterPro; IPR028364; Ribosomal_uL1/biogenesis. DR InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand. DR InterPro; IPR023673; Ribosomal_uL1_CS. DR NCBIfam; TIGR01169; rplA_bact; 1. DR PANTHER; PTHR36427:SF3; 39S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1. DR PANTHER; PTHR36427; 54S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1. DR Pfam; PF00687; Ribosomal_L1; 1. DR PIRSF; PIRSF002155; Ribosomal_L1; 1. DR SUPFAM; SSF56808; Ribosomal protein L1; 1. DR PROSITE; PS01199; RIBOSOMAL_L1; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Reference proteome; Repressor; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; KW Translation regulation; tRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11154066" FT CHAIN 2..229 FT /note="Large ribosomal subunit protein uL1" FT /id="PRO_0000125764" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 41..50 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:5NPM" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 82..89 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 112..116 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:3TG8" FT TURN 133..136 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 150..157 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 170..178 FT /evidence="ECO:0007829|PDB:3TG8" FT HELIX 183..199 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:3TG8" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:3TG8" SQ SEQUENCE 229 AA; 24831 MW; 99EE7BE00801B1B4 CRC64; MPKHGKRYRA LLEKVDPNKV YTIDEAARLV KELATAKFDE TVEVHAKLGI DPRRSDQNVR GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI IQKILDGWMD FDAVVATPDV MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI GEIIREIKAG RIEFRNDKTG AIHAPVGKAS FPPEKLADNI RAFIRALEAH KPEGAKGTFL RSVYVTTTMG PSVRINPHS //