ID RL2_THET2 Reviewed; 276 AA. AC Q72I07; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 08-NOV-2023, entry version 115. DE RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000255|HAMAP-Rule:MF_01320}; DE AltName: Full=50S ribosomal protein L2 {ECO:0000305}; GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=TT_C1325; 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: One of the primary rRNA binding proteins. Required for CC association of the 30S and 50S subunits to form the 70S ribosome, for CC tRNA binding and peptide bond formation. It has been suggested to have CC peptidyltransferase activity; this is somewhat controversial. Makes CC several contacts with the 16S rRNA in the 70S ribosome. CC {ECO:0000255|HAMAP-Rule:MF_01320}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S CC subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family. CC {ECO:0000255|HAMAP-Rule:MF_01320}. 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; AAS81667.1; -; Genomic_DNA. DR RefSeq; WP_011173712.1; NC_005835.1. DR PDB; 4V4I; X-ray; 3.71 A; B=1-276. DR PDB; 4V4J; X-ray; 3.83 A; B=1-276. DR PDB; 4V63; X-ray; 3.21 A; BD/DD=1-276. DR PDB; 4V67; X-ray; 3.00 A; BD/DD=1-276. DR PDB; 4V7P; X-ray; 3.62 A; BC/CC=2-276. DR PDB; 4V83; X-ray; 3.50 A; BC/DC=2-272. DR PDB; 4V84; X-ray; 3.40 A; BC/DC=2-272. DR PDB; 4V9J; X-ray; 3.86 A; BD/DD=2-276. DR PDB; 4V9K; X-ray; 3.50 A; BD/DD=2-276. DR PDB; 4V9L; X-ray; 3.50 A; BD/DD=2-276. DR PDB; 4V9M; X-ray; 4.00 A; BD/DD=2-276. DR PDB; 4V9N; X-ray; 3.40 A; BD/DD=2-272. DR PDB; 4V9Q; X-ray; 3.40 A; AD/CD=2-272. DR PDB; 4W29; X-ray; 3.80 A; BD/DD=2-276. DR PDB; 4XEJ; X-ray; 3.80 A; AL02/BL02=2-272. DR PDB; 5J4D; X-ray; 3.10 A; E/JB=2-276. DR PDB; 5V8I; X-ray; 3.25 A; 1D/2D=1-276. DR PDB; 6B4V; X-ray; 3.40 A; E/IB=2-276. DR PDB; 6BOH; X-ray; 3.40 A; E/JB=2-276. DR PDB; 6BOK; X-ray; 3.55 A; E/HB=2-276. DR PDB; 6N1D; X-ray; 3.20 A; AL02/BL02=1-276. 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; Q72I07; -. DR SMR; Q72I07; -. DR IntAct; Q72I07; 4. DR STRING; 262724.TT_C1325; -. DR EnsemblBacteria; AAS81667; AAS81667; TT_C1325. DR GeneID; 3168720; -. DR KEGG; tth:TT_C1325; -. DR eggNOG; COG0090; Bacteria. DR HOGENOM; CLU_036235_2_1_0; -. DR OMA; SCIELRP; -. DR OrthoDB; 9778722at2; -. DR EvolutionaryTrace; Q72I07; -. 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:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1. DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR002171; Ribosomal_uL2. DR InterPro; IPR005880; Ribosomal_uL2_bac/org-type. DR InterPro; IPR022669; Ribosomal_uL2_C. DR InterPro; IPR022671; Ribosomal_uL2_CS. DR InterPro; IPR014726; Ribosomal_uL2_dom3. DR InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR NCBIfam; TIGR01171; rplB_bact; 1. DR PANTHER; PTHR13691:SF5; 39S RIBOSOMAL PROTEIN L2, MITOCHONDRIAL; 1. DR PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR PIRSF; PIRSF002158; Ribosomal_L2; 1. DR SMART; SM01383; Ribosomal_L2; 1. DR SMART; SM01382; Ribosomal_L2_C; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT CHAIN 1..276 FT /note="Large ribosomal subunit protein uL2" FT /id="PRO_0000237259" FT REGION 223..276 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 256..276 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:4V9Q" FT STRAND 9..15 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 33..38 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:4V63" FT TURN 67..72 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 92..100 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:4V9N" FT STRAND 114..123 FT /evidence="ECO:0007829|PDB:4V84" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:4V9K" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:4V63" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:4V63" FT TURN 149..151 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:4V9K" FT STRAND 163..169 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:4V9L" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 190..197 FT /evidence="ECO:0007829|PDB:4V63" FT HELIX 199..203 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 209..215 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 232..235 FT /evidence="ECO:0007829|PDB:4V9Q" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 265..269 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:4V9K" SQ SEQUENCE 276 AA; 30468 MW; 7CF40C2BD586349B CRC64; MAVKKFKPYT PSRRFMTVAD FSEITKTEPE KSLVKPLKKT GGRNNQGRIT VRFRGGGHKR LYRIIDFKRW DKVGIPAKVA AIEYDPNRSA RIALLHYVDG EKRYIIAPDG LQVGQQVVAG PDAPIQVGNA LPLRFIPVGT VVHAVELEPK KGAKLARAAG TSAQIQGREG DYVILRLPSG ELRKVHGECY ATVGAVGNAD HKNIVLGKAG RSRWLGRRPH VRGAAMNPVD HPHGGGEGRA PRGRPPASPW GWQTKGLKTR KRRKPSSRFI IARRKK //