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 03-OCT-2012, entry version 63. DE RecName: Full=50S ribosomal protein L2; GN Name=rplB; OrderedLocusNames=TT_C1325; OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., RA Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., RA Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., RA Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus RT 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, CC for tRNA binding and peptide bond formation. It has been suggested CC to have peptidyltransferase activity; this is somewhat CC controversial. Makes several contacts with the 16S rRNA in the 70S CC ribosome (By similarity). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the CC 30S subunit in the 70S ribosome (By similarity). CC -!- SIMILARITY: Belongs to the ribosomal protein L2P family. 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; YP_005294.1; NC_005835.1. DR PDB; 1VSA; X-ray; 3.71 A; B=1-276. DR PDB; 1VSP; X-ray; 3.83 A; B=1-276. DR PDB; 3D5B; X-ray; 3.21 A; D=1-276. DR PDB; 3D5D; X-ray; 3.21 A; D=1-276. DR PDB; 3F1F; X-ray; 3.00 A; D=1-276. DR PDB; 3F1H; X-ray; 3.00 A; D=1-276. DR PDB; 3MRZ; X-ray; 3.62 A; C=2-276. DR PDB; 3MS1; X-ray; 3.62 A; C=2-276. DR PDB; 3PYO; X-ray; 3.50 A; C=2-272. DR PDB; 3PYR; X-ray; 3.50 A; C=2-272. DR PDB; 3PYT; X-ray; 3.40 A; C=2-272. DR PDB; 3PYV; X-ray; 3.40 A; C=2-272. DR PDBsum; 1VSA; -. DR PDBsum; 1VSP; -. DR PDBsum; 3D5B; -. DR PDBsum; 3D5D; -. DR PDBsum; 3F1F; -. DR PDBsum; 3F1H; -. DR PDBsum; 3MRZ; -. DR PDBsum; 3MS1; -. DR PDBsum; 3PYO; -. DR PDBsum; 3PYR; -. DR PDBsum; 3PYT; -. DR PDBsum; 3PYV; -. DR ProteinModelPortal; Q72I07; -. DR SMR; Q72I07; 2-273. DR STRING; Q72I07; -. DR GeneID; 2775711; -. DR GenomeReviews; AE017221_GR; TT_C1325. DR KEGG; tth:TTC1325; -. DR PATRIC; 23953057; VBITheThe54392_1317. DR eggNOG; COG0090; -. DR KO; K02886; -. DR OMA; QSNINWG; -. DR ProtClustDB; PRK09374; -. DR BioCyc; TTHE262724:TT_C1325-MONOMER; -. DR EvolutionaryTrace; Q72I07; -. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. 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:InterPro. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1. DR Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 1. DR Gene3D; G3DSA:4.10.950.10; Ribosomal_L2; 1. DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1; -. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR016027; NA-bd_OB-fold-like. DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom. DR InterPro; IPR002171; Ribosomal_L2. DR InterPro; IPR014726; Ribosomal_L2_3. DR InterPro; IPR005880; Ribosomal_L2_bac/org-type. DR InterPro; IPR022669; Ribosomal_L2_C. DR InterPro; IPR022671; Ribosomal_L2_CS. DR InterPro; IPR014722; Transl_SH3-like_sub. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR13691; PTHR13691; 1. DR PANTHER; PTHR13691:SF5; PTHR13691:SF5; 1. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR PIRSF; PIRSF002158; Ribosomal_L2; 1. DR SUPFAM; SSF50249; Nucleic_acid_OB; 1. DR SUPFAM; SSF50104; Transl_SH3_like; 1. DR TIGRFAMs; TIGR01171; rplB_bact; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding. FT CHAIN 1 276 50S ribosomal protein L2. FT /FTId=PRO_0000237259. FT STRAND 9 15 FT STRAND 17 19 FT HELIX 21 23 FT STRAND 33 38 FT STRAND 45 47 FT STRAND 50 54 FT STRAND 61 63 FT TURN 67 72 FT STRAND 77 83 FT STRAND 88 90 FT STRAND 92 100 FT STRAND 102 106 FT STRAND 114 123 FT STRAND 130 132 FT TURN 133 135 FT STRAND 141 148 FT TURN 149 151 FT STRAND 153 155 FT STRAND 163 169 FT STRAND 172 176 FT STRAND 182 186 FT STRAND 190 197 FT HELIX 199 203 FT HELIX 209 215 FT HELIX 223 225 FT TURN 228 230 FT TURN 232 235 FT STRAND 237 239 FT STRAND 243 245 FT HELIX 265 269 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 //