ID RS5_THET2 Reviewed; 162 AA. AC P62665; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 116. DE RecName: Full=Small ribosomal subunit protein uS5 {ECO:0000305}; DE AltName: Full=30S ribosomal protein S5; GN Name=rpsE; Synonyms=rps5; OrderedLocusNames=TT_C1311; 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: With S4 and S12 plays an important role in translational CC accuracy. {ECO:0000250}. CC -!- FUNCTION: Located at the back of the 30S subunit body where it CC stabilizes the conformation of the head with respect to the body. CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and S8 CC (By similarity). {ECO:0000250}. CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S CC subunit; the C-terminal domain interacts with the body and contacts CC protein S4. The interaction surface between S4 and S5 is involved in CC control of translational fidelity. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 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; AE017221; AAS81653.1; -; Genomic_DNA. DR RefSeq; WP_008633389.1; NZ_CP133179.1. DR PDB; 4KVB; X-ray; 4.20 A; E=1-162. DR PDB; 4V4I; X-ray; 3.71 A; f=1-162. DR PDB; 4V4J; X-ray; 3.83 A; f=1-162. DR PDB; 4V63; X-ray; 3.21 A; AE/CE=1-162. DR PDB; 4V67; X-ray; 3.00 A; AE/CE=1-162. DR PDB; 4V7P; X-ray; 3.62 A; AE/DE=5-155. DR PDB; 4V83; X-ray; 3.50 A; AE/CE=5-155. DR PDB; 4V84; X-ray; 3.40 A; AE/CE=5-155. DR PDB; 4V9J; X-ray; 3.86 A; AE/CE=5-155. DR PDB; 4V9K; X-ray; 3.50 A; AE/CE=5-155. DR PDB; 4V9L; X-ray; 3.50 A; AE/CE=5-155. DR PDB; 4V9M; X-ray; 4.00 A; AE/CE=5-155. DR PDB; 4V9N; X-ray; 3.40 A; AE/CE=5-155. DR PDB; 4V9Q; X-ray; 3.40 A; BE/DE=5-155. DR PDB; 4W29; X-ray; 3.80 A; AE/CE=5-155. DR PDB; 4XEJ; X-ray; 3.80 A; AS05/BS05=5-155. DR PDB; 5J4D; X-ray; 3.10 A; NA/SC=1-162. DR PDB; 5V8I; X-ray; 3.25 A; 1e/2e=1-162. DR PDB; 6B4V; X-ray; 3.40 A; NA/RC=1-162. DR PDB; 6BOH; X-ray; 3.40 A; OA/TC=1-162. DR PDB; 6BOK; X-ray; 3.55 A; MA/PC=1-162. DR PDB; 6N1D; X-ray; 3.20 A; AS05/BS05=2-162. DR PDBsum; 4KVB; -. 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; P62665; -. DR SMR; P62665; -. DR IntAct; P62665; 4. DR GeneID; 3169827; -. DR KEGG; tth:TT_C1311; -. DR eggNOG; COG0098; Bacteria. DR HOGENOM; CLU_065898_2_2_0; -. DR OrthoDB; 9809045at2; -. DR EvolutionaryTrace; P62665; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0015935; C:small 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; 3.30.160.20; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_01307_B; Ribosomal_uS5_B; 1. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR000851; Ribosomal_uS5. DR InterPro; IPR005712; Ribosomal_uS5_bac-type. DR InterPro; IPR005324; Ribosomal_uS5_C. DR InterPro; IPR013810; Ribosomal_uS5_N. DR InterPro; IPR018192; Ribosomal_uS5_N_CS. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR NCBIfam; TIGR01021; rpsE_bact; 1. DR PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1. DR PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..162 FT /note="Small ribosomal subunit protein uS5" FT /id="PRO_0000131620" FT DOMAIN 7..70 FT /note="S5 DRBM" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 37..47 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:4V9N" FT HELIX 51..64 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:4V9Q" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 104..112 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 117..124 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 128..139 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 145..151 FT /evidence="ECO:0007829|PDB:4V67" SQ SEQUENCE 162 AA; 17557 MW; BE3367CB619E68D2 CRC64; MPETDFEEKM ILIRRTARMQ AGGRRFRFGA LVVVGDRQGR VGLGFGKAPE VPLAVQKAGY YARRNMVEVP LQNGTIPHEI EVEFGASKIV LKPAAPGTGV IAGAVPRAIL ELAGVTDILT KELGSRNPIN IAYATMEALR QLRTKADVER LRKGEAHAQA QG //