ID RS7_THET2 Reviewed; 156 AA. AC P62667; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 117. DE RecName: Full=Small ribosomal subunit protein uS7 {ECO:0000305}; DE AltName: Full=30S ribosomal protein S7; GN Name=rpsG; Synonyms=rps7; OrderedLocusNames=TT_C1332; 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, it binds directly CC to 16S rRNA where it nucleates assembly of the head domain of the 30S CC subunit. Is located at the subunit interface close to the decoding CC center, probably blocks exit of the E-site tRNA (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 and CC S11 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 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; AAS81674.1; -; Genomic_DNA. DR RefSeq; WP_008633429.1; NZ_CP133179.1. DR PDB; 4KVB; X-ray; 4.20 A; G=1-156. DR PDB; 4V4I; X-ray; 3.71 A; h=1-156. DR PDB; 4V4J; X-ray; 3.83 A; h=1-156. DR PDB; 4V5L; X-ray; 3.10 A; AG=1-156. DR PDB; 4V63; X-ray; 3.21 A; AG/CG=1-156. DR PDB; 4V67; X-ray; 3.00 A; AG/CG=1-156. DR PDB; 4V7P; X-ray; 3.62 A; AG/DG=2-156. DR PDB; 4V83; X-ray; 3.50 A; AG/CG=2-156. DR PDB; 4V84; X-ray; 3.40 A; AG/CG=2-156. DR PDB; 4V9J; X-ray; 3.86 A; AG/CG=2-156. DR PDB; 4V9K; X-ray; 3.50 A; AG/CG=2-156. DR PDB; 4V9L; X-ray; 3.50 A; AG/CG=2-156. DR PDB; 4V9M; X-ray; 4.00 A; AG/CG=2-156. DR PDB; 4V9N; X-ray; 3.40 A; AG/CG=2-156. DR PDB; 4V9Q; X-ray; 3.40 A; BG/DG=2-156. DR PDB; 4W29; X-ray; 3.80 A; AG/CG=2-156. DR PDB; 4XEJ; X-ray; 3.80 A; AS07/BS07=2-156. DR PDB; 5J4D; X-ray; 3.10 A; PA/UC=1-156. DR PDB; 5V8I; X-ray; 3.25 A; 1g/2g=1-156. DR PDB; 6B4V; X-ray; 3.40 A; PA/TC=1-156. DR PDB; 6BOH; X-ray; 3.40 A; QA/VC=1-156. DR PDB; 6BOK; X-ray; 3.55 A; OA/RC=1-156. DR PDB; 6N1D; X-ray; 3.20 A; AS07/BS07=2-156. DR PDBsum; 4KVB; -. DR PDBsum; 4V4I; -. DR PDBsum; 4V4J; -. DR PDBsum; 4V5L; -. 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; P62667; -. DR SMR; P62667; -. DR IntAct; P62667; 4. DR GeneID; 3167931; -. DR KEGG; tth:TT_C1332; -. DR eggNOG; COG0049; Bacteria. DR HOGENOM; CLU_072226_1_1_0; -. DR OrthoDB; 9807653at2; -. DR EvolutionaryTrace; P62667; -. DR Proteomes; UP000000592; Chromosome. 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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd14869; uS7_Bacteria; 1. DR Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1. DR HAMAP; MF_00480_B; Ribosomal_uS7_B; 1. DR InterPro; IPR000235; Ribosomal_uS7. DR InterPro; IPR005717; Ribosomal_uS7_bac/org-type. DR InterPro; IPR020606; Ribosomal_uS7_CS. DR InterPro; IPR023798; Ribosomal_uS7_dom. DR InterPro; IPR036823; Ribosomal_uS7_dom_sf. DR NCBIfam; TIGR01029; rpsG_bact; 1. DR PANTHER; PTHR11205:SF19; 28S RIBOSOMAL PROTEIN S7, MITOCHONDRIAL; 1. DR PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1. DR Pfam; PF00177; Ribosomal_S7; 1. DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1. DR SUPFAM; SSF47973; Ribosomal protein S7; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding; tRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..156 FT /note="Small ribosomal subunit protein uS7" FT /id="PRO_0000124368" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 21..30 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:4V83" FT HELIX 36..53 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:4V63" FT HELIX 58..68 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 72..80 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 93..110 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 116..129 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 133..147 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 148..154 FT /evidence="ECO:0007829|PDB:4V67" SQ SEQUENCE 156 AA; 18016 MW; BC20C4487623B0E9 CRC64; MARRRRAEVR QLQPDLVYGD VLVTAFINKI MRDGKKNLAA RIFYDACKII QEKTGQEPLK VFKQAVENVK PRMEVRSRRV GGANYQVPME VSPRRQQSLA LRWLVQAANQ RPERRAAVRI AHELMDAAEG KGGAVKKKED VERMAEANRA YAHYRW //