RS7_THET2
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 25-MAY-2022, entry version 110.
DE RecName: 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; Deinococcus-Thermus; 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}.
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DR EMBL; AE017221; AAS81674.1; -; Genomic_DNA.
DR RefSeq; WP_008633429.1; NC_005835.1.
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 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 AlphaFoldDB; P62667; -.
DR SMR; P62667; -.
DR IntAct; P62667; 4.
DR STRING; 262724.TT_C1332; -.
DR EnsemblBacteria; AAS81674; AAS81674; TT_C1332.
DR GeneID; 3167931; -.
DR KEGG; tth:TT_C1332; -.
DR eggNOG; COG0049; Bacteria.
DR HOGENOM; CLU_072226_1_1_0; -.
DR OMA; NVMPHVE; -.
DR OrthoDB; 1540940at2; -.
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 Gene3D; 1.10.455.10; -; 1.
DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005717; Ribosomal_S7_bac/org-type.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01029; rpsG_bact; 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="30S ribosomal protein S7"
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
