RS15_THET2
ID RS15_THET2 Reviewed; 89 AA.
AC P62657;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343};
GN Synonyms=rps15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN OrderedLocusNames=TT_C0773;
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 helps nucleate assembly of the platform of the 30S
CC subunit by binding and bridging several RNA helices of the 16S rRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01343}.
CC -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the 50S
CC subunit in the 70S ribosome, contacting the 23S rRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01343}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000255|HAMAP-Rule:MF_01343}.
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DR EMBL; AE017221; AAS81119.1; -; Genomic_DNA.
DR RefSeq; WP_008632621.1; NC_005835.1.
DR PDB; 4KVB; X-ray; 4.20 A; O=1-89.
DR PDB; 4V4G; X-ray; 11.50 A; O=2-89.
DR PDB; 4V4I; X-ray; 3.71 A; p=1-89.
DR PDB; 4V4J; X-ray; 3.83 A; p=1-89.
DR PDB; 4V63; X-ray; 3.21 A; AO/CO=1-89.
DR PDB; 4V67; X-ray; 3.00 A; AO/CO=1-89.
DR PDB; 4V7P; X-ray; 3.62 A; AO/DO=2-89.
DR PDB; 4V83; X-ray; 3.50 A; AO/CO=2-89.
DR PDB; 4V84; X-ray; 3.40 A; AO/CO=2-89.
DR PDB; 4V9J; X-ray; 3.86 A; AO/CO=2-89.
DR PDB; 4V9K; X-ray; 3.50 A; AO/CO=2-89.
DR PDB; 4V9L; X-ray; 3.50 A; AO/CO=2-89.
DR PDB; 4V9M; X-ray; 4.00 A; AO/CO=2-89.
DR PDB; 4V9N; X-ray; 3.40 A; AO/CO=2-89.
DR PDB; 4V9Q; X-ray; 3.40 A; BO/DO=2-89.
DR PDB; 4W29; X-ray; 3.80 A; AO/CO=2-89.
DR PDB; 4XEJ; X-ray; 3.80 A; AS15/BS15=2-89.
DR PDB; 5J4D; X-ray; 3.10 A; CD/XA=1-89.
DR PDBsum; 4KVB; -.
DR PDBsum; 4V4G; -.
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 AlphaFoldDB; P62657; -.
DR SMR; P62657; -.
DR IntAct; P62657; 4.
DR STRING; 262724.TT_C0773; -.
DR EnsemblBacteria; AAS81119; AAS81119; TT_C0773.
DR GeneID; 3169463; -.
DR KEGG; tth:TT_C0773; -.
DR eggNOG; COG0184; Bacteria.
DR HOGENOM; CLU_148518_0_0_0; -.
DR OMA; FKTHVKD; -.
DR OrthoDB; 1990141at2; -.
DR EvolutionaryTrace; P62657; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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 CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR InterPro; IPR000589; Ribosomal_S15.
DR InterPro; IPR005290; Ribosomal_S15_bac-type.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR PANTHER; PTHR23321; PTHR23321; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR TIGRFAMs; TIGR00952; S15_bact; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 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..89
FT /note="30S ribosomal protein S15"
FT /id="PRO_0000115573"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 50..73
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 89 AA; 10554 MW; 9DB7E1C533DBF340 CRC64;
MPITKEEKQK VIQEFARFPG DTGSTEVQVA LLTLRINRLS EHLKVHKKDH HSHRGLLMMV
GQRRRLLRYL QREDPERYRA LIEKLGIRG
