RS17_THETH
ID RS17_THETH Reviewed; 105 AA.
AC P24321;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=30S ribosomal protein S17 {ECO:0000255|HAMAP-Rule:MF_01345};
GN Name=rpsQ {ECO:0000255|HAMAP-Rule:MF_01345};
GN Synonyms=rps17 {ECO:0000255|HAMAP-Rule:MF_01345};
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VK1;
RX PubMed=9249063; DOI=10.1016/s0378-1119(97)00072-3;
RA Vysotskaya V.S., Shcherbakov D.V., Garber M.B.;
RT "Sequencing and analysis of the Thermus thermophilus ribosomal protein gene
RT cluster equivalent to the spectinomycin operon.";
RL Gene 193:23-30(1997).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-
CC Rule:MF_01345}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01345}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC {ECO:0000255|HAMAP-Rule:MF_01345}.
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DR EMBL; Z36971; CAA85419.1; -; Genomic_DNA.
DR RefSeq; WP_011173708.1; NZ_VHHQ01000024.1.
DR PDB; 1QD7; X-ray; 5.50 A; I=6-85.
DR PDB; 2VQE; X-ray; 2.50 A; Q=1-105.
DR PDB; 2VQF; X-ray; 2.90 A; Q=1-105.
DR PDB; 5IMQ; EM; 3.80 A; U=1-105.
DR PDB; 5IMR; EM; -; U=1-105.
DR PDBsum; 1QD7; -.
DR PDBsum; 2VQE; -.
DR PDBsum; 2VQF; -.
DR PDBsum; 5IMQ; -.
DR PDBsum; 5IMR; -.
DR AlphaFoldDB; P24321; -.
DR SMR; P24321; -.
DR IntAct; P24321; 1.
DR EvolutionaryTrace; P24321; -.
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 Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01345_B; Ribosomal_S17_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019984; Ribosomal_S17.
DR InterPro; IPR000266; Ribosomal_S17/S11.
DR InterPro; IPR019979; Ribosomal_S17_CS.
DR PANTHER; PTHR10744; PTHR10744; 1.
DR Pfam; PF00366; Ribosomal_S17; 1.
DR PRINTS; PR00973; RIBOSOMALS17.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR03635; uS17_bact; 1.
DR PROSITE; PS00056; RIBOSOMAL_S17; 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..105
FT /note="30S ribosomal protein S17"
FT /id="PRO_0000128493"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:2VQE"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:2VQE"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2VQE"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:2VQE"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:2VQE"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:2VQE"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2VQE"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2VQE"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2VQE"
SQ SEQUENCE 105 AA; 12297 MW; 6089596D57478FBD CRC64;
MPKKVLTGVV VSDKMQKTVT VLVERQFPHP LYGKVIKRSK KYLAHDPEEK YKLGDVVEII
ESRPISKRKR FRVLRLVESG RMDLVEKYLI RRQNYQSLSK RGGKA
