(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 100.
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}.
DR   EMBL; Z36971; CAA85419.1; -; Genomic_DNA.
DR   RefSeq; WP_011173708.1; NZ_AP019801.1.
DR   PDB; 1QD7; X-ray; 5.50 A; I=6-85.
DR   PDB; 1TWT; Model; -; T=2-105.
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; 1TWT; -.
DR   PDBsum; 2VQE; -.
DR   PDBsum; 2VQF; -.
DR   PDBsum; 5IMQ; -.
DR   PDBsum; 5IMR; -.
DR   SMR; P24321; -.
DR   eggNOG; ENOG4105K87; Bacteria.
DR   eggNOG; COG0186; LUCA.
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   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;
DR   PRODOM; P24321.
DR   SWISS-2DPAGE; P24321.
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:0000244|PDB:2VQE"
FT   STRAND          18..28
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   TURN            30..32
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   STRAND          35..45
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   STRAND          56..66
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   STRAND          69..78
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   HELIX           82..93
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   HELIX           94..97
FT                   /evidence="ECO:0000244|PDB:2VQE"
FT   STRAND          98..101
FT                   /evidence="ECO:0000244|PDB:2VQE"
SQ   SEQUENCE   105 AA;  12297 MW;  6089596D57478FBD CRC64;
     MPKKVLTGVV VSDKMQKTVT VLVERQFPHP LYGKVIKRSK KYLAHDPEEK YKLGDVVEII
     ESRPISKRKR FRVLRLVESG RMDLVEKYLI RRQNYQSLSK RGGKA
//

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