RS9_THET2
ID RS9_THET2 Reviewed; 128 AA.
AC P62669;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=30S ribosomal protein S9;
GN Name=rpsI; Synonyms=rps9; OrderedLocusNames=TT_C1100;
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 [GENOMIC DNA].
RX PubMed=11296217; DOI=10.1093/emboj/20.8.1829;
RA Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H.,
RA Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A.,
RA Franceschi F.;
RT "Crystal structures of complexes of the small ribosomal subunit with
RT tetracycline, edeine and IF3.";
RL EMBO J. 20:1829-1839(2001).
RN [2]
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: Part of the top of the head of the 30S subunit. The C-
CC terminal region penetrates the head emerging in the P-site where it
CC contacts tRNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S7 and
CC S10 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC {ECO:0000305}.
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DR EMBL; AJ409331; CAC35063.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81442.1; -; Genomic_DNA.
DR RefSeq; WP_008632991.1; NC_005835.1.
DR PDB; 1I94; X-ray; 3.20 A; I=1-128.
DR PDB; 1I96; X-ray; 4.20 A; I=1-128.
DR PDB; 2R1G; EM; 12.50 A; G=2-128.
DR PDB; 2UXB; X-ray; 3.10 A; I=1-128.
DR PDB; 2UXC; X-ray; 2.90 A; I=1-128.
DR PDB; 2UXD; X-ray; 3.20 A; I=1-128.
DR PDB; 2VQE; X-ray; 2.50 A; I=1-128.
DR PDB; 2VQF; X-ray; 2.90 A; I=1-128.
DR PDB; 3T1H; X-ray; 3.11 A; I=1-128.
DR PDB; 3T1Y; X-ray; 2.80 A; I=1-128.
DR PDB; 4KVB; X-ray; 4.20 A; I=1-128.
DR PDB; 4V4I; X-ray; 3.71 A; j=1-128.
DR PDB; 4V4J; X-ray; 3.83 A; j=1-128.
DR PDB; 4V51; X-ray; 2.80 A; AI/CI=1-128.
DR PDB; 4V5A; X-ray; 3.50 A; AI/CI=1-128.
DR PDB; 4V5C; X-ray; 3.30 A; AI/CI=1-128.
DR PDB; 4V5D; X-ray; 3.50 A; AI/CI=1-128.
DR PDB; 4V63; X-ray; 3.21 A; AI/CI=1-128.
DR PDB; 4V67; X-ray; 3.00 A; AI/CI=1-128.
DR PDB; 4V7P; X-ray; 3.62 A; AI/DI=2-128.
DR PDB; 4V83; X-ray; 3.50 A; AI/CI=2-128.
DR PDB; 4V84; X-ray; 3.40 A; AI/CI=2-128.
DR PDB; 4V9J; X-ray; 3.86 A; AI/CI=2-128.
DR PDB; 4V9K; X-ray; 3.50 A; AI/CI=2-128.
DR PDB; 4V9L; X-ray; 3.50 A; AI/CI=2-128.
DR PDB; 4V9M; X-ray; 4.00 A; AI/CI=2-128.
DR PDB; 4V9N; X-ray; 3.40 A; AI/CI=2-128.
DR PDB; 4V9Q; X-ray; 3.40 A; BI/DI=2-128.
DR PDB; 4W29; X-ray; 3.80 A; AI/CI=2-128.
DR PDB; 4XEJ; X-ray; 3.80 A; AS09/BS09=2-128.
DR PDB; 5J4D; X-ray; 3.10 A; RA/WC=1-128.
DR PDBsum; 1I94; -.
DR PDBsum; 1I96; -.
DR PDBsum; 2R1G; -.
DR PDBsum; 2UXB; -.
DR PDBsum; 2UXC; -.
DR PDBsum; 2UXD; -.
DR PDBsum; 2VQE; -.
DR PDBsum; 2VQF; -.
DR PDBsum; 3T1H; -.
DR PDBsum; 3T1Y; -.
DR PDBsum; 4KVB; -.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V51; -.
DR PDBsum; 4V5A; -.
DR PDBsum; 4V5C; -.
DR PDBsum; 4V5D; -.
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; P62669; -.
DR SMR; P62669; -.
DR IntAct; P62669; 5.
DR STRING; 262724.TT_C1100; -.
DR DrugBank; DB08185; 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.
DR EnsemblBacteria; AAS81442; AAS81442; TT_C1100.
DR KEGG; tth:TT_C1100; -.
DR eggNOG; COG0103; Bacteria.
DR HOGENOM; CLU_046483_2_1_0; -.
DR OMA; QWKINGR; -.
DR OrthoDB; 1766414at2; -.
DR EvolutionaryTrace; P62669; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR023035; Ribosomal_S9_bac/plastid.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..128
FT /note="30S ribosomal protein S9"
FT /id="PRO_0000111430"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3T1Y"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3T1Y"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3T1Y"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3T1Y"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3T1Y"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:3T1Y"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3T1Y"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:3T1Y"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3T1H"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3T1Y"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:3T1Y"
FT TURN 90..99
FT /evidence="ECO:0007829|PDB:3T1Y"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3T1H"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3T1Y"
SQ SEQUENCE 128 AA; 14402 MW; 7886A020CC5D9934 CRC64;
MEQYYGTGRR KEAVARVFLR PGNGKVTVNG QDFNEYFQGL VRAVAALEPL RAVDALGRFD
AYITVRGGGK SGQIDAIKLG IARALVQYNP DYRAKLKPLG FLTRDARVVE RKKYGKHKAR
RAPQYSKR
