ID RS11_THET2 Reviewed; 129 AA. AC P62654; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 114. DE RecName: Full=Small ribosomal subunit protein uS11 {ECO:0000305}; DE AltName: Full=30S ribosomal protein S11; GN Name=rpsK; Synonyms=rps11; OrderedLocusNames=TT_C1302; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; 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: Located on the upper part of the platform of the 30S subunit, CC where it bridges several disparate RNA helices of the 16S rRNA. Forms CC part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Interacts with proteins S7 CC and S18. Binds to the C-terminus of IF-3; however exactly how IF-3 CC interacts with the 30S subunit is unclear. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017221; AAS81644.1; -; Genomic_DNA. DR RefSeq; WP_008633365.1; NZ_CP133179.1. DR PDB; 4KVB; X-ray; 4.20 A; K=1-129. DR PDB; 4V4I; X-ray; 3.71 A; l=1-129. DR PDB; 4V4J; X-ray; 3.83 A; l=1-129. DR PDB; 4V63; X-ray; 3.21 A; AK/CK=1-129. DR PDB; 4V67; X-ray; 3.00 A; AK/CK=1-129. DR PDB; 4V7P; X-ray; 3.62 A; AK/DK=11-129. DR PDB; 4V83; X-ray; 3.50 A; AK/CK=11-129. DR PDB; 4V84; X-ray; 3.40 A; AK/CK=11-129. DR PDB; 4V9J; X-ray; 3.86 A; AK/CK=11-129. DR PDB; 4V9K; X-ray; 3.50 A; AK/CK=11-129. DR PDB; 4V9L; X-ray; 3.50 A; AK/CK=11-129. DR PDB; 4V9M; X-ray; 4.00 A; AK/CK=11-129. DR PDB; 4V9N; X-ray; 3.40 A; AK/CK=11-124. DR PDB; 4V9Q; X-ray; 3.40 A; BK/DK=11-124. DR PDB; 4W29; X-ray; 3.80 A; AK/CK=11-129. DR PDB; 4XEJ; X-ray; 3.80 A; AS11/BS11=11-124. DR PDB; 5J4D; X-ray; 3.10 A; TA/YC=1-129. DR PDB; 5V8I; X-ray; 3.25 A; 1k/2k=1-129. DR PDB; 6B4V; X-ray; 3.40 A; TA/XC=1-129. DR PDB; 6BOH; X-ray; 3.40 A; UA/ZC=1-129. DR PDB; 6BOK; X-ray; 3.55 A; SA/VC=1-129. DR PDB; 6N1D; X-ray; 3.20 A; AS11/BS11=2-129. DR PDBsum; 4KVB; -. 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 PDBsum; 5V8I; -. DR PDBsum; 6B4V; -. DR PDBsum; 6BOH; -. DR PDBsum; 6BOK; -. DR PDBsum; 6N1D; -. DR AlphaFoldDB; P62654; -. DR SMR; P62654; -. DR IntAct; P62654; 4. DR GeneID; 3168024; -. DR KEGG; tth:TT_C1302; -. DR eggNOG; COG0100; Bacteria. DR HOGENOM; CLU_072439_5_0_0; -. DR OrthoDB; 9806415at2; -. DR EvolutionaryTrace; P62654; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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; 3.30.420.80; Ribosomal protein S11; 1. DR HAMAP; MF_01310; Ribosomal_uS11; 1. DR InterPro; IPR001971; Ribosomal_uS11. DR InterPro; IPR019981; Ribosomal_uS11_bac-type. DR InterPro; IPR018102; Ribosomal_uS11_CS. DR InterPro; IPR036967; Ribosomal_uS11_sf. DR NCBIfam; TIGR03632; uS11_bact; 1. DR PANTHER; PTHR11759:SF3; 28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL; 1. DR PANTHER; PTHR11759; 40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11; 1. DR Pfam; PF00411; Ribosomal_S11; 1. DR PIRSF; PIRSF002131; Ribosomal_S11; 1. DR SUPFAM; SSF53137; Translational machinery components; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 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..129 FT /note="Small ribosomal subunit protein uS11" FT /id="PRO_0000123245" FT REGION 109..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT STRAND 15..23 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:4V84" FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 58..74 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 79..86 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 103..110 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:4V63" SQ SEQUENCE 129 AA; 13713 MW; 028E047E6DCE3CA2 CRC64; MAKKPSKKKV KRQVASGRAY IHASYNNTIV TITDPDGNPI TWSSGGVIGY KGSRKGTPYA AQLAALDAAK KAMAYGMQSV DVIVRGTGAG REQAIRALQA SGLQVKSIVD DTPVPHNGCR PKKKFRKAS //