ID RS14Z_THET2 Reviewed; 61 AA. AC P62656; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 118. DE RecName: Full=Small ribosomal subunit protein uS14 {ECO:0000255|HAMAP-Rule:MF_01364}; DE AltName: Full=30S ribosomal protein S14 type Z {ECO:0000305}; GN Name=rpsZ {ECO:0000255|HAMAP-Rule:MF_01364}; GN Synonyms=rps14 {ECO:0000255|HAMAP-Rule:MF_01364}, rpsN GN {ECO:0000255|HAMAP-Rule:MF_01364}; OrderedLocusNames=TT_C1315; 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: Binds 16S rRNA, required for the assembly of 30S particles CC and may also be responsible for determining the conformation of the 16S CC rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01364}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01364}; CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 and CC S10. {ECO:0000255|HAMAP-Rule:MF_01364}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family. CC Zinc-binding uS14 subfamily. {ECO:0000255|HAMAP-Rule:MF_01364}. 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; AAS81657.1; -; Genomic_DNA. DR RefSeq; WP_008633399.1; NZ_CP133179.1. DR PDB; 4KVB; X-ray; 4.20 A; N=1-61. DR PDB; 4V4J; X-ray; 3.83 A; o=1-61. DR PDB; 4V63; X-ray; 3.21 A; AN/CN=1-61. DR PDB; 4V67; X-ray; 3.00 A; AN/CN=1-61. DR PDB; 4V7P; X-ray; 3.62 A; AN/DN=2-61. DR PDB; 4V83; X-ray; 3.50 A; AN/CN=2-61. DR PDB; 4V84; X-ray; 3.40 A; AN/CN=2-61. DR PDB; 4V9J; X-ray; 3.86 A; AN/CN=2-61. DR PDB; 4V9K; X-ray; 3.50 A; AN/CN=2-61. DR PDB; 4V9L; X-ray; 3.50 A; AN/CN=2-61. DR PDB; 4V9M; X-ray; 4.00 A; AN/CN=2-61. DR PDB; 4V9N; X-ray; 3.40 A; AN/CN=2-61. DR PDB; 4V9Q; X-ray; 3.40 A; BN/DN=2-61. DR PDB; 4W29; X-ray; 3.80 A; AN/CN=2-61. DR PDB; 4XEJ; X-ray; 3.80 A; AS14/BS14=2-61. DR PDB; 5J4D; X-ray; 3.10 A; BD/WA=1-61. DR PDB; 5V8I; X-ray; 3.25 A; 1n/2n=1-61. DR PDB; 6B4V; X-ray; 3.40 A; AD/WA=1-61. DR PDB; 6BOH; X-ray; 3.40 A; CD/XA=1-61. DR PDB; 6BOK; X-ray; 3.55 A; VA/YC=1-61. DR PDB; 6N1D; X-ray; 3.20 A; AS14/BS14=2-61. DR PDBsum; 4KVB; -. 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; P62656; -. DR SMR; P62656; -. DR IntAct; P62656; 4. DR GeneID; 3169802; -. DR KEGG; tth:TT_C1315; -. DR eggNOG; COG0199; Bacteria. DR HOGENOM; CLU_139869_3_0_0; -. DR OrthoDB; 9810484at2; -. DR EvolutionaryTrace; P62656; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR HAMAP; MF_01364_B; Ribosomal_uS14_2_B; 1. DR InterPro; IPR001209; Ribosomal_uS14. DR InterPro; IPR023053; Ribosomal_uS14_bact. DR InterPro; IPR018271; Ribosomal_uS14_CS. DR InterPro; IPR043140; Ribosomal_uS14_sf. DR PANTHER; PTHR19836:SF19; 28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL; 1. DR PANTHER; PTHR19836; 30S RIBOSOMAL PROTEIN S14; 1. DR Pfam; PF00253; Ribosomal_S14; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR PROSITE; PS00527; RIBOSOMAL_S14; 1. PE 1: Evidence at protein level; KW 3D-structure; Metal-binding; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..61 FT /note="Small ribosomal subunit protein uS14" FT /id="PRO_0000130954" FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01364" FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01364" FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01364" FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01364" FT HELIX 4..12 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 35..38 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 41..50 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:4V63" SQ SEQUENCE 61 AA; 7140 MW; BEE8AB1E1E86B531 CRC64; MARKALIEKA KRTPKFKVRA YTRCVRCGRA RSVYRFFGLC RICLRELAHK GQLPGVRKAS W //