ID RS18_ECOLI Reviewed; 75 AA. AC P0A7T7; P02374; Q2M6A3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 29-APR-2015, entry version 106. DE RecName: Full=30S ribosomal protein S18; GN Name=rpsR; OrderedLocusNames=b4202, JW4160; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3528756; DOI=10.1007/BF00330199; RA Schnier J., Kitakawa M., Isono K.; RT "The nucleotide sequence of an Escherichia coli chromosomal region RT containing the genes for ribosomal proteins S6, S18, L9 and an open RT reading frame."; RL Mol. Gen. Genet. 204:126-132(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., RA Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the RT region from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 2-75. RC STRAIN=K; RX PubMed=776663; DOI=10.1016/0014-5793(75)80378-4; RA Yaguchi M.; RT "Primary structure of protein S18 from the small Escherichia coli RT ribosomal subunit."; RL FEBS Lett. 59:217-220(1975). RN [6] RP PROTEIN SEQUENCE OF 31-38, AND CROSS-LINKING TO RRNA. RC STRAIN=MRE-600; RX PubMed=7556101; RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.; RT "Protein-rRNA binding features and their structural and functional RT implications in ribosomes as determined by cross-linking studies."; RL EMBO J. 14:4578-4588(1995). RN [7] RP MASS SPECTROMETRY. RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290; RX PubMed=10094780; DOI=10.1006/abio.1998.3077; RA Arnold R.J., Reilly J.P.; RT "Observation of Escherichia coli ribosomal proteins and their RT posttranslational modifications by mass spectrometry."; RL Anal. Biochem. 269:105-112(1999). RN [8] RP 3D-STRUCTURE MODELING. RX PubMed=12244297; DOI=10.1038/nsb841; RA Tung C.-S., Joseph S., Sanbonmatsu K.Y.; RT "All-atom homology model of the Escherichia coli 30S ribosomal RT subunit."; RL Nat. Struct. Biol. 9:750-755(2002). RN [9] RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). RC STRAIN=MRE-600; RX PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6; RA Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., RA Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., RA Frank J.; RT "Study of the structural dynamics of the E. coli 70S ribosome using RT real-space refinement."; RL Cell 113:789-801(2003). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME RP STRUCTURES. RC STRAIN=MRE-600; RX PubMed=16272117; DOI=10.1126/science.1117230; RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., RA Vila-Sanjurjo A., Holton J.M., Cate J.H.D.; RT "Structures of the bacterial ribosome at 3.5 A resolution."; RL Science 310:827-834(2005). CC -!- FUNCTION: Binds as a heterodimer with protein S6 to the central CC domain of the 16S rRNA, where it helps stabilize the platform of CC the 30S subunit. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight CC heterodimer with protein S6. CC -!- INTERACTION: CC P02358:rpsF; NbExp=4; IntAct=EBI-548844, EBI-543068; CC -!- MASS SPECTROMETRY: Mass=8897.0; Method=MALDI; Range=2-75; CC Evidence={ECO:0000269|PubMed:10094780}; CC -!- SIMILARITY: Belongs to the ribosomal protein S18P 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; X04022; CAA27654.1; -; Genomic_DNA. DR EMBL; U14003; AAA97098.1; -; Genomic_DNA. DR EMBL; U00096; AAC77159.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78203.1; -; Genomic_DNA. DR PIR; S56427; R3EC18. DR RefSeq; NP_418623.1; NC_000913.3. DR RefSeq; YP_492344.1; NC_007779.1. DR PDB; 1M5G; Model; -; R=5-75. DR PDB; 2YKR; EM; 9.80 A; R=20-74. DR PDB; 4A2I; EM; 16.50 A; R=20-74. DR PDB; 4ADV; EM; 13.50 A; R=2-75. DR PDB; 4U1U; X-ray; 2.95 A; AR/CR=20-74. DR PDB; 4U1V; X-ray; 3.00 A; AR/CR=20-74. DR PDB; 4U20; X-ray; 2.90 A; AR/CR=20-74. DR PDB; 4U24; X-ray; 2.90 A; AR/CR=20-74. DR PDB; 4U25; X-ray; 2.90 A; AR/CR=20-74. DR PDB; 4U26; X-ray; 2.80 A; AR/CR=20-74. DR PDB; 4U27; X-ray; 2.80 A; AR/CR=20-74. DR PDB; 4V47; EM; 12.30 A; BR=2-75. DR PDB; 4V48; EM; 11.50 A; BR=2-75. DR PDB; 4V4H; X-ray; 3.46 A; AR/CR=1-75. DR PDB; 4V4Q; X-ray; 3.46 A; AR/CR=2-75. DR PDB; 4V4V; EM; 15.00 A; AR=7-75. DR PDB; 4V4W; EM; 15.00 A; AR=7-75. DR PDB; 4V50; X-ray; 3.22 A; AR/CR=2-75. DR PDB; 4V52; X-ray; 3.21 A; AR/CR=2-75. DR PDB; 4V53; X-ray; 3.54 A; AR/CR=2-75. DR PDB; 4V54; X-ray; 3.30 A; AR/CR=2-75. DR PDB; 4V55; X-ray; 4.00 A; AR/CR=2-75. DR PDB; 4V56; X-ray; 3.93 A; AR/CR=2-75. DR PDB; 4V57; X-ray; 3.50 A; AR/CR=2-75. DR PDB; 4V5B; X-ray; 3.74 A; BR/DR=2-75. DR PDB; 4V5H; EM; 5.80 A; AR=20-74. DR PDB; 4V5Y; X-ray; 4.45 A; AR/CR=2-75. DR PDB; 4V64; X-ray; 3.50 A; AR/CR=2-75. DR PDB; 4V65; EM; 9.00 A; AK=1-75. DR PDB; 4V66; EM; 9.00 A; AK=1-75. DR PDB; 4V69; EM; 6.70 A; AR=20-74. DR PDB; 4V6C; X-ray; 3.19 A; AR/CR=1-75. DR PDB; 4V6D; X-ray; 3.81 A; AR/CR=1-75. DR PDB; 4V6E; X-ray; 3.71 A; AR/CR=1-75. DR PDB; 4V6K; EM; 8.25 A; BV=1-75. DR PDB; 4V6L; EM; 13.20 A; AV=1-75. DR PDB; 4V6M; EM; 7.10 A; AR=2-75. DR PDB; 4V6N; EM; 12.10 A; BU=2-75. DR PDB; 4V6O; EM; 14.70 A; AU=2-75. DR PDB; 4V6P; EM; 13.50 A; AU=2-75. DR PDB; 4V6Q; EM; 11.50 A; AU=2-75. DR PDB; 4V6R; EM; 11.50 A; AU=2-75. DR PDB; 4V6S; EM; 13.10 A; BT=2-75. DR PDB; 4V6T; EM; 8.30 A; AR=20-74. DR PDB; 4V6V; EM; 9.80 A; R=2-75. DR PDB; 4V6Y; EM; 12.00 A; AR=20-74. DR PDB; 4V6Z; EM; 12.00 A; AR=20-74. DR PDB; 4V70; EM; 17.00 A; AR=20-74. DR PDB; 4V71; EM; 20.00 A; AR=20-74. DR PDB; 4V72; EM; 13.00 A; AR=20-74. DR PDB; 4V73; EM; 15.00 A; AR=20-74. DR PDB; 4V74; EM; 17.00 A; AR=20-74. DR PDB; 4V75; EM; 12.00 A; AR=20-74. DR PDB; 4V76; EM; 17.00 A; AR=20-74. DR PDB; 4V77; EM; 17.00 A; AR=20-74. DR PDB; 4V78; EM; 20.00 A; AR=20-74. DR PDB; 4V79; EM; 15.00 A; AR=20-74. DR PDB; 4V7A; EM; 9.00 A; AR=20-74. DR PDB; 4V7B; EM; 6.80 A; AR=1-75. DR PDB; 4V7C; EM; 7.60 A; AR=2-75. DR PDB; 4V7D; EM; 7.60 A; BR=2-75. DR PDB; 4V7I; EM; 9.60 A; BR=1-75. DR PDB; 4V7S; X-ray; 3.25 A; AR/CR=20-74. DR PDB; 4V7T; X-ray; 3.19 A; AR/CR=20-74. DR PDB; 4V7U; X-ray; 3.10 A; AR/CR=20-74. DR PDB; 4V7V; X-ray; 3.29 A; AR/CR=20-74. DR PDB; 4V85; X-ray; 3.20 A; R=1-75. DR PDB; 4V89; X-ray; 3.70 A; AR=1-75. DR PDB; 4V9C; X-ray; 3.30 A; AR/CR=1-75. DR PDB; 4V9D; X-ray; 3.00 A; AR/BR=20-74. DR PDB; 4V9O; X-ray; 2.90 A; BR/DR/FR/HR=1-75. DR PDB; 4V9P; X-ray; 2.90 A; BR/DR/FR/HR=1-75. DR PDB; 4WF1; X-ray; 3.09 A; AR/CR=20-74. DR PDB; 4WWW; X-ray; 3.10 A; QR/XR=20-74. DR PDB; 5AFI; EM; 2.90 A; r=1-75. DR PDBsum; 1M5G; -. DR PDBsum; 2YKR; -. DR PDBsum; 4A2I; -. DR PDBsum; 4ADV; -. DR PDBsum; 4U1U; -. DR PDBsum; 4U1V; -. DR PDBsum; 4U20; -. DR PDBsum; 4U24; -. DR PDBsum; 4U25; -. DR PDBsum; 4U26; -. DR PDBsum; 4U27; -. DR PDBsum; 4V47; -. DR PDBsum; 4V48; -. DR PDBsum; 4V4H; -. DR PDBsum; 4V4Q; -. DR PDBsum; 4V4V; -. DR PDBsum; 4V4W; -. DR PDBsum; 4V50; -. DR PDBsum; 4V52; -. DR PDBsum; 4V53; -. DR PDBsum; 4V54; -. DR PDBsum; 4V55; -. DR PDBsum; 4V56; -. DR PDBsum; 4V57; -. DR PDBsum; 4V5B; -. DR PDBsum; 4V5H; -. DR PDBsum; 4V5Y; -. DR PDBsum; 4V64; -. DR PDBsum; 4V65; -. DR PDBsum; 4V66; -. DR PDBsum; 4V69; -. DR PDBsum; 4V6C; -. DR PDBsum; 4V6D; -. DR PDBsum; 4V6E; -. DR PDBsum; 4V6K; -. DR PDBsum; 4V6L; -. DR PDBsum; 4V6M; -. DR PDBsum; 4V6N; -. DR PDBsum; 4V6O; -. DR PDBsum; 4V6P; -. DR PDBsum; 4V6Q; -. DR PDBsum; 4V6R; -. DR PDBsum; 4V6S; -. DR PDBsum; 4V6T; -. DR PDBsum; 4V6V; -. DR PDBsum; 4V6Y; -. DR PDBsum; 4V6Z; -. DR PDBsum; 4V70; -. DR PDBsum; 4V71; -. DR PDBsum; 4V72; -. DR PDBsum; 4V73; -. DR PDBsum; 4V74; -. DR PDBsum; 4V75; -. DR PDBsum; 4V76; -. DR PDBsum; 4V77; -. DR PDBsum; 4V78; -. DR PDBsum; 4V79; -. DR PDBsum; 4V7A; -. DR PDBsum; 4V7B; -. DR PDBsum; 4V7C; -. DR PDBsum; 4V7D; -. DR PDBsum; 4V7I; -. DR PDBsum; 4V7S; -. DR PDBsum; 4V7T; -. DR PDBsum; 4V7U; -. DR PDBsum; 4V7V; -. DR PDBsum; 4V85; -. DR PDBsum; 4V89; -. DR PDBsum; 4V9C; -. DR PDBsum; 4V9D; -. DR PDBsum; 4V9O; -. DR PDBsum; 4V9P; -. DR PDBsum; 4WF1; -. DR PDBsum; 4WWW; -. DR PDBsum; 5AFI; -. DR DisProt; DP00146; -. DR ProteinModelPortal; P0A7T7; -. DR SMR; P0A7T7; 2-75. DR DIP; DIP-47889N; -. DR IntAct; P0A7T7; 26. DR MINT; MINT-1247424; -. DR STRING; 511145.b4202; -. DR ChEMBL; CHEMBL2363135; -. DR PaxDb; P0A7T7; -. DR PRIDE; P0A7T7; -. DR EnsemblBacteria; AAC77159; AAC77159; b4202. DR EnsemblBacteria; BAE78203; BAE78203; BAE78203. DR GeneID; 12930640; -. DR GeneID; 948721; -. DR KEGG; ecj:Y75_p4088; -. DR KEGG; eco:b4202; -. DR PATRIC; 32123979; VBIEscCol129921_4334. DR EchoBASE; EB0910; -. DR EcoGene; EG10917; rpsR. DR eggNOG; COG0238; -. DR HOGENOM; HOG000218466; -. DR InParanoid; P0A7T7; -. DR KO; K02963; -. DR OMA; YRRRKSC; -. DR OrthoDB; EOG6PCQ4R; -. DR PhylomeDB; P0A7T7; -. DR BioCyc; EcoCyc:EG10917-MONOMER; -. DR BioCyc; ECOL316407:JW4160-MONOMER; -. DR EvolutionaryTrace; P0A7T7; -. DR PRO; PR:P0A7T7; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR Genevestigator; P0A7T7; -. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:EcoCyc. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 4.10.640.10; -; 1. DR HAMAP; MF_00270; Ribosomal_S18; 1. DR InterPro; IPR001648; Ribosomal_S18. DR InterPro; IPR018275; Ribosomal_S18_CS. DR PANTHER; PTHR13479; PTHR13479; 1. DR Pfam; PF01084; Ribosomal_S18; 1. DR PRINTS; PR00974; RIBOSOMALS18. DR ProDom; PD002239; Ribosomal_S18; 1. DR SUPFAM; SSF46911; SSF46911; 1. DR TIGRFAMs; TIGR00165; S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:776663}. FT CHAIN 2 75 30S ribosomal protein S18. FT /FTId=PRO_0000111153. FT MOD_RES 2 2 N-acetylalanine. FT CONFLICT 24 24 K -> E (in Ref. 5; AA sequence). FT {ECO:0000305}. FT STRAND 22 24 {ECO:0000244|PDB:4V50}. FT HELIX 26 29 {ECO:0000244|PDB:4U26}. FT HELIX 30 32 {ECO:0000244|PDB:4U26}. FT STRAND 37 39 {ECO:0000244|PDB:4V52}. FT HELIX 42 45 {ECO:0000244|PDB:4U26}. FT HELIX 49 64 {ECO:0000244|PDB:4U26}. FT TURN 65 67 {ECO:0000244|PDB:4V9C}. FT STRAND 70 72 {ECO:0000244|PDB:4U26}. SQ SEQUENCE 75 AA; 8986 MW; AB2E8288901B73B8 CRC64; MARYFRRRKF CRFTAEGVQE IDYKDIATLK NYITESGKIV PSRITGTRAK YQRQLARAIK RARYLSLLPY TDRHQ //