ID RS18_ECOLI STANDARD; PRT; 74 AA. AC P0A7T7; P02374; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE 30S ribosomal protein S18. GN Name=rpsR; OrderedLocusNames=b4202; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=K; RX MEDLINE=76210737; 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 [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=86310297; 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 [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K12 / MG1655; RX MEDLINE=95334362; PubMed=7610040; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; 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 277:1453-1474(1997). RN [5] RP PROTEIN SEQUENCE OF 30-37, AND CROSS-LINKING TO RRNA. RC STRAIN=MRE-600; RX MEDLINE=96003638; 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 [6] RP MASS SPECTROMETRY. RC STRAIN=K12 / ATCC 25404; RX MEDLINE=99196679; 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 [7] RP 3D-STRUCTURE MODELING. RX MEDLINE=22239879; 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 [8] RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). RC STRAIN=MRE-600; RX MEDLINE=22694394; 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). 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 P23304:deaD; NbExp=1; IntAct=EBI-548844, EBI-546193; CC P0A6Q3:fabA; NbExp=1; IntAct=EBI-548844, EBI-369375; CC P04742:fimB; NbExp=1; IntAct=EBI-548844, EBI-550135; CC P0A6X3:hfq; NbExp=1; IntAct=EBI-548844, EBI-547637; CC P0A707:infC; NbExp=1; IntAct=EBI-548844, EBI-546262; CC P21645:lpxD; NbExp=1; IntAct=EBI-548844, EBI-542924; CC P68739:nfi; NbExp=1; IntAct=EBI-548844, EBI-551698; CC P0A776:nudH; NbExp=1; IntAct=EBI-548844, EBI-562338; CC P05055:pnp; NbExp=1; IntAct=EBI-548844, EBI-548080; CC P37765:rluB; NbExp=1; IntAct=EBI-548844, EBI-561550; CC P23851:rluC; NbExp=1; IntAct=EBI-548844, EBI-561528; CC P0A7Y8:rnpA; NbExp=1; IntAct=EBI-548844, EBI-557396; CC P21499:rnr; NbExp=1; IntAct=EBI-548844, EBI-548136; CC P17580:spoT; NbExp=1; IntAct=EBI-548844, EBI-543228; CC P0A8G0:uvrC; NbExp=1; IntAct=EBI-548844, EBI-559448; CC P36979:yfgB; NbExp=1; IntAct=EBI-548844, EBI-559071; CC P33635:yfiF; NbExp=1; IntAct=EBI-548844, EBI-547368; CC -!- MASS SPECTROMETRY: MW=8897.0; METHOD=MALDI; RANGE=1-74; CC NOTE=Ref.6. CC -!- SIMILARITY: Belongs to the ribosomal protein S18P family. 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 PIR; S56427; R3EC18. DR PDB; 1P6G; EM; R=1-74. DR PDB; 1P87; EM; R=1-74. DR IntAct; P0A7T7; -. DR EchoBASE; EB0910; -. DR EcoGene; EG10917; rpsR. DR HAMAP; MF_00270; -; 1. DR InterPro; IPR001648; Ribosomal_S18. DR Pfam; PF01084; Ribosomal_S18; 1. DR PRINTS; PR00974; RIBOSOMALS18. DR ProDom; PD002239; Ribosomal_S18; 1. DR TIGRFAMs; TIGR00165; S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding. FT INIT_MET 0 0 FT MOD_RES 1 1 N-acetylalanine. FT CONFLICT 23 23 K -> E (in Ref. 1). SQ SEQUENCE 74 AA; 8855 MW; AB2EDDEEA9441581 CRC64; ARYFRRRKFC RFTAEGVQEI DYKDIATLKN YITESGKIVP SRITGTRAKY QRQLARAIKR ARYLSLLPYT DRHQ //