ID RL23_ECOLI STANDARD; PRT; 100 AA. AC P0ADZ0; P02424; DT 21-JUL-1986 (Rel. 01, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE 50S ribosomal protein L23. GN Name=rplW; OrderedLocusNames=b3318; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=K12; RX MEDLINE=80092111; PubMed=391594; DOI=10.1016/0014-5793(79)81181-3; RA Wittmann-Liebold B., Greuer B.; RT "Primary structure of protein L23 from the Escherichia coli RT ribosome."; RL FEBS Lett. 108:69-74(1979). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85242118; PubMed=3892488; RA Zurawski G., Zurawski S.M.; RT "Structure of the Escherichia coli S10 ribosomal protein operon."; RL Nucleic Acids Res. 13:4521-4526(1985). RN [3] 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 [4] 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 [5] 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 to a specific region on the 23S rRNA. CC -!- FUNCTION: One of the proteins that surrounds the polypeptide exit CC tunnel on the outside of the subunit. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- INTERACTION: CC P30867:accA; NbExp=1; IntAct=EBI-542264, EBI-542031; CC P00837:atpG; NbExp=1; IntAct=EBI-542264, EBI-544306; CC P36996:cspC; NbExp=1; IntAct=EBI-542264, EBI-547832; CC P23304:deaD; NbExp=1; IntAct=EBI-542264, EBI-546193; CC P03004:dnaA; NbExp=1; IntAct=EBI-542264, EBI-548951; CC P03005:dnaB; NbExp=1; IntAct=EBI-542264, EBI-548978; CC P08622:dnaJ; NbExp=1; IntAct=EBI-542264, EBI-545285; CC P27430:dps; NbExp=1; IntAct=EBI-542264, EBI-549640; CC P39286:engC; NbExp=1; IntAct=EBI-542264, EBI-562672; CC P0A6R3:fis; NbExp=1; IntAct=EBI-542264, EBI-550170; CC P06982:gyrB; NbExp=1; IntAct=EBI-542264, EBI-541911; CC P28689:holE; NbExp=1; IntAct=EBI-542264, EBI-549182; CC P0A6Y1:ihfB; NbExp=1; IntAct=EBI-542264, EBI-551813; CC P07813:leuS; NbExp=1; IntAct=EBI-542264, EBI-553345; CC P07906:map; NbExp=1; IntAct=EBI-542264, EBI-553355; CC P33938:napD; NbExp=1; IntAct=EBI-542264, EBI-554985; CC P20625:nth; NbExp=1; IntAct=EBI-542264, EBI-555213; CC P16921:nusG; NbExp=1; IntAct=EBI-542264, EBI-369628; CC P39159:ppiC; NbExp=1; IntAct=EBI-542264, EBI-555953; CC P42184:prsA; NbExp=1; IntAct=EBI-542264, EBI-544466; CC P23830:pssA; NbExp=1; IntAct=EBI-542264, EBI-553760; CC P0A7E9:pyrH; NbExp=1; IntAct=EBI-542264, EBI-370182; CC P69405:rcsA; NbExp=1; IntAct=EBI-542264, EBI-556695; CC P21513:rne; NbExp=1; IntAct=EBI-542264, EBI-549958; CC P21499:rnr; NbExp=1; IntAct=EBI-542264, EBI-548136; CC P0A7L0:rplA; NbExp=1; IntAct=EBI-542264, EBI-543771; CC P60422:rplB; NbExp=1; IntAct=EBI-542264, EBI-543515; CC P60438:rplC; NbExp=1; IntAct=EBI-542264, EBI-542200; CC P60723:rplD; NbExp=1; IntAct=EBI-542264, EBI-545597; CC P62399:rplE; NbExp=1; IntAct=EBI-542264, EBI-545956; CC P02390:rplF; NbExp=1; IntAct=EBI-542264, EBI-546389; CC P0A7R1:rplI; NbExp=1; IntAct=EBI-542264, EBI-546437; CC P0A7J3:rplJ; NbExp=1; IntAct=EBI-542264, EBI-546827; CC P0A7J7:rplK; NbExp=1; IntAct=EBI-542264, EBI-547288; CC P0A7K2:rplL; NbExp=1; IntAct=EBI-542264, EBI-543702; CC P02410:rplM; NbExp=1; IntAct=EBI-542264, EBI-543801; CC P02413:rplO; NbExp=1; IntAct=EBI-542264, EBI-543017; CC P02419:rplR; NbExp=1; IntAct=EBI-542264, EBI-542207; CC P0A7K6:rplS; NbExp=1; IntAct=EBI-542264, EBI-543891; CC P02422:rplU; NbExp=1; IntAct=EBI-542264, EBI-542445; CC P61175:rplV; NbExp=1; IntAct=EBI-542264, EBI-542255; CC P60624:rplX; NbExp=1; IntAct=EBI-542264, EBI-546481; CC P68919:rplY; NbExp=1; IntAct=EBI-542264, EBI-553087; CC P0A7M2:rpmB; NbExp=1; IntAct=EBI-542264, EBI-543024; CC P0A7M6:rpmC; NbExp=1; IntAct=EBI-542264, EBI-546493; CC P0A7N9:rpmG; NbExp=1; IntAct=EBI-542264, EBI-542475; CC P0A7Z4:rpoA; NbExp=1; IntAct=EBI-542264, EBI-544985; CC P0A800:rpoZ; NbExp=1; IntAct=EBI-542264, EBI-370560; CC P0A7V3:rpsC; NbExp=1; IntAct=EBI-542264, EBI-544851; CC P10408:secA; NbExp=1; IntAct=EBI-542264, EBI-543213; CC P15082:srlR; NbExp=1; IntAct=EBI-542264, EBI-558448; CC P21507:srmB; NbExp=1; IntAct=EBI-542264, EBI-546628; CC P0A850:tig; NbExp=1; IntAct=EBI-542264, EBI-544862; CC P39177:uspG; NbExp=1; IntAct=EBI-542264, EBI-561722; CC P03018:uvrD; NbExp=1; IntAct=EBI-542264, EBI-559573; CC P08999:ybgC; NbExp=1; IntAct=EBI-542264, EBI-543276; CC P75767:ybhK; NbExp=1; IntAct=EBI-542264, EBI-550390; CC P36979:yfgB; NbExp=1; IntAct=EBI-542264, EBI-559071; CC P52126:yfjK; NbExp=1; IntAct=EBI-542264, EBI-560956; CC P23839:yicC; NbExp=1; IntAct=EBI-542264, EBI-558867; CC P39336:yjgL; NbExp=1; IntAct=EBI-542264, EBI-549937; CC P45748:yrdC; NbExp=1; IntAct=EBI-542264, EBI-554067; CC -!- MASS SPECTROMETRY: MW=11198.0; METHOD=MALDI; RANGE=1-100; CC NOTE=Ref.4. CC -!- SIMILARITY: Belongs to the ribosomal protein L23P 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; X02613; CAA26462.1; -; Genomic_DNA. DR EMBL; U18997; AAA58115.1; -; Genomic_DNA. DR EMBL; U00096; AAC76343.1; -; Genomic_DNA. DR PIR; A65125; R5EC23. DR PDB; 1P85; EM; R=1-100. DR PDB; 1P86; EM; R=1-100. DR ECO2DBASE; I013.0; 6TH EDITION. DR EchoBASE; EB0876; -. DR EcoGene; EG10883; rplW. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR012677; a_b_plait_nuc_bd. DR InterPro; IPR012678; L23_L15e_core. DR InterPro; IPR001014; Ribosomal_L23. DR Pfam; PF00276; Ribosomal_L23; 1. DR ProDom; PD001141; Ribosomal_L23; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CONFLICT 80 80 Missing (in Ref. 1). SQ SEQUENCE 100 AA; 11199 MW; 30CD1D77CC7CF9EB CRC64; MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE //