ID RL23_ECOLI Reviewed; 100 AA. AC P0ADZ0; P02424; Q2M6Y3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 22-SEP-2009, entry version 43. DE RecName: Full=50S ribosomal protein L23; GN Name=rplW; OrderedLocusNames=b3318, JW3280; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; 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; DOI=10.1093/nar/13.12.4521; 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 / ATCC 47076; 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 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 CROSS-LINKING TO 23S RRNA. RC STRAIN=MRE-600; RX PubMed=6170935; DOI=10.1093/nar/9.17.4285; RA Wower I., Wower J., Meinke M., Brimacombe R.; RT "The use of 2-iminothiolane as an RNA-protein cross-linking agent in RT Escherichia coli ribosomes, and the localisation on 23S RNA of sites RT cross-linked to proteins L4, L6, L21, L23, L27 and L29."; RL Nucleic Acids Res. 9:4285-4302(1981). RN [6] RP ASSEMBLY MAP OF THE 50S SUBUNIT. RC STRAIN=K12; RX MEDLINE=87250508; PubMed=3298242; RA Herold M., Nierhaus K.H.; RT "Incorporation of six additional proteins to complete the assembly map RT of the 50 S subunit from Escherichia coli ribosomes."; RL J. Biol. Chem. 262:8826-8833(1987). RN [7] RP CROSS-LINKING TO L29. RX PubMed=2665813; DOI=10.1021/bi00435a071; RA Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.; RT "Comparative cross-linking study on the 50S ribosomal subunit from RT Escherichia coli."; RL Biochemistry 28:4099-4105(1989). RN [8] RP BINDING TO TRIGGER FACTOR, AND MUTAGENESIS OF 16-VAL--GLU-18; GLU-18; RP 51-PHE--VAL-53 AND GLU-52. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=12226666; DOI=10.1038/nature01047; RA Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., RA Schulze-Specking A., Ban N., Deuerling E., Bukau B.; RT "L23 protein functions as a chaperone docking site on the ribosome."; RL Nature 419:171-174(2002). RN [9] RP CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN RP CHAINS. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=12756233; DOI=10.1083/jcb.200302130; RA Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., RA Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.; RT "Interplay of signal recognition particle and trigger factor at L23 RT near the nascent chain exit site on the Escherichia coli ribosome."; RL J. Cell Biol. 161:679-684(2003). RN [10] RP IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RP RECOGNITION PARTICLE. RC STRAIN=MRE-600; RX PubMed=12702815; DOI=10.1261/rna.2196403; RA Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.; RT "The signal recognition particle binds to protein L23 at the peptide RT exit of the Escherichia coli ribosome."; RL RNA 9:566-573(2003). RN [11] RP MASS SPECTROMETRY. RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290; 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 [12] 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). RN [13] 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: One of the early assembly protein, it binds 23S rRNA; is CC essential for growth. One of the proteins that surrounds the CC polypeptide exit tunnel on the outside of the subunit. Acts as the CC docking site for trigger factor (PubMed:12226666) for Ffh binding CC to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and CC to nascent polypeptide chains (PubMed:12756233). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29 CC and trigger factor. CC -!- INTERACTION: CC P0A7W1:rpsE; NbExp=1; IntAct=EBI-542264, EBI-543949; CC P0A8Z3:ybgC; NbExp=1; IntAct=EBI-542264, EBI-543276; CC P39336:yjgL; NbExp=1; IntAct=EBI-542264, EBI-549937; CC -!- MASS SPECTROMETRY: Mass=11198.0; Method=MALDI; Range=1-100; CC Source=PubMed:10094780; 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 EMBL; AP009048; BAE77973.1; -; Genomic_DNA. DR PIR; A65125; R5EC23. DR RefSeq; AP_004472.1; -. DR RefSeq; NP_417777.1; -. DR PDB; 1P85; EM; 12.30 A; R=1-100. DR PDB; 1P86; EM; 11.50 A; R=1-100. DR PDB; 1VS6; X-ray; 3.46 A; T=1-100. DR PDB; 1VS8; X-ray; 3.46 A; T=1-100. DR PDB; 2AW4; X-ray; 3.46 A; T=1-100. DR PDB; 2AWB; X-ray; 3.46 A; T=1-100. DR PDB; 2GYA; EM; 2.00 A; R=7-98. DR PDB; 2GYC; EM; -; R=7-98. DR PDB; 2I2T; X-ray; 3.22 A; T=1-100. DR PDB; 2I2V; X-ray; 3.22 A; T=1-100. DR PDB; 2J28; EM; 8.00 A; T=1-99. DR PDB; 2QAM; X-ray; 3.21 A; T=1-100. DR PDB; 2QAO; X-ray; 3.21 A; T=1-100. DR PDB; 2QBA; X-ray; 3.54 A; T=1-100. DR PDB; 2QBC; X-ray; 3.54 A; T=1-100. DR PDB; 2QBE; X-ray; 3.30 A; T=1-100. DR PDB; 2QBG; X-ray; 3.30 A; T=1-100. DR PDB; 2QBI; X-ray; 4.00 A; T=1-100. DR PDB; 2QBK; X-ray; 4.00 A; T=1-100. DR PDB; 2QOV; X-ray; 3.93 A; T=1-100. DR PDB; 2QOX; X-ray; 3.93 A; T=1-100. DR PDB; 2QOZ; X-ray; 3.50 A; T=1-100. DR PDB; 2QP1; X-ray; 3.50 A; T=1-100. DR PDB; 2RDO; EM; 9.10 A; T=1-100. DR PDB; 2Z4L; X-ray; 4.45 A; T=1-100. DR PDB; 2Z4N; X-ray; 4.45 A; T=1-100. DR PDB; 3BBX; EM; -; T=1-100. DR PDB; 3FIK; EM; -; T=1-93. DR PDBsum; 1P85; -. DR PDBsum; 1P86; -. DR PDBsum; 1VS6; -. DR PDBsum; 1VS8; -. DR PDBsum; 2AW4; -. DR PDBsum; 2AWB; -. DR PDBsum; 2GYA; -. DR PDBsum; 2GYC; -. DR PDBsum; 2I2T; -. DR PDBsum; 2I2V; -. DR PDBsum; 2J28; -. DR PDBsum; 2QAM; -. DR PDBsum; 2QAO; -. DR PDBsum; 2QBA; -. DR PDBsum; 2QBC; -. DR PDBsum; 2QBE; -. DR PDBsum; 2QBG; -. DR PDBsum; 2QBI; -. DR PDBsum; 2QBK; -. DR PDBsum; 2QOV; -. DR PDBsum; 2QOX; -. DR PDBsum; 2QOZ; -. DR PDBsum; 2QP1; -. DR PDBsum; 2RDO; -. DR PDBsum; 2Z4L; -. DR PDBsum; 2Z4N; -. DR PDBsum; 3BBX; -. DR PDBsum; 3FIK; -. DR IntAct; P0ADZ0; 73. DR STRING; P0ADZ0; -. DR ECO2DBASE; I013.0; 6TH EDITION. DR PRIDE; P0ADZ0; -. DR GeneID; 947819; -. DR GenomeReviews; AP009048_GR; JW3280. DR GenomeReviews; U00096_GR; b3318. DR KEGG; ecj:JW3280; -. DR KEGG; eco:b3318; -. DR EchoBASE; EB0876; -. DR EcoGene; EG10883; rplW. DR HOGENOM; P0ADZ0; -. DR OMA; P0ADZ0; VSEKATM. DR BioCyc; EcoCyc:EG10883-MON; -. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019843; F:rRNA binding; IEA:HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:HAMAP. DR HAMAP; MF_01369; -; 1. DR InterPro; IPR012677; a_b_plait_nuc_bd. DR InterPro; IPR001014; Ribosomal_L23/L25_CS. DR InterPro; IPR013025; Ribosomal_L25/23. DR Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1. DR Pfam; PF00276; Ribosomal_L23; 1. DR ProDom; PD001141; Ribosomal_L23; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 100 50S ribosomal protein L23. FT /FTId=PRO_0000129407. FT MUTAGEN 16 18 VSE->AAA: Strongly reduces trigger factor FT binding. FT MUTAGEN 18 18 E->A: Binds normally to ribosomes; FT strongly reduces trigger factor binding. FT MUTAGEN 18 18 E->Q: Strongly reduces trigger factor FT binding. FT MUTAGEN 51 53 FEV->AAA: No effect on trigger factor FT binding. FT MUTAGEN 52 52 E->K: No effect on trigger factor FT binding. FT CONFLICT 80 80 Missing (in Ref. 1; AA sequence). FT TURN 4 6 FT HELIX 7 9 FT TURN 20 22 FT STRAND 25 27 FT HELIX 40 49 FT TURN 50 52 FT STRAND 70 73 SQ SEQUENCE 100 AA; 11199 MW; 30CD1D77CC7CF9EB CRC64; MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE //