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 30-NOV-2010, entry version 57. 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 POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX. RC STRAIN=MRE-600; RX PubMed=16292303; DOI=10.1038/nature04133; RA Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., RA Brooks C.L. III, Ban N., Frank J.; RT "Structure of the E. coli protein-conducting channel bound to a RT translating ribosome."; RL Nature 438:318-324(2005). RN [13] 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 [14] 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 proteins, it binds 23S rRNA; CC is essential for growth. One of the proteins that surround 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. Might also contact SecE and probably does CC contact SecG when the SecYEG translocation complex is docked with CC the ribosome. 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; AC_000091.1. DR RefSeq; NP_417777.1; NC_000913.2. 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; 15.00 A; R=7-98. DR PDB; 2GYC; EM; 15.00 A; 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; 2WWQ; EM; 5.80 A; T=1-93. 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; 10.00 A; T=1-100. DR PDB; 3E1B; EM; -; M=1-99. DR PDB; 3E1D; EM; -; M=1-99. DR PDB; 3FIK; EM; 6.70 A; T=1-93. DR PDB; 3I1N; X-ray; 3.19 A; T=1-100. DR PDB; 3I1P; X-ray; 3.19 A; T=1-100. DR PDB; 3I1R; X-ray; 3.81 A; T=1-100. DR PDB; 3I1T; X-ray; 3.81 A; T=1-100. DR PDB; 3I20; X-ray; 3.71 A; T=1-100. DR PDB; 3I22; X-ray; 3.71 A; T=1-100. DR PDB; 3KCR; EM; -; T=1-100. 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; 2WWQ; -. DR PDBsum; 2Z4L; -. DR PDBsum; 2Z4N; -. DR PDBsum; 3BBX; -. DR PDBsum; 3E1B; -. DR PDBsum; 3E1D; -. DR PDBsum; 3FIK; -. DR PDBsum; 3I1N; -. DR PDBsum; 3I1P; -. DR PDBsum; 3I1R; -. DR PDBsum; 3I1T; -. DR PDBsum; 3I20; -. DR PDBsum; 3I22; -. DR PDBsum; 3KCR; -. DR ProteinModelPortal; P0ADZ0; -. DR SMR; P0ADZ0; 1-99. DR DIP; DIP-35972N; -. DR IntAct; P0ADZ0; 77. DR MINT; MINT-1225825; -. DR STRING; P0ADZ0; -. DR ECO2DBASE; I013.0; 6TH EDITION. DR EnsemblBacteria; EBESCT00000003161; EBESCP00000003161; EBESCG00000002594. DR EnsemblBacteria; EBESCT00000014267; EBESCP00000013558; EBESCG00000013329. 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 eggNOG; COG0089; -. DR HOGENOM; HBG439330; -. DR OMA; WKKAYVS; -. DR ProtClustDB; PRK05738; -. DR BioCyc; EcoCyc:EG10883-MONOMER; -. DR Genevestigator; P0ADZ0; -. 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:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1; -. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR012678; Ribosomal_L23/L15e. 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 SUPFAM; SSF54189; L23_L15e_core; 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 //