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 10-AUG-2010, entry version 54.
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 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.
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.
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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; 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 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; a_b_plait_nuc-bd.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core.
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
//