GenomeNet

Database: UniProt
Entry: P0ADZ0
LinkDB: P0ADZ0
Original site: P0ADZ0 
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   07-JUN-2017, entry version 118.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
DE   AltName: Full=Large ribosomal subunit protein uL23 {ECO:0000303|PubMed:24524803};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=b3318, JW3280;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBUNIT.
RC   STRAIN=K12;
RX   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   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   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 277:1453-1462(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   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   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [9]
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   [10]
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   [11]
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   [12]
RP   MASS SPECTROMETRY, AND SUBUNIT.
RC   STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX   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   [13]
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   [14]
RP   NOMENCLATURE.
RX   PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA   Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA   Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA   Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA   Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA   Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT   "A new system for naming ribosomal proteins.";
RL   Curr. Opin. Struct. Biol. 24:165-169(2014).
RN   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
RC   STRAIN=MRE-600;
RX   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   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP   STRUCTURES, AND SUBUNIT.
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).
RN   [17]
RP   STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A
RP   NASCENT POLYPEPTIDE CHAIN, AND SUBUNIT.
RX   PubMed=21499241; DOI=10.1038/nsmb.2026;
RA   Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M.,
RA   Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K.,
RA   Beckmann R.;
RT   "Cryo-EM structure of the ribosome-SecYE complex in the membrane
RT   environment.";
RL   Nat. Struct. Mol. Biol. 18:614-621(2011).
RN   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 1-93 IN
RP   TNAC-STALLED 50S RIBOSOMAL SUBUNIT, AND SUBUNIT.
RC   STRAIN=K12 / A19 / KC6;
RX   PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA   Bischoff L., Berninghausen O., Beckmann R.;
RT   "Molecular basis for the ribosome functioning as an L-tryptophan
RT   sensor.";
RL   Cell Rep. 9:469-475(2014).
RN   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 50S RIBOSOMAL
RP   SUBUNIT IN COMPLEX WITH OBGE AND GMP-PNP, AND SUBUNIT.
RX   PubMed=24844575; DOI=10.1371/journal.pbio.1001866;
RA   Feng B., Mandava C.S., Guo Q., Wang J., Cao W., Li N., Zhang Y.,
RA   Zhang Y., Wang Z., Wu J., Sanyal S., Lei J., Gao N.;
RT   "Structural and functional insights into the mode of action of a
RT   universally conserved Obg GTPase.";
RL   PLoS Biol. 12:E1001866-E1001866(2014).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27906160; DOI=10.1038/nature20822;
RA   Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT   "Mechanistic insights into the alternative translation termination by
RT   ArfA and RF2.";
RL   Nature 541:550-553(2017).
RN   [21]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27906161; DOI=10.1038/nature20821;
RA   Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O.,
RA   Beckmann R., Wilson D.N.;
RT   "Structural basis for ArfA-RF2-mediated translation termination on
RT   mRNAs lacking stop codons.";
RL   Nature 541:546-549(2017).
RN   [22]
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27934701; DOI=10.1126/science.aai9127;
RA   James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT   "Translational termination without a stop codon.";
RL   Science 354:1437-1440(2016).
RN   [23]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=28077875; DOI=10.1038/nature21053;
RA   Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA   Jin H.;
RT   "Structural basis of co-translational quality control by ArfA and RF2
RT   bound to ribosome.";
RL   Nature 541:554-557(2017).
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       {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:12702815,
CC       ECO:0000269|PubMed:12756233, ECO:0000269|PubMed:3298242,
CC       ECO:0000269|PubMed:6170935}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:391594,
CC       PubMed:10094780, PubMed:12809609, PubMed:16272117,
CC       PubMed:21499241, PubMed:25310980, PubMed:24844575,
CC       PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts
CC       protein L29 and trigger factor. Might also contact SecE and
CC       probably does contact SecG and SecY when the SecYEG translocation
CC       complex is docked with the ribosome (PubMed:16292303).
CC       {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12226666,
CC       ECO:0000269|PubMed:12756233, ECO:0000269|PubMed:12809609,
CC       ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:16292303,
CC       ECO:0000269|PubMed:21499241, ECO:0000269|PubMed:24844575,
CC       ECO:0000269|PubMed:25310980, ECO:0000269|PubMed:2665813,
CC       ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC       ECO:0000269|PubMed:27934701, ECO:0000305|PubMed:16292303}.
CC   -!- INTERACTION:
CC       P0A7W1:rpsE; NbExp=2; IntAct=EBI-542264, EBI-543949;
CC   -!- MASS SPECTROMETRY: Mass=11198.0; Method=MALDI; Range=1-100;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23
CC       family. {ECO:0000255|HAMAP-Rule:MF_01369}.
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; NP_417777.1; NC_000913.3.
DR   RefSeq; WP_000617544.1; NZ_LN832404.1.
DR   PDB; 1ML5; EM; 14.00 A; t=2-85.
DR   PDB; 2J28; EM; 8.00 A; T=1-99.
DR   PDB; 2RDO; EM; 9.10 A; T=1-100.
DR   PDB; 2VRH; EM; 19.00 A; B=1-100.
DR   PDB; 3BBX; EM; 10.00 A; T=1-100.
DR   PDB; 3IY9; EM; 14.10 A; T=1-99.
DR   PDB; 3J45; EM; 9.50 A; T=1-100.
DR   PDB; 3J46; EM; 10.10 A; T=1-100.
DR   PDB; 3J5L; EM; 6.60 A; T=1-93.
DR   PDB; 3J7Z; EM; 3.90 A; T=1-100.
DR   PDB; 3J8G; EM; 5.00 A; T=1-100.
DR   PDB; 3J9Y; EM; 3.90 A; T=1-100.
DR   PDB; 3J9Z; EM; 3.60 A; LR=1-100.
DR   PDB; 3JA1; EM; 3.60 A; LV=1-100.
DR   PDB; 3JBU; EM; 3.64 A; t=1-100.
DR   PDB; 3JBV; EM; 3.32 A; t=1-100.
DR   PDB; 3JCD; EM; 3.70 A; T=1-100.
DR   PDB; 3JCE; EM; 3.20 A; T=1-100.
DR   PDB; 3JCJ; EM; 3.70 A; S=1-100.
DR   PDB; 3JCN; EM; 4.60 A; T=1-100.
DR   PDB; 4CSU; EM; 5.50 A; T=1-100.
DR   PDB; 4U1U; X-ray; 2.95 A; BT/DT=1-93.
DR   PDB; 4U1V; X-ray; 3.00 A; BT/DT=1-93.
DR   PDB; 4U20; X-ray; 2.90 A; BT/DT=1-93.
DR   PDB; 4U24; X-ray; 2.90 A; BT/DT=1-93.
DR   PDB; 4U25; X-ray; 2.90 A; BT/DT=1-93.
DR   PDB; 4U26; X-ray; 2.80 A; BT/DT=1-93.
DR   PDB; 4U27; X-ray; 2.80 A; BT/DT=1-93.
DR   PDB; 4UY8; EM; 3.80 A; T=1-93.
DR   PDB; 4V47; EM; 12.30 A; AR=1-100.
DR   PDB; 4V48; EM; 11.50 A; AR=1-100.
DR   PDB; 4V4H; X-ray; 3.46 A; BT/DT=1-100.
DR   PDB; 4V4Q; X-ray; 3.46 A; BT/DT=1-100.
DR   PDB; 4V4V; EM; 15.00 A; BR=7-98.
DR   PDB; 4V4W; EM; 15.00 A; BR=7-98.
DR   PDB; 4V50; X-ray; 3.22 A; BT/DT=1-100.
DR   PDB; 4V52; X-ray; 3.21 A; BT/DT=1-100.
DR   PDB; 4V53; X-ray; 3.54 A; BT/DT=1-100.
DR   PDB; 4V54; X-ray; 3.30 A; BT/DT=1-100.
DR   PDB; 4V55; X-ray; 4.00 A; BT/DT=1-100.
DR   PDB; 4V56; X-ray; 3.93 A; BT/DT=1-100.
DR   PDB; 4V57; X-ray; 3.50 A; BT/DT=1-100.
DR   PDB; 4V5B; X-ray; 3.74 A; AT/CT=1-100.
DR   PDB; 4V5H; EM; 5.80 A; BT=1-93.
DR   PDB; 4V5Y; X-ray; 4.45 A; BT/DT=1-100.
DR   PDB; 4V64; X-ray; 3.50 A; BT/DT=1-100.
DR   PDB; 4V65; EM; 9.00 A; BM=1-99.
DR   PDB; 4V66; EM; 9.00 A; BM=1-99.
DR   PDB; 4V69; EM; 6.70 A; BT=1-93.
DR   PDB; 4V6C; X-ray; 3.19 A; BT/DT=1-100.
DR   PDB; 4V6D; X-ray; 3.81 A; BT/DT=1-100.
DR   PDB; 4V6E; X-ray; 3.71 A; BT/DT=1-100.
DR   PDB; 4V6K; EM; 8.25 A; AU=1-100.
DR   PDB; 4V6L; EM; 13.20 A; BU=1-100.
DR   PDB; 4V6M; EM; 7.10 A; BT=1-100.
DR   PDB; 4V6N; EM; 12.10 A; AV=1-100.
DR   PDB; 4V6O; EM; 14.70 A; BV=1-100.
DR   PDB; 4V6P; EM; 13.50 A; BV=1-100.
DR   PDB; 4V6Q; EM; 11.50 A; BV=1-100.
DR   PDB; 4V6R; EM; 11.50 A; BV=1-100.
DR   PDB; 4V6S; EM; 13.10 A; AV=1-100.
DR   PDB; 4V6T; EM; 8.30 A; BT=1-93.
DR   PDB; 4V6V; EM; 9.80 A; BX=1-100.
DR   PDB; 4V6Y; EM; 12.00 A; BT=1-93.
DR   PDB; 4V6Z; EM; 12.00 A; BT=1-93.
DR   PDB; 4V70; EM; 17.00 A; BT=1-93.
DR   PDB; 4V71; EM; 20.00 A; BT=1-93.
DR   PDB; 4V72; EM; 13.00 A; BT=1-93.
DR   PDB; 4V73; EM; 15.00 A; BT=1-93.
DR   PDB; 4V74; EM; 17.00 A; BT=1-93.
DR   PDB; 4V75; EM; 12.00 A; BT=1-93.
DR   PDB; 4V76; EM; 17.00 A; BT=1-93.
DR   PDB; 4V77; EM; 17.00 A; BT=1-93.
DR   PDB; 4V78; EM; 20.00 A; BT=1-93.
DR   PDB; 4V79; EM; 15.00 A; BT=1-93.
DR   PDB; 4V7A; EM; 9.00 A; BT=1-93.
DR   PDB; 4V7B; EM; 6.80 A; BT=1-100.
DR   PDB; 4V7C; EM; 7.60 A; BV=1-100.
DR   PDB; 4V7D; EM; 7.60 A; AW=1-100.
DR   PDB; 4V7I; EM; 9.60 A; AT=1-100.
DR   PDB; 4V7S; X-ray; 3.25 A; BT/DT=1-93.
DR   PDB; 4V7T; X-ray; 3.19 A; BT/DT=1-93.
DR   PDB; 4V7U; X-ray; 3.10 A; BT/DT=1-93.
DR   PDB; 4V7V; X-ray; 3.29 A; BT/DT=1-93.
DR   PDB; 4V85; X-ray; 3.20 A; X=1-100.
DR   PDB; 4V89; X-ray; 3.70 A; BX=1-100.
DR   PDB; 4V9C; X-ray; 3.30 A; BT/DT=1-100.
DR   PDB; 4V9D; X-ray; 3.00 A; CT/DT=1-93.
DR   PDB; 4V9O; X-ray; 2.90 A; AT/CT/ET/GT=1-100.
DR   PDB; 4V9P; X-ray; 2.90 A; AT/CT/ET/GT=1-100.
DR   PDB; 4WF1; X-ray; 3.09 A; BT/DT=1-93.
DR   PDB; 4WOI; X-ray; 3.00 A; BT/CT=1-100.
DR   PDB; 4WWW; X-ray; 3.10 A; RT/YT=1-93.
DR   PDB; 4YBB; X-ray; 2.10 A; CU/DU=1-93.
DR   PDB; 5ADY; EM; 4.50 A; T=1-100.
DR   PDB; 5AFI; EM; 2.90 A; T=1-100.
DR   PDB; 5AKA; EM; 5.70 A; T=1-100.
DR   PDB; 5GAD; EM; 3.70 A; U=1-100.
DR   PDB; 5GAE; EM; 3.33 A; U=1-100.
DR   PDB; 5GAF; EM; 4.30 A; U=2-96.
DR   PDB; 5GAG; EM; 3.80 A; U=1-100.
DR   PDB; 5GAH; EM; 3.80 A; U=1-100.
DR   PDB; 5H5U; EM; 3.00 A; U=1-100.
DR   PDB; 5IQR; EM; 3.00 A; T=1-100.
DR   PDB; 5IT8; X-ray; 3.12 A; CU/DU=1-93.
DR   PDB; 5J5B; X-ray; 2.80 A; CU/DU=1-93.
DR   PDB; 5J7L; X-ray; 3.00 A; CU/DU=1-93.
DR   PDB; 5J88; X-ray; 3.32 A; CU/DU=1-100.
DR   PDB; 5J8A; X-ray; 3.10 A; CU/DU=1-93.
DR   PDB; 5J91; X-ray; 2.96 A; CU/DU=1-93.
DR   PDB; 5JC9; X-ray; 3.03 A; CU/DU=1-93.
DR   PDB; 5JTE; EM; 3.60 A; BT=1-100.
DR   PDB; 5JU8; EM; 3.60 A; BT=1-100.
DR   PDB; 5KCR; EM; 3.60 A; 1X=1-100.
DR   PDB; 5KCS; EM; 3.90 A; 1X=1-100.
DR   PDB; 5KPS; EM; 3.90 A; T=1-100.
DR   PDB; 5KPV; EM; 4.10 A; S=1-100.
DR   PDB; 5KPW; EM; 3.90 A; S=1-100.
DR   PDB; 5KPX; EM; 3.90 A; S=1-100.
DR   PDB; 5L3P; EM; 3.70 A; X=1-100.
DR   PDB; 5LZA; EM; 3.60 A; T=1-93.
DR   PDB; 5LZB; EM; 5.30 A; T=1-93.
DR   PDB; 5LZC; EM; 4.80 A; T=1-93.
DR   PDB; 5LZD; EM; 3.40 A; T=1-93.
DR   PDB; 5LZE; EM; 3.50 A; T=1-93.
DR   PDB; 5LZF; EM; 4.60 A; T=1-93.
DR   PDB; 5MDV; EM; 2.97 A; T=1-100.
DR   PDB; 5MDW; EM; 3.06 A; T=1-100.
DR   PDB; 5MDY; EM; 3.35 A; T=1-100.
DR   PDB; 5MDZ; EM; 3.10 A; T=1-100.
DR   PDB; 5MGP; EM; 3.10 A; T=1-93.
DR   PDB; 5U4I; EM; 3.50 A; U=1-100.
DR   PDBsum; 1ML5; -.
DR   PDBsum; 2J28; -.
DR   PDBsum; 2RDO; -.
DR   PDBsum; 2VRH; -.
DR   PDBsum; 3BBX; -.
DR   PDBsum; 3IY9; -.
DR   PDBsum; 3J45; -.
DR   PDBsum; 3J46; -.
DR   PDBsum; 3J5L; -.
DR   PDBsum; 3J7Z; -.
DR   PDBsum; 3J8G; -.
DR   PDBsum; 3J9Y; -.
DR   PDBsum; 3J9Z; -.
DR   PDBsum; 3JA1; -.
DR   PDBsum; 3JBU; -.
DR   PDBsum; 3JBV; -.
DR   PDBsum; 3JCD; -.
DR   PDBsum; 3JCE; -.
DR   PDBsum; 3JCJ; -.
DR   PDBsum; 3JCN; -.
DR   PDBsum; 4CSU; -.
DR   PDBsum; 4U1U; -.
DR   PDBsum; 4U1V; -.
DR   PDBsum; 4U20; -.
DR   PDBsum; 4U24; -.
DR   PDBsum; 4U25; -.
DR   PDBsum; 4U26; -.
DR   PDBsum; 4U27; -.
DR   PDBsum; 4UY8; -.
DR   PDBsum; 4V47; -.
DR   PDBsum; 4V48; -.
DR   PDBsum; 4V4H; -.
DR   PDBsum; 4V4Q; -.
DR   PDBsum; 4V4V; -.
DR   PDBsum; 4V4W; -.
DR   PDBsum; 4V50; -.
DR   PDBsum; 4V52; -.
DR   PDBsum; 4V53; -.
DR   PDBsum; 4V54; -.
DR   PDBsum; 4V55; -.
DR   PDBsum; 4V56; -.
DR   PDBsum; 4V57; -.
DR   PDBsum; 4V5B; -.
DR   PDBsum; 4V5H; -.
DR   PDBsum; 4V5Y; -.
DR   PDBsum; 4V64; -.
DR   PDBsum; 4V65; -.
DR   PDBsum; 4V66; -.
DR   PDBsum; 4V69; -.
DR   PDBsum; 4V6C; -.
DR   PDBsum; 4V6D; -.
DR   PDBsum; 4V6E; -.
DR   PDBsum; 4V6K; -.
DR   PDBsum; 4V6L; -.
DR   PDBsum; 4V6M; -.
DR   PDBsum; 4V6N; -.
DR   PDBsum; 4V6O; -.
DR   PDBsum; 4V6P; -.
DR   PDBsum; 4V6Q; -.
DR   PDBsum; 4V6R; -.
DR   PDBsum; 4V6S; -.
DR   PDBsum; 4V6T; -.
DR   PDBsum; 4V6V; -.
DR   PDBsum; 4V6Y; -.
DR   PDBsum; 4V6Z; -.
DR   PDBsum; 4V70; -.
DR   PDBsum; 4V71; -.
DR   PDBsum; 4V72; -.
DR   PDBsum; 4V73; -.
DR   PDBsum; 4V74; -.
DR   PDBsum; 4V75; -.
DR   PDBsum; 4V76; -.
DR   PDBsum; 4V77; -.
DR   PDBsum; 4V78; -.
DR   PDBsum; 4V79; -.
DR   PDBsum; 4V7A; -.
DR   PDBsum; 4V7B; -.
DR   PDBsum; 4V7C; -.
DR   PDBsum; 4V7D; -.
DR   PDBsum; 4V7I; -.
DR   PDBsum; 4V7S; -.
DR   PDBsum; 4V7T; -.
DR   PDBsum; 4V7U; -.
DR   PDBsum; 4V7V; -.
DR   PDBsum; 4V85; -.
DR   PDBsum; 4V89; -.
DR   PDBsum; 4V9C; -.
DR   PDBsum; 4V9D; -.
DR   PDBsum; 4V9O; -.
DR   PDBsum; 4V9P; -.
DR   PDBsum; 4WF1; -.
DR   PDBsum; 4WOI; -.
DR   PDBsum; 4WWW; -.
DR   PDBsum; 4YBB; -.
DR   PDBsum; 5ADY; -.
DR   PDBsum; 5AFI; -.
DR   PDBsum; 5AKA; -.
DR   PDBsum; 5GAD; -.
DR   PDBsum; 5GAE; -.
DR   PDBsum; 5GAF; -.
DR   PDBsum; 5GAG; -.
DR   PDBsum; 5GAH; -.
DR   PDBsum; 5H5U; -.
DR   PDBsum; 5IQR; -.
DR   PDBsum; 5IT8; -.
DR   PDBsum; 5J5B; -.
DR   PDBsum; 5J7L; -.
DR   PDBsum; 5J88; -.
DR   PDBsum; 5J8A; -.
DR   PDBsum; 5J91; -.
DR   PDBsum; 5JC9; -.
DR   PDBsum; 5JTE; -.
DR   PDBsum; 5JU8; -.
DR   PDBsum; 5KCR; -.
DR   PDBsum; 5KCS; -.
DR   PDBsum; 5KPS; -.
DR   PDBsum; 5KPV; -.
DR   PDBsum; 5KPW; -.
DR   PDBsum; 5KPX; -.
DR   PDBsum; 5L3P; -.
DR   PDBsum; 5LZA; -.
DR   PDBsum; 5LZB; -.
DR   PDBsum; 5LZC; -.
DR   PDBsum; 5LZD; -.
DR   PDBsum; 5LZE; -.
DR   PDBsum; 5LZF; -.
DR   PDBsum; 5MDV; -.
DR   PDBsum; 5MDW; -.
DR   PDBsum; 5MDY; -.
DR   PDBsum; 5MDZ; -.
DR   PDBsum; 5MGP; -.
DR   PDBsum; 5U4I; -.
DR   ProteinModelPortal; P0ADZ0; -.
DR   SMR; P0ADZ0; -.
DR   BioGrid; 4261290; 352.
DR   DIP; DIP-35972N; -.
DR   IntAct; P0ADZ0; 73.
DR   MINT; MINT-1225825; -.
DR   STRING; 511145.b3318; -.
DR   EPD; P0ADZ0; -.
DR   PaxDb; P0ADZ0; -.
DR   PRIDE; P0ADZ0; -.
DR   EnsemblBacteria; AAC76343; AAC76343; b3318.
DR   EnsemblBacteria; BAE77973; BAE77973; BAE77973.
DR   GeneID; 947819; -.
DR   KEGG; ecj:JW3280; -.
DR   KEGG; eco:b3318; -.
DR   PATRIC; fig|1411691.4.peg.3413; -.
DR   EchoBASE; EB0876; -.
DR   EcoGene; EG10883; rplW.
DR   eggNOG; ENOG41080KG; Bacteria.
DR   eggNOG; COG0089; LUCA.
DR   HOGENOM; HOG000231364; -.
DR   InParanoid; P0ADZ0; -.
DR   KO; K02892; -.
DR   PhylomeDB; P0ADZ0; -.
DR   BioCyc; EcoCyc:EG10883-MONOMER; -.
DR   BioCyc; MetaCyc:EG10883-MONOMER; -.
DR   EvolutionaryTrace; P0ADZ0; -.
DR   PRO; PR:P0ADZ0; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:CAFA.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IDA:CAFA.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   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. {ECO:0000269|PubMed:12226666}.
FT   MUTAGEN      18     18       E->A: Binds normally to ribosomes;
FT                                strongly reduces trigger factor binding.
FT                                {ECO:0000269|PubMed:12226666}.
FT   MUTAGEN      18     18       E->Q: Strongly reduces trigger factor
FT                                binding. {ECO:0000269|PubMed:12226666}.
FT   MUTAGEN      51     53       FEV->AAA: No effect on trigger factor
FT                                binding. {ECO:0000269|PubMed:12226666}.
FT   MUTAGEN      52     52       E->K: No effect on trigger factor
FT                                binding. {ECO:0000269|PubMed:12226666}.
FT   CONFLICT     80     80       Missing (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX         4      8       {ECO:0000244|PDB:5GAE}.
FT   STRAND       11     14       {ECO:0000244|PDB:5GAE}.
FT   HELIX        18     26       {ECO:0000244|PDB:5GAE}.
FT   STRAND       29     34       {ECO:0000244|PDB:5GAE}.
FT   HELIX        40     50       {ECO:0000244|PDB:5GAE}.
FT   STRAND       55     63       {ECO:0000244|PDB:5GAE}.
FT   STRAND       67     70       {ECO:0000244|PDB:5GAE}.
FT   STRAND       73     76       {ECO:0000244|PDB:5GAE}.
FT   STRAND       80     87       {ECO:0000244|PDB:5GAE}.
SQ   SEQUENCE   100 AA;  11199 MW;  30CD1D77CC7CF9EB CRC64;
     MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT
     LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE
//
DBGET integrated database retrieval system