RL23_ECOLI
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 03-AUG-2022, entry version 153.
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 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., Mau B.,
RA 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 MG1655
RT 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 cross-
RT 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; DOI=10.1016/s0021-9258(18)47489-3;
RA Herold M., Nierhaus K.H.;
RT "Incorporation of six additional proteins to complete the assembly map of
RT 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., 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 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., Ehrenberg M.,
RA Brunner J., Oudega B., Harms N., Luirink J.;
RT "Interplay of signal recognition particle and trigger factor at L23 near
RT 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 exit
RT 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., Brooks C.L. III,
RA Ban N., Frank J.;
RT "Structure of the E. coli protein-conducting channel bound to a translating
RT 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., Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using real-
RT space refinement.";
RL Cell 113:789-801(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES,
RP 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., Vila-Sanjurjo A.,
RA 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 NASCENT
RP POLYPEPTIDE CHAIN, AND SUBUNIT.
RX PubMed=21499241; DOI=10.1038/nsmb.2026;
RA Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B.,
RA Mielke T., Berninghausen O., Becker T., Schulten K., 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 TNAC-STALLED
RP 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 sensor.";
RL Cell Rep. 9:469-475(2014).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 50S RIBOSOMAL SUBUNIT
RP 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., Zhang Y.,
RA 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 COMPLEX
RP 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 ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT 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 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: One of the early assembly proteins, it binds 23S rRNA; is
CC essential for growth. One of the proteins that surround the polypeptide
CC exit tunnel on the outside of the subunit. Acts as the docking site for
CC trigger factor (PubMed:12226666) for Ffh binding to the ribosome
CC (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide
CC chains (PubMed:12756233). {ECO:0000269|PubMed:12226666,
CC ECO:0000269|PubMed:12702815, ECO:0000269|PubMed:12756233,
CC ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:6170935}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:391594,
CC PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:21499241,
CC PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160,
CC PubMed:27906161). Contacts protein L29 and trigger factor. Might also
CC contact SecE and probably does contact SecG and SecY when the SecYEG
CC translocation 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 P0ADZ0; P0A7W1: rpsE; NbExp=2; IntAct=EBI-542264, EBI-543949;
CC P0ADZ0; P0A8Z3: ybgC; NbExp=2; IntAct=EBI-542264, EBI-543276;
CC P0ADZ0; P39336: yjgL; NbExp=2; IntAct=EBI-542264, EBI-549937;
CC -!- MASS SPECTROMETRY: Mass=11198.0; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000255|HAMAP-Rule:MF_01369}.
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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; NP_417777.1; NC_000913.3.
DR RefSeq; WP_000617544.1; NZ_STEB01000038.1.
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; BX=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; 5NCO; EM; 4.80 A; U=2-96.
DR PDB; 5NP6; EM; 3.60 A; r=1-93.
DR PDB; 5NWY; EM; 2.93 A; g=1-100.
DR PDB; 5O2R; EM; 3.40 A; T=1-93.
DR PDB; 5U4I; EM; 3.50 A; U=1-100.
DR PDB; 5U9F; EM; 3.20 A; 22=1-100.
DR PDB; 5U9G; EM; 3.20 A; 22=1-100.
DR PDB; 5UYK; EM; 3.90 A; 22=1-93.
DR PDB; 5UYL; EM; 3.60 A; 22=1-93.
DR PDB; 5UYM; EM; 3.20 A; 22=1-93.
DR PDB; 5UYN; EM; 4.00 A; 22=1-93.
DR PDB; 5UYP; EM; 3.90 A; 22=1-93.
DR PDB; 5UYQ; EM; 3.80 A; 22=1-93.
DR PDB; 5WDT; EM; 3.00 A; T=2-93.
DR PDB; 5WE4; EM; 3.10 A; T=2-93.
DR PDB; 5WE6; EM; 3.40 A; T=2-93.
DR PDB; 5WFK; EM; 3.40 A; T=2-93.
DR PDB; 6BU8; EM; 3.50 A; 22=1-93.
DR PDB; 6BY1; X-ray; 3.94 A; CT/DT=1-93.
DR PDB; 6C4I; EM; 3.24 A; U=1-100.
DR PDB; 6ENF; EM; 3.20 A; T=1-93.
DR PDB; 6ENJ; EM; 3.70 A; T=1-93.
DR PDB; 6ENU; EM; 3.10 A; T=1-93.
DR PDB; 6FU8; EM; 3.20 A; C=1-93.
DR PDB; 6GBZ; EM; 3.80 A; T=1-93.
DR PDB; 6GC0; EM; 3.80 A; T=1-93.
DR PDB; 6GC4; EM; 4.30 A; T=1-93.
DR PDB; 6GC6; EM; 4.30 A; T=1-93.
DR PDB; 6GC7; EM; 4.30 A; T=1-93.
DR PDB; 6GC8; EM; 3.80 A; T=1-93.
DR PDB; 6GWT; EM; 3.80 A; T=1-93.
DR PDB; 6GXM; EM; 3.80 A; T=1-93.
DR PDB; 6GXN; EM; 3.90 A; T=1-93.
DR PDB; 6GXO; EM; 3.90 A; T=1-93.
DR PDB; 6GXP; EM; 4.40 A; T=1-93.
DR PDB; 6H4N; EM; 3.00 A; T=1-93.
DR PDB; 6H58; EM; 7.90 A; T/TT=1-93.
DR PDB; 6HRM; EM; 2.96 A; T=1-94.
DR PDB; 6I0Y; EM; 3.20 A; T=1-93.
DR PDB; 6I7V; X-ray; 2.90 A; CU/DU=1-93.
DR PDB; 6O9J; EM; 3.90 A; T=1-99.
DR PDB; 6O9K; EM; 4.00 A; T=1-93.
DR PDB; 6OFX; EM; 3.30 A; t=1-93.
DR PDB; 6OG7; EM; 3.30 A; t=1-93.
DR PDB; 6ORE; EM; 2.90 A; T=1-94.
DR PDB; 6ORL; EM; 3.50 A; T=1-94.
DR PDB; 6OST; EM; 4.20 A; T=1-94.
DR PDB; 6OT3; EM; 3.90 A; T=1-94.
DR PDB; 6OUO; EM; 3.70 A; T=1-94.
DR PDB; 6Q97; EM; 3.90 A; T=1-94.
DR PDB; 6Q98; EM; 4.30 A; T=1-100.
DR PDB; 6Q9A; EM; 3.70 A; T=1-94.
DR PDB; 6QUL; EM; 3.00 A; U=1-100.
DR PDB; 6S0K; EM; 3.10 A; U=1-100.
DR PDB; 6SZS; EM; 3.06 A; T=1-100.
DR PDB; 6TBV; EM; 2.70 A; L231=1-100.
DR PDB; 6TC3; EM; 2.70 A; L231=1-100.
DR PDB; 6VWL; EM; 3.10 A; R=1-100.
DR PDB; 6VWM; EM; 3.40 A; R=1-100.
DR PDB; 6VWN; EM; 3.40 A; R=1-100.
DR PDB; 6WD6; EM; 3.70 A; t=1-93.
DR PDB; 6WDB; EM; 4.00 A; t=1-93.
DR PDB; 6WDC; EM; 4.20 A; t=1-93.
DR PDB; 6WDD; EM; 3.20 A; t=1-93.
DR PDB; 6WDE; EM; 3.00 A; t=1-93.
DR PDB; 6WDF; EM; 3.30 A; t=1-93.
DR PDB; 6WDG; EM; 3.30 A; t=1-93.
DR PDB; 6WDH; EM; 4.30 A; t=1-93.
DR PDB; 6WDI; EM; 4.00 A; t=1-93.
DR PDB; 6WDJ; EM; 3.70 A; t=1-93.
DR PDB; 6WDK; EM; 3.60 A; t=1-93.
DR PDB; 6WDL; EM; 3.70 A; t=1-93.
DR PDB; 6WDM; EM; 3.60 A; t=1-93.
DR PDB; 6WNT; EM; 3.10 A; t=1-93.
DR PDB; 6WNV; EM; 3.50 A; t=1-93.
DR PDB; 6WNW; EM; 3.20 A; t=1-93.
DR PDB; 6XZ7; EM; 2.10 A; T=1-93.
DR PDB; 6XZA; EM; 2.66 A; T2=1-93.
DR PDB; 6XZB; EM; 2.54 A; T2=1-93.
DR PDB; 6Y69; EM; 2.86 A; T=1-93.
DR PDB; 6YS3; EM; 2.58 A; t=1-100.
DR PDB; 6YSR; EM; 3.10 A; T=1-100.
DR PDB; 6YSS; EM; 2.60 A; T=1-100.
DR PDB; 6YST; EM; 3.20 A; T=1-100.
DR PDB; 6YSU; EM; 3.70 A; T=1-100.
DR PDB; 6ZTJ; EM; 3.40 A; BU=1-100.
DR PDB; 6ZTL; EM; 3.50 A; BU=1-100.
DR PDB; 6ZTM; EM; 3.30 A; BU=1-100.
DR PDB; 6ZTN; EM; 3.90 A; BU=1-100.
DR PDB; 6ZTO; EM; 3.00 A; BU=1-100.
DR PDB; 6ZTP; EM; 3.00 A; BU=1-100.
DR PDB; 6ZU1; EM; 3.00 A; BU=1-100.
DR PDB; 7ABZ; EM; 3.21 A; T=1-93.
DR PDB; 7AC7; EM; 3.08 A; T=1-94.
DR PDB; 7ACJ; EM; 3.20 A; T=1-94.
DR PDB; 7ACR; EM; 3.44 A; T=1-94.
DR PDB; 7B5K; EM; 2.90 A; T=1-93.
DR PDB; 7BL2; EM; 3.70 A; T=1-100.
DR PDB; 7BL3; EM; 3.50 A; T=1-100.
DR PDB; 7BL4; EM; 2.40 A; T=1-100.
DR PDB; 7BL5; EM; 3.30 A; T=1-100.
DR PDB; 7BL6; EM; 4.00 A; T=1-100.
DR PDB; 7BV8; EM; 3.14 A; U=1-100.
DR PDB; 7D6Z; EM; 3.40 A; Z=1-100.
DR PDB; 7D80; EM; 4.10 A; W=1-100.
DR PDB; 7JSS; EM; 3.70 A; t=1-93.
DR PDB; 7JSW; EM; 3.80 A; t=1-93.
DR PDB; 7JSZ; EM; 3.70 A; t=1-93.
DR PDB; 7JT1; EM; 3.30 A; t=1-93.
DR PDB; 7JT2; EM; 3.50 A; t=1-93.
DR PDB; 7JT3; EM; 3.70 A; t=1-93.
DR PDB; 7K50; EM; 3.40 A; t=1-93.
DR PDB; 7K51; EM; 3.50 A; t=1-93.
DR PDB; 7K52; EM; 3.40 A; t=1-93.
DR PDB; 7K53; EM; 3.20 A; t=1-93.
DR PDB; 7K54; EM; 3.20 A; t=1-93.
DR PDB; 7K55; EM; 3.30 A; t=1-93.
DR PDB; 7LV0; EM; 3.20 A; t=1-93.
DR PDB; 7N1P; EM; 2.33 A; LW=1-100.
DR PDB; 7N2C; EM; 2.72 A; LW=1-100.
DR PDB; 7N2U; EM; 2.53 A; LW=1-100.
DR PDB; 7N2V; EM; 2.54 A; LW=1-100.
DR PDB; 7N30; EM; 2.66 A; LW=1-100.
DR PDB; 7N31; EM; 2.69 A; LW=1-100.
DR PDB; 7NBU; EM; 3.11 A; s=1-93.
DR PDB; 7NWT; EM; 2.66 A; T=1-100.
DR PDB; 7O19; EM; 2.90 A; BT=1-100.
DR PDB; 7O1A; EM; 2.40 A; BT=1-100.
DR PDB; 7O1C; EM; 2.60 A; BT=1-100.
DR PDB; 7OIZ; EM; 2.90 A; s=1-100.
DR PDB; 7OJ0; EM; 3.50 A; s=1-100.
DR PDB; 7P3K; EM; 2.90 A; s=1-100.
DR PDB; 7PJS; EM; 2.35 A; T=1-100.
DR PDB; 7PJT; EM; 6.00 A; T=1-100.
DR PDB; 7PJV; EM; 3.10 A; T=1-100.
DR PDB; 7PJW; EM; 4.00 A; T=1-100.
DR PDB; 7PJX; EM; 6.50 A; T=1-100.
DR PDB; 7PJY; EM; 3.10 A; T=1-100.
DR PDB; 7PJZ; EM; 6.00 A; T=1-100.
DR PDB; 7QG8; EM; 3.97 A; g=1-100.
DR PDB; 7QGH; EM; 4.48 A; g=1-100.
DR PDB; 7SS9; EM; 3.90 A; t=1-93.
DR PDB; 7SSD; EM; 3.30 A; t=1-93.
DR PDB; 7SSL; EM; 3.80 A; t=1-93.
DR PDB; 7SSN; EM; 3.20 A; t=1-93.
DR PDB; 7SSO; EM; 3.20 A; t=1-93.
DR PDB; 7SSW; EM; 3.80 A; t=1-93.
DR PDB; 7ST2; EM; 2.90 A; t=1-93.
DR PDB; 7ST6; EM; 3.00 A; t=1-93.
DR PDB; 7ST7; EM; 3.20 A; t=1-93.
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; 5NCO; -.
DR PDBsum; 5NP6; -.
DR PDBsum; 5NWY; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 5U4I; -.
DR PDBsum; 5U9F; -.
DR PDBsum; 5U9G; -.
DR PDBsum; 5UYK; -.
DR PDBsum; 5UYL; -.
DR PDBsum; 5UYM; -.
DR PDBsum; 5UYN; -.
DR PDBsum; 5UYP; -.
DR PDBsum; 5UYQ; -.
DR PDBsum; 5WDT; -.
DR PDBsum; 5WE4; -.
DR PDBsum; 5WE6; -.
DR PDBsum; 5WFK; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6BY1; -.
DR PDBsum; 6C4I; -.
DR PDBsum; 6ENF; -.
DR PDBsum; 6ENJ; -.
DR PDBsum; 6ENU; -.
DR PDBsum; 6FU8; -.
DR PDBsum; 6GBZ; -.
DR PDBsum; 6GC0; -.
DR PDBsum; 6GC4; -.
DR PDBsum; 6GC6; -.
DR PDBsum; 6GC7; -.
DR PDBsum; 6GC8; -.
DR PDBsum; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I0Y; -.
DR PDBsum; 6I7V; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6OFX; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6ORE; -.
DR PDBsum; 6ORL; -.
DR PDBsum; 6OST; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 6Q97; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6QUL; -.
DR PDBsum; 6S0K; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6WD6; -.
DR PDBsum; 6WDB; -.
DR PDBsum; 6WDC; -.
DR PDBsum; 6WDD; -.
DR PDBsum; 6WDE; -.
DR PDBsum; 6WDF; -.
DR PDBsum; 6WDG; -.
DR PDBsum; 6WDH; -.
DR PDBsum; 6WDI; -.
DR PDBsum; 6WDJ; -.
DR PDBsum; 6WDK; -.
DR PDBsum; 6WDL; -.
DR PDBsum; 6WDM; -.
DR PDBsum; 6WNT; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6XZ7; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 6Y69; -.
DR PDBsum; 6YS3; -.
DR PDBsum; 6YSR; -.
DR PDBsum; 6YSS; -.
DR PDBsum; 6YST; -.
DR PDBsum; 6YSU; -.
DR PDBsum; 6ZTJ; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 6ZTM; -.
DR PDBsum; 6ZTN; -.
DR PDBsum; 6ZTO; -.
DR PDBsum; 6ZTP; -.
DR PDBsum; 6ZU1; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BL2; -.
DR PDBsum; 7BL3; -.
DR PDBsum; 7BL4; -.
DR PDBsum; 7BL5; -.
DR PDBsum; 7BL6; -.
DR PDBsum; 7BV8; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR PDBsum; 7JSS; -.
DR PDBsum; 7JSW; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7JT1; -.
DR PDBsum; 7JT2; -.
DR PDBsum; 7JT3; -.
DR PDBsum; 7K50; -.
DR PDBsum; 7K51; -.
DR PDBsum; 7K52; -.
DR PDBsum; 7K53; -.
DR PDBsum; 7K54; -.
DR PDBsum; 7K55; -.
DR PDBsum; 7LV0; -.
DR PDBsum; 7N1P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7N2U; -.
DR PDBsum; 7N2V; -.
DR PDBsum; 7N30; -.
DR PDBsum; 7N31; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7NWT; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7OIZ; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJS; -.
DR PDBsum; 7PJT; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJW; -.
DR PDBsum; 7PJX; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7PJZ; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
DR PDBsum; 7SS9; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSN; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7SSW; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST6; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P0ADZ0; -.
DR SMR; P0ADZ0; -.
DR BioGRID; 4261290; 352.
DR BioGRID; 852131; 1.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35972N; -.
DR IntAct; P0ADZ0; 91.
DR STRING; 511145.b3318; -.
DR jPOST; P0ADZ0; -.
DR PaxDb; P0ADZ0; -.
DR PRIDE; P0ADZ0; -.
DR EnsemblBacteria; AAC76343; AAC76343; b3318.
DR EnsemblBacteria; BAE77973; BAE77973; BAE77973.
DR GeneID; 67415359; -.
DR GeneID; 947819; -.
DR KEGG; ecj:JW3280; -.
DR KEGG; eco:b3318; -.
DR PATRIC; fig|1411691.4.peg.3413; -.
DR EchoBASE; EB0876; -.
DR eggNOG; COG0089; Bacteria.
DR HOGENOM; CLU_037562_3_1_6; -.
DR InParanoid; P0ADZ0; -.
DR OMA; FEVDHRA; -.
DR PhylomeDB; P0ADZ0; -.
DR BioCyc; EcoCyc:EG10883-MON; -.
DR BioCyc; MetaCyc:EG10883-MON; -.
DR EvolutionaryTrace; P0ADZ0; -.
DR PRO; PR:P0ADZ0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:CAFA.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:CAFA.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
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; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..100
FT /note="50S ribosomal protein L23"
FT /id="PRO_0000129407"
FT MUTAGEN 16..18
FT /note="VSE->AAA: Strongly reduces trigger factor binding."
FT /evidence="ECO:0000269|PubMed:12226666"
FT MUTAGEN 18
FT /note="E->A: Binds normally to ribosomes; strongly reduces
FT trigger factor binding."
FT /evidence="ECO:0000269|PubMed:12226666"
FT MUTAGEN 18
FT /note="E->Q: Strongly reduces trigger factor binding."
FT /evidence="ECO:0000269|PubMed:12226666"
FT MUTAGEN 51..53
FT /note="FEV->AAA: No effect on trigger factor binding."
FT /evidence="ECO:0000269|PubMed:12226666"
FT MUTAGEN 52
FT /note="E->K: No effect on trigger factor binding."
FT /evidence="ECO:0000269|PubMed:12226666"
FT CONFLICT 80
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6XZ7"
SQ SEQUENCE 100 AA; 11199 MW; 30CD1D77CC7CF9EB CRC64;
MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT
LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE
