RL5_ECOLI
ID RL5_ECOLI Reviewed; 179 AA.
AC P62399; P02389; Q2M6X3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=50S ribosomal protein L5;
DE AltName: Full=Large ribosomal subunit protein uL5 {ECO:0000303|PubMed:24524803};
GN Name=rplE; OrderedLocusNames=b3308, JW3270;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6222285; DOI=10.1093/nar/11.9.2599;
RA Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.;
RT "The spc ribosomal protein operon of Escherichia coli: sequence and
RT cotranscription of the ribosomal protein genes and a protein export gene.";
RL Nucleic Acids Res. 11:2599-2616(1983).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-179, AND SUBUNIT.
RC STRAIN=K;
RX PubMed=791672; DOI=10.1016/0014-5793(76)80695-3;
RA Chen R., Ehrke G.;
RT "The primary structure of the 5 S RNA binding protein L5 of Escherichia
RT coli ribosomes.";
RL FEBS Lett. 69:240-245(1976).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC STRAIN=K12 / JM105 / ATCC 47016;
RX PubMed=6262737; DOI=10.1093/nar/9.7.1757;
RA Olins P.O., Nomura M.;
RT "Translational regulation by ribosomal protein S8 in Escherichia coli:
RT structural homology between rRNA binding site and feedback target on
RT mRNA.";
RL Nucleic Acids Res. 9:1757-1764(1981).
RN [6]
RP FORMATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
RC STRAIN=MRE-600;
RX PubMed=354687; DOI=10.1021/bi00606a002;
RA Spierer P., Zimmermann R.A.;
RT "Stoichiometry, cooperativity, and stability of interactions between 5S RNA
RT and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia
RT coli.";
RL Biochemistry 17:2474-2479(1978).
RN [7]
RP REQUIREMENT FOR INCORPORATION OF 5S RRNA INTO THE 50S SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=7038683; DOI=10.1073/pnas.79.3.729;
RA Rohl R., Nierhaus K.H.;
RT "Assembly map of the large subunit (50S) of Escherichia coli ribosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:729-733(1982).
RN [8]
RP CROSS-LINKING TO THE TRNA CENTRAL FOLD.
RC STRAIN=MRE-600;
RX PubMed=8524654; DOI=10.1093/nar/23.22.4635;
RA Osswald M., Doering T., Brimacombe R.;
RT "The ribosomal neighbourhood of the central fold of tRNA: cross-links from
RT position 47 of tRNA located at the A, P or E site.";
RL Nucleic Acids Res. 23:4635-4641(1995).
RN [9]
RP CHARACTERIZATION OF A 5S RRNA/L5/L18/L25 SUBCOMPLEX.
RC STRAIN=K12 / A19;
RX PubMed=8925931; DOI=10.1016/0014-5793(96)00872-1;
RA Shpanchenko O.V., Zvereva M.I., Dontsova O.A., Nierhaus K.H.,
RA Bogdanov A.A.;
RT "5S rRNA sugar-phosphate backbone protection in complexes with specific
RT ribosomal proteins.";
RL FEBS Lett. 394:71-75(1996).
RN [10]
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 [11]
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 [12]
RP PARTIALLY SUPPRESSES AN RSGA MUTANT.
RC STRAIN=K12;
RX PubMed=18223068; DOI=10.1128/jb.01744-07;
RA Campbell T.L., Brown E.D.;
RT "Genetic interaction screens with ordered overexpression and deletion clone
RT sets implicate the Escherichia coli GTPase YjeQ in late ribosome
RT biogenesis.";
RL J. Bacteriol. 190:2537-2545(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
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), SUBUNIT, AND
RP INTERSUBUNIT BRIDGE FORMATION.
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 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON
RP TRANSLOCATION, AND SUBUNIT.
RX PubMed=12859903; DOI=10.1016/s0092-8674(03)00476-8;
RA Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.;
RT "Locking and unlocking of ribosomal motions.";
RL Cell 114:123-134(2003).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES
RP INCLUDING 2 CONFORMATIONS OF INTERSUBUNIT BRIDGE B1B, AND SUBUNIT.
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 [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 2-178 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 2-179 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., 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: This is 1 of the proteins that binds and probably mediates
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. Its 5S rRNA binding is
CC significantly enhanced in the presence of L18.
CC {ECO:0000269|PubMed:354687, ECO:0000269|PubMed:7038683,
CC ECO:0000269|PubMed:8925931}.
CC -!- FUNCTION: In the 70S ribosome in the initiation state (PubMed:12809609)
CC was modeled to contact protein S13 of the 30S subunit (bridge B1b),
CC connecting the 2 subunits; the protein-protein contacts between S13 and
CC L5 in B1b change in the model with bound EF-G implicating this bridge
CC in subunit movement (PubMed:12809609 and PubMed:18723842). In the two
CC 3.5 A resolved ribosome structures (PubMed:16272117) the contacts
CC between L5, S13 and S19 are different, confirming the dynamic nature of
CC this interaction. {ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:12859903, ECO:0000269|PubMed:16272117}.
CC -!- FUNCTION: Contacts the P site tRNA; the 5S rRNA and some of its
CC associated proteins might help stabilize positioning of ribosome-bound
CC tRNAs. {ECO:0000269|PubMed:8524654}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:791672,
CC PubMed:12809609, PubMed:12859903, PubMed:16272117, PubMed:25310980,
CC PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161);
CC part of the 5S rRNA/L5/L18/L25 subcomplex (PubMed:354687,
CC PubMed:8925931). Contacts the 5S rRNA; cross-links to the P site tRNA
CC (PubMed:8925931). Forms a bridge to the 30S subunit in the 70S
CC ribosome, contacting protein S13 and S19. {ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:12859903, ECO:0000269|PubMed:16272117,
CC ECO:0000269|PubMed:24844575, ECO:0000269|PubMed:25310980,
CC ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:354687,
CC ECO:0000269|PubMed:7038683, ECO:0000269|PubMed:791672,
CC ECO:0000269|PubMed:8524654, ECO:0000269|PubMed:8925931}.
CC -!- MASS SPECTROMETRY: Mass=20169.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: Identified as a multicopy suppressor of the slow growth
CC phenotype of an rsgA (yjeQ) deletion mutant.
CC {ECO:0000269|PubMed:18223068}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; X01563; CAA25717.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58105.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76333.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77983.1; -; Genomic_DNA.
DR EMBL; M10195; AAA24051.1; -; Genomic_DNA.
DR PIR; G65123; R5EC5.
DR RefSeq; NP_417767.1; NC_000913.3.
DR RefSeq; WP_001096200.1; NZ_STEB01000038.1.
DR PDB; 1ML5; EM; 14.00 A; g=2-177.
DR PDB; 2J28; EM; 8.00 A; F=2-179.
DR PDB; 2RDO; EM; 9.10 A; F=2-179.
DR PDB; 3BBX; EM; 10.00 A; F=2-179.
DR PDB; 3J5L; EM; 6.60 A; F=2-178.
DR PDB; 3J5S; EM; 7.50 A; G=2-179.
DR PDB; 3J7Z; EM; 3.90 A; F=1-179.
DR PDB; 3J8G; EM; 5.00 A; F=1-179.
DR PDB; 3J9Y; EM; 3.90 A; F=1-179.
DR PDB; 3J9Z; EM; 3.60 A; L7=2-179.
DR PDB; 3JA1; EM; 3.60 A; LG=2-179.
DR PDB; 3JBU; EM; 3.64 A; f=1-179.
DR PDB; 3JBV; EM; 3.32 A; f=1-179.
DR PDB; 3JCD; EM; 3.70 A; F=1-179.
DR PDB; 3JCE; EM; 3.20 A; F=1-179.
DR PDB; 3JCJ; EM; 3.70 A; E=1-179.
DR PDB; 3JCN; EM; 4.60 A; F=1-179.
DR PDB; 4CSU; EM; 5.50 A; F=2-179.
DR PDB; 4U1U; X-ray; 2.95 A; BF/DF=2-178.
DR PDB; 4U1V; X-ray; 3.00 A; BF/DF=2-178.
DR PDB; 4U20; X-ray; 2.90 A; BF/DF=2-178.
DR PDB; 4U24; X-ray; 2.90 A; BF/DF=2-178.
DR PDB; 4U25; X-ray; 2.90 A; BF/DF=2-178.
DR PDB; 4U26; X-ray; 2.80 A; BF/DF=2-178.
DR PDB; 4U27; X-ray; 2.80 A; BF/DF=2-178.
DR PDB; 4UY8; EM; 3.80 A; F=2-178.
DR PDB; 4V47; EM; 12.30 A; AD=2-179.
DR PDB; 4V48; EM; 11.50 A; AD=2-179.
DR PDB; 4V4H; X-ray; 3.46 A; BF/DF=1-179.
DR PDB; 4V4Q; X-ray; 3.46 A; BF/DF=2-179.
DR PDB; 4V4V; EM; 15.00 A; BD=3-179.
DR PDB; 4V4W; EM; 15.00 A; BD=3-179.
DR PDB; 4V50; X-ray; 3.22 A; BF/DF=2-179.
DR PDB; 4V52; X-ray; 3.21 A; BF/DF=2-179.
DR PDB; 4V53; X-ray; 3.54 A; BF/DF=2-179.
DR PDB; 4V54; X-ray; 3.30 A; BF/DF=2-179.
DR PDB; 4V55; X-ray; 4.00 A; BF/DF=2-179.
DR PDB; 4V56; X-ray; 3.93 A; BF/DF=2-179.
DR PDB; 4V57; X-ray; 3.50 A; BF/DF=2-179.
DR PDB; 4V5B; X-ray; 3.74 A; AF/CF=2-179.
DR PDB; 4V5H; EM; 5.80 A; BF=2-179.
DR PDB; 4V5Y; X-ray; 4.45 A; BF/DF=2-179.
DR PDB; 4V64; X-ray; 3.50 A; BF/DF=2-179.
DR PDB; 4V65; EM; 9.00 A; B2=2-179.
DR PDB; 4V66; EM; 9.00 A; B2=2-179.
DR PDB; 4V69; EM; 6.70 A; BF=2-179.
DR PDB; 4V6C; X-ray; 3.19 A; BF/DF=1-179.
DR PDB; 4V6D; X-ray; 3.81 A; BF/DF=1-179.
DR PDB; 4V6E; X-ray; 3.71 A; BF/DF=1-179.
DR PDB; 4V6K; EM; 8.25 A; AG=1-179.
DR PDB; 4V6L; EM; 13.20 A; BG=1-179.
DR PDB; 4V6M; EM; 7.10 A; BF=2-179.
DR PDB; 4V6N; EM; 12.10 A; AG=2-179.
DR PDB; 4V6O; EM; 14.70 A; BG=2-179.
DR PDB; 4V6P; EM; 13.50 A; BG=2-179.
DR PDB; 4V6Q; EM; 11.50 A; BG=2-179.
DR PDB; 4V6R; EM; 11.50 A; BG=2-179.
DR PDB; 4V6S; EM; 13.10 A; AG=2-179.
DR PDB; 4V6T; EM; 8.30 A; BF=2-178.
DR PDB; 4V6V; EM; 9.80 A; BG=2-179.
DR PDB; 4V6Y; EM; 12.00 A; BF=1-179.
DR PDB; 4V6Z; EM; 12.00 A; BF=1-179.
DR PDB; 4V70; EM; 17.00 A; BF=1-179.
DR PDB; 4V71; EM; 20.00 A; BF=1-179.
DR PDB; 4V72; EM; 13.00 A; BF=1-179.
DR PDB; 4V73; EM; 15.00 A; BF=1-179.
DR PDB; 4V74; EM; 17.00 A; BF=1-179.
DR PDB; 4V75; EM; 12.00 A; BF=1-179.
DR PDB; 4V76; EM; 17.00 A; BF=1-179.
DR PDB; 4V77; EM; 17.00 A; BF=1-179.
DR PDB; 4V78; EM; 20.00 A; BF=1-179.
DR PDB; 4V79; EM; 15.00 A; BF=1-179.
DR PDB; 4V7A; EM; 9.00 A; BF=1-179.
DR PDB; 4V7B; EM; 6.80 A; BF=1-179.
DR PDB; 4V7C; EM; 7.60 A; BG=2-179.
DR PDB; 4V7D; EM; 7.60 A; AG=2-179.
DR PDB; 4V7I; EM; 9.60 A; AF=1-179.
DR PDB; 4V7S; X-ray; 3.25 A; BF=2-178, DF=2-179.
DR PDB; 4V7T; X-ray; 3.19 A; BF=2-178, DF=2-179.
DR PDB; 4V7U; X-ray; 3.10 A; BF/DF=2-179.
DR PDB; 4V7V; X-ray; 3.29 A; BF=2-178, DF=2-179.
DR PDB; 4V85; X-ray; 3.20 A; BF=1-179.
DR PDB; 4V89; X-ray; 3.70 A; BF=1-179.
DR PDB; 4V9C; X-ray; 3.30 A; BF/DF=1-179.
DR PDB; 4V9D; X-ray; 3.00 A; CF/DF=2-178.
DR PDB; 4V9O; X-ray; 2.90 A; AF/CF/EF/GF=1-179.
DR PDB; 4V9P; X-ray; 2.90 A; AF/CF/EF/GF=1-179.
DR PDB; 4WF1; X-ray; 3.09 A; BF/DF=2-178.
DR PDB; 4WOI; X-ray; 3.00 A; BF/CF=1-179.
DR PDB; 4WWW; X-ray; 3.10 A; RF/YF=2-179.
DR PDB; 4YBB; X-ray; 2.10 A; CF/DF=2-178.
DR PDB; 5ADY; EM; 4.50 A; F=1-179.
DR PDB; 5AFI; EM; 2.90 A; F=1-179.
DR PDB; 5AKA; EM; 5.70 A; F=2-179.
DR PDB; 5GAD; EM; 3.70 A; F=1-179.
DR PDB; 5GAE; EM; 3.33 A; F=1-179.
DR PDB; 5GAF; EM; 4.30 A; F=2-178.
DR PDB; 5GAG; EM; 3.80 A; F=1-179.
DR PDB; 5GAH; EM; 3.80 A; F=1-179.
DR PDB; 5H5U; EM; 3.00 A; F=2-179.
DR PDB; 5IQR; EM; 3.00 A; E=1-179.
DR PDB; 5IT8; X-ray; 3.12 A; CF/DF=2-178.
DR PDB; 5J5B; X-ray; 2.80 A; CF/DF=2-178.
DR PDB; 5J7L; X-ray; 3.00 A; CF/DF=2-178.
DR PDB; 5J88; X-ray; 3.32 A; CF/DF=2-179.
DR PDB; 5J8A; X-ray; 3.10 A; CF/DF=2-179.
DR PDB; 5J91; X-ray; 2.96 A; CF/DF=2-179.
DR PDB; 5JC9; X-ray; 3.03 A; CF/DF=2-178.
DR PDB; 5JTE; EM; 3.60 A; BF=1-179.
DR PDB; 5JU8; EM; 3.60 A; BF=1-179.
DR PDB; 5KCR; EM; 3.60 A; 1G=1-179.
DR PDB; 5KCS; EM; 3.90 A; 1G=1-179.
DR PDB; 5KPS; EM; 3.90 A; E=1-179.
DR PDB; 5KPV; EM; 4.10 A; D=1-179.
DR PDB; 5KPW; EM; 3.90 A; D=1-179.
DR PDB; 5KPX; EM; 3.90 A; D=1-179.
DR PDB; 5L3P; EM; 3.70 A; G=1-179.
DR PDB; 5LZA; EM; 3.60 A; F=2-178.
DR PDB; 5LZB; EM; 5.30 A; F=2-178.
DR PDB; 5LZC; EM; 4.80 A; F=2-178.
DR PDB; 5LZD; EM; 3.40 A; F=2-178.
DR PDB; 5LZE; EM; 3.50 A; F=2-178.
DR PDB; 5LZF; EM; 4.60 A; F=2-178.
DR PDB; 5MDV; EM; 2.97 A; E=1-179.
DR PDB; 5MDW; EM; 3.06 A; E=1-179.
DR PDB; 5MDY; EM; 3.35 A; E=1-179.
DR PDB; 5MDZ; EM; 3.10 A; E=1-179.
DR PDB; 5MGP; EM; 3.10 A; F=2-178.
DR PDB; 5NCO; EM; 4.80 A; F=2-178.
DR PDB; 5NP6; EM; 3.60 A; d=2-178.
DR PDB; 5NWY; EM; 2.93 A; S=1-179.
DR PDB; 5O2R; EM; 3.40 A; F=2-178.
DR PDB; 5U4I; EM; 3.50 A; F=1-179.
DR PDB; 5U9F; EM; 3.20 A; 07=1-179.
DR PDB; 5U9G; EM; 3.20 A; 07=1-179.
DR PDB; 5UYK; EM; 3.90 A; 07=2-178.
DR PDB; 5UYL; EM; 3.60 A; 07=2-178.
DR PDB; 5UYM; EM; 3.20 A; 07=2-178.
DR PDB; 5UYN; EM; 4.00 A; 07=2-178.
DR PDB; 5UYP; EM; 3.90 A; 07=2-178.
DR PDB; 5UYQ; EM; 3.80 A; 07=2-178.
DR PDB; 5WDT; EM; 3.00 A; F=2-178.
DR PDB; 5WE4; EM; 3.10 A; F=2-178.
DR PDB; 5WE6; EM; 3.40 A; F=2-178.
DR PDB; 5WFK; EM; 3.40 A; F=2-178.
DR PDB; 6BU8; EM; 3.50 A; 07=2-178.
DR PDB; 6BY1; X-ray; 3.94 A; CF/DF=2-178.
DR PDB; 6C4I; EM; 3.24 A; F=2-178.
DR PDB; 6ENF; EM; 3.20 A; F=2-178.
DR PDB; 6ENJ; EM; 3.70 A; F=2-178.
DR PDB; 6ENU; EM; 3.10 A; F=2-178.
DR PDB; 6GBZ; EM; 3.80 A; F=2-178.
DR PDB; 6GC0; EM; 3.80 A; F=2-178.
DR PDB; 6GC4; EM; 4.30 A; F=2-178.
DR PDB; 6GC8; EM; 3.80 A; F=2-178.
DR PDB; 6GWT; EM; 3.80 A; F=2-178.
DR PDB; 6GXM; EM; 3.80 A; F=2-178.
DR PDB; 6GXN; EM; 3.90 A; F=2-178.
DR PDB; 6GXO; EM; 3.90 A; F=2-178.
DR PDB; 6GXP; EM; 4.40 A; F=2-178.
DR PDB; 6H4N; EM; 3.00 A; F=2-178.
DR PDB; 6H58; EM; 7.90 A; F/FF=2-178.
DR PDB; 6HRM; EM; 2.96 A; E=2-178.
DR PDB; 6I0Y; EM; 3.20 A; F=2-178.
DR PDB; 6I7V; X-ray; 2.90 A; CF/DF=2-178.
DR PDB; 6O9J; EM; 3.90 A; F=2-179.
DR PDB; 6O9K; EM; 4.00 A; F=2-178.
DR PDB; 6OFX; EM; 3.30 A; e=2-178.
DR PDB; 6OG7; EM; 3.30 A; e=2-178.
DR PDB; 6ORE; EM; 2.90 A; E=2-178.
DR PDB; 6ORL; EM; 3.50 A; E=2-178.
DR PDB; 6OST; EM; 4.20 A; E=2-178.
DR PDB; 6OT3; EM; 3.90 A; E=2-178.
DR PDB; 6OUO; EM; 3.70 A; E=2-178.
DR PDB; 6Q97; EM; 3.90 A; E=2-178.
DR PDB; 6Q98; EM; 4.30 A; E=1-179.
DR PDB; 6Q9A; EM; 3.70 A; E=2-178.
DR PDB; 6QDW; EM; 2.83 A; f=1-179.
DR PDB; 6QUL; EM; 3.00 A; F=1-179.
DR PDB; 6S0K; EM; 3.10 A; F=1-179.
DR PDB; 6SZS; EM; 3.06 A; F=1-179.
DR PDB; 6TBV; EM; 2.70 A; L051=1-179.
DR PDB; 6TC3; EM; 2.70 A; L051=1-179.
DR PDB; 6WD6; EM; 3.70 A; e=2-178.
DR PDB; 6WDB; EM; 4.00 A; e=2-178.
DR PDB; 6WDC; EM; 4.20 A; e=2-178.
DR PDB; 6WDD; EM; 3.20 A; e=2-178.
DR PDB; 6WDE; EM; 3.00 A; e=2-178.
DR PDB; 6WDF; EM; 3.30 A; e=2-178.
DR PDB; 6WDG; EM; 3.30 A; e=2-178.
DR PDB; 6WDH; EM; 4.30 A; e=2-178.
DR PDB; 6WDI; EM; 4.00 A; e=2-178.
DR PDB; 6WDJ; EM; 3.70 A; e=2-178.
DR PDB; 6WDK; EM; 3.60 A; e=2-178.
DR PDB; 6WDL; EM; 3.70 A; e=2-178.
DR PDB; 6WDM; EM; 3.60 A; e=2-178.
DR PDB; 6WNT; EM; 3.10 A; e=2-178.
DR PDB; 6WNV; EM; 3.50 A; e=2-178.
DR PDB; 6WNW; EM; 3.20 A; e=2-178.
DR PDB; 6XZ7; EM; 2.10 A; F=2-178.
DR PDB; 6XZA; EM; 2.66 A; F2=2-178.
DR PDB; 6XZB; EM; 2.54 A; F2=2-178.
DR PDB; 6Y69; EM; 2.86 A; F=2-178.
DR PDB; 6YS3; EM; 2.58 A; f=1-179.
DR PDB; 6YSR; EM; 3.10 A; F=1-179.
DR PDB; 6YSS; EM; 2.60 A; F=1-179.
DR PDB; 6YST; EM; 3.20 A; F=1-179.
DR PDB; 6YSU; EM; 3.70 A; F=1-179.
DR PDB; 6ZTJ; EM; 3.40 A; BF=1-179.
DR PDB; 6ZTL; EM; 3.50 A; BF=1-179.
DR PDB; 6ZTM; EM; 3.30 A; BF=1-179.
DR PDB; 6ZTN; EM; 3.90 A; BF=1-179.
DR PDB; 6ZTO; EM; 3.00 A; BF=1-179.
DR PDB; 6ZTP; EM; 3.00 A; BF=1-179.
DR PDB; 6ZU1; EM; 3.00 A; BF=1-179.
DR PDB; 7ABZ; EM; 3.21 A; E=2-178.
DR PDB; 7AC7; EM; 3.08 A; E=2-178.
DR PDB; 7ACJ; EM; 3.20 A; E=2-178.
DR PDB; 7ACR; EM; 3.44 A; E=2-178.
DR PDB; 7B5K; EM; 2.90 A; F=2-178.
DR PDB; 7BL2; EM; 3.70 A; F=1-179.
DR PDB; 7BL3; EM; 3.50 A; F=1-179.
DR PDB; 7BL4; EM; 2.40 A; F=1-179.
DR PDB; 7BL5; EM; 3.30 A; F=1-179.
DR PDB; 7BL6; EM; 4.00 A; F=1-179.
DR PDB; 7BV8; EM; 3.14 A; F=1-179.
DR PDB; 7D6Z; EM; 3.40 A; F=1-179.
DR PDB; 7D80; EM; 4.10 A; e=1-179.
DR PDB; 7JSS; EM; 3.70 A; e=2-178.
DR PDB; 7JSW; EM; 3.80 A; e=2-178.
DR PDB; 7JSZ; EM; 3.70 A; e=2-178.
DR PDB; 7JT1; EM; 3.30 A; e=2-178.
DR PDB; 7JT2; EM; 3.50 A; e=2-178.
DR PDB; 7JT3; EM; 3.70 A; e=2-178.
DR PDB; 7K50; EM; 3.40 A; e=2-178.
DR PDB; 7K51; EM; 3.50 A; e=2-178.
DR PDB; 7K52; EM; 3.40 A; e=2-178.
DR PDB; 7K53; EM; 3.20 A; e=2-178.
DR PDB; 7K54; EM; 3.20 A; e=2-178.
DR PDB; 7K55; EM; 3.30 A; e=2-178.
DR PDB; 7LV0; EM; 3.20 A; e=2-178.
DR PDB; 7N1P; EM; 2.33 A; LE=1-179.
DR PDB; 7N2C; EM; 2.72 A; LE=1-179.
DR PDB; 7N2U; EM; 2.53 A; LE=1-179.
DR PDB; 7N2V; EM; 2.54 A; LE=1-179.
DR PDB; 7N30; EM; 2.66 A; LE=1-179.
DR PDB; 7N31; EM; 2.69 A; LE=1-179.
DR PDB; 7NBU; EM; 3.11 A; f=2-178.
DR PDB; 7NWT; EM; 2.66 A; E=1-179.
DR PDB; 7O19; EM; 2.90 A; BF=1-179.
DR PDB; 7O1A; EM; 2.40 A; BF=1-179.
DR PDB; 7O1C; EM; 2.60 A; BF=1-179.
DR PDB; 7OIZ; EM; 2.90 A; f=1-179.
DR PDB; 7OJ0; EM; 3.50 A; f=1-179.
DR PDB; 7P3K; EM; 2.90 A; f=1-179.
DR PDB; 7PJS; EM; 2.35 A; F=1-179.
DR PDB; 7PJT; EM; 6.00 A; F=1-179.
DR PDB; 7PJV; EM; 3.10 A; F=1-179.
DR PDB; 7PJW; EM; 4.00 A; F=1-179.
DR PDB; 7PJX; EM; 6.50 A; F=1-179.
DR PDB; 7PJY; EM; 3.10 A; F=1-179.
DR PDB; 7PJZ; EM; 6.00 A; F=1-179.
DR PDB; 7QG8; EM; 3.97 A; S=1-179.
DR PDB; 7QGH; EM; 4.48 A; S=1-179.
DR PDB; 7SS9; EM; 3.90 A; e=2-178.
DR PDB; 7SSD; EM; 3.30 A; e=2-178.
DR PDB; 7SSL; EM; 3.80 A; e=2-178.
DR PDB; 7SSN; EM; 3.20 A; e=2-178.
DR PDB; 7SSO; EM; 3.20 A; e=2-178.
DR PDB; 7SSW; EM; 3.80 A; e=2-178.
DR PDB; 7ST2; EM; 2.90 A; e=2-178.
DR PDB; 7ST6; EM; 3.00 A; e=2-178.
DR PDB; 7ST7; EM; 3.20 A; e=2-178.
DR PDBsum; 1ML5; -.
DR PDBsum; 2J28; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3BBX; -.
DR PDBsum; 3J5L; -.
DR PDBsum; 3J5S; -.
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; 6GBZ; -.
DR PDBsum; 6GC0; -.
DR PDBsum; 6GC4; -.
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; 6QDW; -.
DR PDBsum; 6QUL; -.
DR PDBsum; 6S0K; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
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; P62399; -.
DR SMR; P62399; -.
DR BioGRID; 852112; 1.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35914N; -.
DR IntAct; P62399; 87.
DR STRING; 511145.b3308; -.
DR iPTMnet; P62399; -.
DR jPOST; P62399; -.
DR PaxDb; P62399; -.
DR PRIDE; P62399; -.
DR EnsemblBacteria; AAC76333; AAC76333; b3308.
DR EnsemblBacteria; BAE77983; BAE77983; BAE77983.
DR GeneID; 64293237; -.
DR GeneID; 67415349; -.
DR GeneID; 947800; -.
DR KEGG; ecj:JW3270; -.
DR KEGG; eco:b3308; -.
DR PATRIC; fig|1411691.4.peg.3423; -.
DR EchoBASE; EB0861; -.
DR eggNOG; COG0094; Bacteria.
DR HOGENOM; CLU_061015_2_1_6; -.
DR InParanoid; P62399; -.
DR OMA; ERMYAFL; -.
DR PhylomeDB; P62399; -.
DR BioCyc; EcoCyc:EG10868-MON; -.
DR BioCyc; MetaCyc:EG10868-MON; -.
DR EvolutionaryTrace; P62399; -.
DR PRO; PR:P62399; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:EcoCyc.
DR GO; GO:0008097; F:5S rRNA binding; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:EcoCyc.
DR Gene3D; 3.30.1440.10; -; 1.
DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR020930; Ribosomal_L5_bac-type.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:791672"
FT CHAIN 2..179
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000124925"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 94
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6I0Y"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:6XZ7"
SQ SEQUENCE 179 AA; 20302 MW; B2E95A8BE4B8D2A7 CRC64;
MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL DNAAADLAAI
SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF ERLITIAVPR IRDFRGLSAK
SFDGRGNYSM GVREQIIFPE IDYDKVDRVR GLDITITTTA KSDEEGRALL AAFDFPFRK
