RL11_ECOLI
ID RL11_ECOLI Reviewed; 142 AA.
AC P0A7J7; P02409; P76778; Q2M8R9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
DE AltName: Full=Large ribosomal subunit protein uL11 {ECO:0000303|PubMed:24524803};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; Synonyms=relC;
GN OrderedLocusNames=b3983, JW3946;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=377281; DOI=10.1073/pnas.76.4.1697;
RA Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.;
RT "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the
RT gene for RNA polymerase subunit beta in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 PROTEIN SEQUENCE OF 2-142, SUBUNIT, AND METHYLATION AT ALA-2; LYS-4 AND
RP LYS-40.
RC STRAIN=K12;
RX PubMed=7004866; DOI=10.1111/j.1432-1033.1980.tb04995.x;
RA Dognin M.J., Wittmann-Liebold B.;
RT "Purification and primary structure determination of the N-terminal blocked
RT protein, L11, from Escherichia coli ribosomes.";
RL Eur. J. Biochem. 112:131-151(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=2137819; DOI=10.1128/jb.172.3.1621-1627.1990;
RA Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.;
RT "Sequence and transcriptional pattern of the essential Escherichia coli
RT secE-nusG operon.";
RL J. Bacteriol. 172:1621-1627(1990).
RN [7]
RP STRUCTURAL STUDIES.
RX PubMed=2483975;
RA Choli T.;
RT "Structural properties of ribosomal protein L11 from Escherichia coli.";
RL Biochem. Int. 19:1323-1338(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 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 [10]
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 [11]
RP 3D-STRUCTURE MODELING, AND SUBUNIT.
RX PubMed=10756104; DOI=10.1006/jmbi.2000.3635;
RA Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J.,
RA Goerlach M., van Heel M., Brimacombe R.;
RT "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S
RT ribosomal subunit based on a cryo-electron microscopic reconstruction at
RT 7.5 A resolution.";
RL J. Mol. Biol. 298:35-59(2000).
RN [12]
RP SUBUNIT, AND STOICHIOMETRY.
RX PubMed=15923259; DOI=10.1073/pnas.0502193102;
RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H.,
RA Robinson C.V.;
RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found
RT by tandem MS of intact ribosomes from thermophilic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005).
RN [13]
RP SUCCINYLATION AT LYS-72 AND LYS-81.
RC STRAIN=K12;
RX PubMed=21151122; DOI=10.1038/nchembio.495;
RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
RT "Identification of lysine succinylation as a new post-translational
RT modification.";
RL Nat. Chem. Biol. 7:58-63(2011).
RN [14]
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 [15]
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 [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 2-142 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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 2-142 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 [18]
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 [19]
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 [20]
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 [21]
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: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit
CC (PubMed:15923259). Interacts with L10 and the large rRNA to form the
CC base of the stalk. L10 forms an elongated spine to which 2 L12 dimers
CC bind in a sequential fashion forming a pentameric L10(L12)2(L12)2
CC complex (PubMed:15923259). {ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:10756104, ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:15923259, 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:7004866}.
CC -!- INTERACTION:
CC P0A7J7; P0A805: frr; NbExp=2; IntAct=EBI-547288, EBI-1114349;
CC P0A7J7; P0A8T1: prmA; NbExp=4; IntAct=EBI-547288, EBI-556300;
CC -!- MASS SPECTROMETRY: Mass=14870.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; V00339; CAA23621.1; -; Genomic_DNA.
DR EMBL; M30610; AAA24623.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43081.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76957.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77337.1; -; Genomic_DNA.
DR PIR; S12572; R5EC11.
DR RefSeq; NP_418410.1; NC_000913.3.
DR RefSeq; WP_001085926.1; NZ_STEB01000045.1.
DR PDB; 1EG0; EM; 11.50 A; K=1-140.
DR PDB; 1MJ1; EM; 13.00 A; L=1-141.
DR PDB; 1ML5; EM; 14.00 A; l=1-141.
DR PDB; 2J28; EM; 8.00 A; I=2-142.
DR PDB; 2RDO; EM; 9.10 A; I=2-142.
DR PDB; 3DEG; EM; -; H=2-142.
DR PDB; 3EP2; EM; -; I=2-142.
DR PDB; 3EQ3; EM; -; I=2-142.
DR PDB; 3EQ4; EM; -; I=2-142.
DR PDB; 3J0D; EM; 11.10 A; G=2-142.
DR PDB; 3J5L; EM; 6.60 A; I=2-142.
DR PDB; 3J7Z; EM; 3.90 A; I=1-142.
DR PDB; 3J8G; EM; 5.00 A; I=1-142.
DR PDB; 3J9Y; EM; 3.90 A; I=1-142.
DR PDB; 3J9Z; EM; 3.60 A; LE=2-142.
DR PDB; 3JA1; EM; 3.60 A; LK=2-142.
DR PDB; 3JBV; EM; 3.32 A; i=1-142.
DR PDB; 3JCD; EM; 3.70 A; I=1-142.
DR PDB; 3JCE; EM; 3.20 A; I=1-142.
DR PDB; 3JCJ; EM; 3.70 A; H=1-142.
DR PDB; 3JCN; EM; 4.60 A; I=1-142.
DR PDB; 487D; EM; 7.50 A; L=10-86.
DR PDB; 4CSU; EM; 5.50 A; I=2-142.
DR PDB; 4U1U; X-ray; 2.95 A; BI/DI=2-142.
DR PDB; 4U1V; X-ray; 3.00 A; BI/DI=2-142.
DR PDB; 4U20; X-ray; 2.90 A; BI/DI=2-142.
DR PDB; 4U24; X-ray; 2.90 A; BI/DI=2-142.
DR PDB; 4U25; X-ray; 2.90 A; BI/DI=2-142.
DR PDB; 4U26; X-ray; 2.80 A; BI/DI=2-142.
DR PDB; 4U27; X-ray; 2.80 A; BI/DI=2-142.
DR PDB; 4UY8; EM; 3.80 A; I=2-142.
DR PDB; 4V47; EM; 12.30 A; AG=2-142.
DR PDB; 4V48; EM; 11.50 A; AG=2-142.
DR PDB; 4V4H; X-ray; 3.46 A; BI/DI=1-142.
DR PDB; 4V4Q; X-ray; 3.46 A; BI/DI=2-142.
DR PDB; 4V4V; EM; 15.00 A; BG=3-141.
DR PDB; 4V4W; EM; 15.00 A; BG=3-141.
DR PDB; 4V50; X-ray; 3.22 A; BI/DI=2-142.
DR PDB; 4V52; X-ray; 3.21 A; BI/DI=2-142.
DR PDB; 4V53; X-ray; 3.54 A; BI/DI=2-142.
DR PDB; 4V54; X-ray; 3.30 A; BI/DI=2-142.
DR PDB; 4V55; X-ray; 4.00 A; BI/DI=2-142.
DR PDB; 4V56; X-ray; 3.93 A; BI/DI=2-142.
DR PDB; 4V57; X-ray; 3.50 A; BI/DI=2-142.
DR PDB; 4V5B; X-ray; 3.74 A; AI/CI=2-142.
DR PDB; 4V5H; EM; 5.80 A; BI=2-142.
DR PDB; 4V5Y; X-ray; 4.45 A; BI/DI=2-142.
DR PDB; 4V64; X-ray; 3.50 A; BI/DI=2-142.
DR PDB; 4V65; EM; 9.00 A; B5=1-142.
DR PDB; 4V66; EM; 9.00 A; B5=1-142.
DR PDB; 4V69; EM; 6.70 A; BI=2-142.
DR PDB; 4V6C; X-ray; 3.19 A; BI/DI=1-142.
DR PDB; 4V6D; X-ray; 3.81 A; BI/DI=1-142.
DR PDB; 4V6E; X-ray; 3.71 A; BI/DI=1-142.
DR PDB; 4V6K; EM; 8.25 A; AJ=1-142.
DR PDB; 4V6L; EM; 13.20 A; BJ=1-142.
DR PDB; 4V6M; EM; 7.10 A; BI=2-142.
DR PDB; 4V6N; EM; 12.10 A; AK=2-142.
DR PDB; 4V6O; EM; 14.70 A; BK=2-142.
DR PDB; 4V6P; EM; 13.50 A; BK=2-142.
DR PDB; 4V6Q; EM; 11.50 A; BK=2-142.
DR PDB; 4V6R; EM; 11.50 A; BK=2-142.
DR PDB; 4V6S; EM; 13.10 A; AK=2-142.
DR PDB; 4V6T; EM; 8.30 A; BI=2-142.
DR PDB; 4V6V; EM; 9.80 A; BK=2-142.
DR PDB; 4V6Y; EM; 12.00 A; BI=1-142.
DR PDB; 4V6Z; EM; 12.00 A; BI=1-142.
DR PDB; 4V70; EM; 17.00 A; BI=1-142.
DR PDB; 4V71; EM; 20.00 A; BI=1-142.
DR PDB; 4V72; EM; 13.00 A; BI=1-142.
DR PDB; 4V73; EM; 15.00 A; BI=1-142.
DR PDB; 4V74; EM; 17.00 A; BI=1-142.
DR PDB; 4V75; EM; 12.00 A; BI=1-142.
DR PDB; 4V76; EM; 17.00 A; BI=1-142.
DR PDB; 4V77; EM; 17.00 A; BI=1-142.
DR PDB; 4V78; EM; 20.00 A; BI=1-142.
DR PDB; 4V79; EM; 15.00 A; BI=1-142.
DR PDB; 4V7A; EM; 9.00 A; BI=1-142.
DR PDB; 4V7B; EM; 6.80 A; BI=1-142.
DR PDB; 4V7C; EM; 7.60 A; BK=2-142.
DR PDB; 4V7D; EM; 7.60 A; AK=2-142.
DR PDB; 4V7I; EM; 9.60 A; AI=1-142.
DR PDB; 4V7S; X-ray; 3.25 A; BI/DI=2-142.
DR PDB; 4V7T; X-ray; 3.19 A; BI/DI=2-142.
DR PDB; 4V7U; X-ray; 3.10 A; BI/DI=2-142.
DR PDB; 4V7V; X-ray; 3.29 A; BI/DI=2-142.
DR PDB; 4V85; X-ray; 3.20 A; BI=1-142.
DR PDB; 4V89; X-ray; 3.70 A; BI=1-142.
DR PDB; 4V9C; X-ray; 3.30 A; BI/DI=1-142.
DR PDB; 4V9D; X-ray; 3.00 A; CI/DI=2-142.
DR PDB; 4V9O; X-ray; 2.90 A; AI/CI/EI/GI=1-142.
DR PDB; 4V9P; X-ray; 2.90 A; AI/CI/EI/GI=1-142.
DR PDB; 4WF1; X-ray; 3.09 A; BI/DI=2-142.
DR PDB; 4WOI; X-ray; 3.00 A; BI/CI=1-142.
DR PDB; 4WWW; X-ray; 3.10 A; RI/YI=2-142.
DR PDB; 4YBB; X-ray; 2.10 A; CJ/DJ=8-141.
DR PDB; 5ADY; EM; 4.50 A; I=1-142.
DR PDB; 5AFI; EM; 2.90 A; I=1-142.
DR PDB; 5AKA; EM; 5.70 A; I=2-142.
DR PDB; 5GAD; EM; 3.70 A; J=1-142.
DR PDB; 5GAE; EM; 3.33 A; J=1-142.
DR PDB; 5GAF; EM; 4.30 A; J=8-141.
DR PDB; 5GAG; EM; 3.80 A; J=1-142.
DR PDB; 5GAH; EM; 3.80 A; J=1-142.
DR PDB; 5H5U; EM; 3.00 A; J=2-142.
DR PDB; 5IQR; EM; 3.00 A; I=1-142.
DR PDB; 5IT8; X-ray; 3.12 A; CJ/DJ=8-141.
DR PDB; 5J5B; X-ray; 2.80 A; CJ/DJ=8-141.
DR PDB; 5J7L; X-ray; 3.00 A; CJ/DJ=8-141.
DR PDB; 5J88; X-ray; 3.32 A; CJ/DJ=8-142.
DR PDB; 5J8A; X-ray; 3.10 A; CJ/DJ=8-142.
DR PDB; 5J91; X-ray; 2.96 A; CJ/DJ=8-141.
DR PDB; 5JC9; X-ray; 3.03 A; CJ/DJ=8-141.
DR PDB; 5JTE; EM; 3.60 A; BI=1-142.
DR PDB; 5JU8; EM; 3.60 A; BI=1-142.
DR PDB; 5KCR; EM; 3.60 A; 1K=1-142.
DR PDB; 5KCS; EM; 3.90 A; 1K=1-142.
DR PDB; 5KPS; EM; 3.90 A; I=1-142.
DR PDB; 5KPV; EM; 4.10 A; H=1-142.
DR PDB; 5KPW; EM; 3.90 A; H=1-142.
DR PDB; 5KPX; EM; 3.90 A; H=1-142.
DR PDB; 5L3P; EM; 3.70 A; K=1-142.
DR PDB; 5LZA; EM; 3.60 A; I=2-142.
DR PDB; 5LZB; EM; 5.30 A; I=2-142.
DR PDB; 5LZC; EM; 4.80 A; I=2-142.
DR PDB; 5LZD; EM; 3.40 A; I=2-142.
DR PDB; 5LZE; EM; 3.50 A; I=2-142.
DR PDB; 5LZF; EM; 4.60 A; I=2-142.
DR PDB; 5MDV; EM; 2.97 A; I=1-142.
DR PDB; 5MDW; EM; 3.06 A; I=1-142.
DR PDB; 5MDY; EM; 3.35 A; I=1-142.
DR PDB; 5MDZ; EM; 3.10 A; I=1-142.
DR PDB; 5NCO; EM; 4.80 A; J=8-141.
DR PDB; 5NP6; EM; 3.60 A; g=2-142.
DR PDB; 5NWY; EM; 2.93 A; V=1-142.
DR PDB; 5O2R; EM; 3.40 A; I=2-142.
DR PDB; 5U4I; EM; 3.50 A; J=1-142.
DR PDB; 5U9F; EM; 3.20 A; 11=1-142.
DR PDB; 5U9G; EM; 3.20 A; 11=1-142.
DR PDB; 5UYK; EM; 3.90 A; 11=2-142.
DR PDB; 5UYL; EM; 3.60 A; 11=2-142.
DR PDB; 5UYM; EM; 3.20 A; 11=2-142.
DR PDB; 5UYN; EM; 4.00 A; 11=2-142.
DR PDB; 5UYP; EM; 3.90 A; 11=2-142.
DR PDB; 5UYQ; EM; 3.80 A; 11=2-142.
DR PDB; 5WDT; EM; 3.00 A; I=2-142.
DR PDB; 5WE4; EM; 3.10 A; I=2-142.
DR PDB; 5WE6; EM; 3.40 A; I=2-142.
DR PDB; 5WFK; EM; 3.40 A; I=2-142.
DR PDB; 6BU8; EM; 3.50 A; 11=2-142.
DR PDB; 6BY1; X-ray; 3.94 A; CI/DI=71-142.
DR PDB; 6C4I; EM; 3.24 A; J=1-142.
DR PDB; 6GWT; EM; 3.80 A; I=2-142.
DR PDB; 6GXM; EM; 3.80 A; I=2-142.
DR PDB; 6GXN; EM; 3.90 A; I=2-142.
DR PDB; 6GXO; EM; 3.90 A; I=2-142.
DR PDB; 6GXP; EM; 4.40 A; I=2-142.
DR PDB; 6HRM; EM; 2.96 A; I=6-140.
DR PDB; 6I0Y; EM; 3.20 A; I=2-142.
DR PDB; 6I7V; X-ray; 2.90 A; CJ/DJ=2-142.
DR PDB; 6O9J; EM; 3.90 A; 6=2-142.
DR PDB; 6O9K; EM; 4.00 A; I=2-142.
DR PDB; 6Q97; EM; 3.90 A; I=6-140.
DR PDB; 6Q98; EM; 4.30 A; I=1-142.
DR PDB; 6Q9A; EM; 3.70 A; I=6-140.
DR PDB; 6S0K; EM; 3.10 A; J=1-142.
DR PDB; 6WD6; EM; 3.70 A; i=2-142.
DR PDB; 6WDB; EM; 4.00 A; i=2-142.
DR PDB; 6WDC; EM; 4.20 A; i=2-142.
DR PDB; 6WDD; EM; 3.20 A; i=2-142.
DR PDB; 6WDE; EM; 3.00 A; i=2-142.
DR PDB; 6WDF; EM; 3.30 A; i=2-142.
DR PDB; 6WDG; EM; 3.30 A; i=2-142.
DR PDB; 6WDH; EM; 4.30 A; i=2-142.
DR PDB; 6WDI; EM; 4.00 A; i=2-142.
DR PDB; 6WDJ; EM; 3.70 A; i=2-142.
DR PDB; 6WDK; EM; 3.60 A; i=2-142.
DR PDB; 6WDL; EM; 3.70 A; i=2-142.
DR PDB; 6WDM; EM; 3.60 A; i=2-142.
DR PDB; 6WNT; EM; 3.10 A; i=2-142.
DR PDB; 6WNV; EM; 3.50 A; i=2-142.
DR PDB; 6WNW; EM; 3.20 A; i=2-142.
DR PDB; 6XZ7; EM; 2.10 A; I=8-141.
DR PDB; 6XZA; EM; 2.66 A; I2=8-141.
DR PDB; 6XZB; EM; 2.54 A; I2=8-141.
DR PDB; 6YSR; EM; 3.10 A; I=1-142.
DR PDB; 6YSS; EM; 2.60 A; I=1-142.
DR PDB; 6YST; EM; 3.20 A; I=1-142.
DR PDB; 6YSU; EM; 3.70 A; I=1-142.
DR PDB; 6ZTJ; EM; 3.40 A; BJ=1-142.
DR PDB; 7ABZ; EM; 3.21 A; I=1-142.
DR PDB; 7BL2; EM; 3.70 A; I=1-142.
DR PDB; 7BL3; EM; 3.50 A; I=1-142.
DR PDB; 7BL5; EM; 3.30 A; I=1-142.
DR PDB; 7BV8; EM; 3.14 A; J=1-142.
DR PDB; 7D6Z; EM; 3.40 A; I=1-142.
DR PDB; 7D80; EM; 4.10 A; h=1-142.
DR PDB; 7JSZ; EM; 3.70 A; i=1-142.
DR PDB; 7JT3; EM; 3.70 A; i=1-142.
DR PDB; 7K50; EM; 3.40 A; i=2-142.
DR PDB; 7K51; EM; 3.50 A; i=2-142.
DR PDB; 7K52; EM; 3.40 A; i=2-142.
DR PDB; 7K53; EM; 3.20 A; i=2-142.
DR PDB; 7K54; EM; 3.20 A; i=2-142.
DR PDB; 7K55; EM; 3.30 A; i=2-142.
DR PDB; 7LV0; EM; 3.20 A; i=2-142.
DR PDB; 7N1P; EM; 2.33 A; LK=1-142.
DR PDB; 7N2C; EM; 2.72 A; LK=1-142.
DR PDB; 7N2V; EM; 2.54 A; LK=1-142.
DR PDB; 7NWT; EM; 2.66 A; I=1-142.
DR PDB; 7PJS; EM; 2.35 A; I=1-142.
DR PDB; 7PJT; EM; 6.00 A; I=1-142.
DR PDB; 7PJV; EM; 3.10 A; I=1-142.
DR PDB; 7PJW; EM; 4.00 A; I=1-142.
DR PDB; 7PJX; EM; 6.50 A; I=1-142.
DR PDB; 7PJY; EM; 3.10 A; I=1-142.
DR PDB; 7PJZ; EM; 6.00 A; I=1-142.
DR PDB; 7QG8; EM; 3.97 A; V=1-142.
DR PDB; 7QGH; EM; 4.48 A; V=1-142.
DR PDB; 7SS9; EM; 3.90 A; i=1-142.
DR PDB; 7SSD; EM; 3.30 A; i=1-142.
DR PDB; 7SSL; EM; 3.80 A; i=2-142.
DR PDB; 7SSN; EM; 3.20 A; i=2-142.
DR PDB; 7SSO; EM; 3.20 A; i=2-142.
DR PDB; 7SSW; EM; 3.80 A; i=1-142.
DR PDB; 7ST2; EM; 2.90 A; i=1-142.
DR PDB; 7ST6; EM; 3.00 A; i=1-142.
DR PDB; 7ST7; EM; 3.20 A; i=2-142.
DR PDBsum; 1EG0; -.
DR PDBsum; 1MJ1; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 2J28; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3DEG; -.
DR PDBsum; 3EP2; -.
DR PDBsum; 3EQ3; -.
DR PDBsum; 3EQ4; -.
DR PDBsum; 3J0D; -.
DR PDBsum; 3J5L; -.
DR PDBsum; 3J7Z; -.
DR PDBsum; 3J8G; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JBV; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 3JCN; -.
DR PDBsum; 487D; -.
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; 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; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I0Y; -.
DR PDBsum; 6I7V; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6Q97; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6S0K; -.
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; 6YSR; -.
DR PDBsum; 6YSS; -.
DR PDBsum; 6YST; -.
DR PDBsum; 6YSU; -.
DR PDBsum; 6ZTJ; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7BL2; -.
DR PDBsum; 7BL3; -.
DR PDBsum; 7BL5; -.
DR PDBsum; 7BV8; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR PDBsum; 7JSZ; -.
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; 7N2V; -.
DR PDBsum; 7NWT; -.
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; P0A7J7; -.
DR SMR; P0A7J7; -.
DR BioGRID; 852778; 2.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35882N; -.
DR IntAct; P0A7J7; 103.
DR STRING; 511145.b3983; -.
DR iPTMnet; P0A7J7; -.
DR jPOST; P0A7J7; -.
DR PaxDb; P0A7J7; -.
DR PRIDE; P0A7J7; -.
DR EnsemblBacteria; AAC76957; AAC76957; b3983.
DR EnsemblBacteria; BAE77337; BAE77337; BAE77337.
DR GeneID; 67415316; -.
DR GeneID; 948484; -.
DR KEGG; ecj:JW3946; -.
DR KEGG; eco:b3983; -.
DR PATRIC; fig|1411691.4.peg.2729; -.
DR EchoBASE; EB0865; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_0_6; -.
DR InParanoid; P0A7J7; -.
DR OMA; CKQFNAK; -.
DR PhylomeDB; P0A7J7; -.
DR BioCyc; EcoCyc:EG10872-MON; -.
DR BioCyc; MetaCyc:EG10872-MON; -.
DR EvolutionaryTrace; P0A7J7; -.
DR PRO; PR:P0A7J7; -.
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:CAFA.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
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 GO; GO:0015968; P:stringent response; IDA:EcoCyc.
DR GO; GO:0006412; P:translation; IMP:EcoCyc.
DR GO; GO:0006415; P:translational termination; IMP:EcoCyc.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR TIGRFAMs; TIGR01632; L11_bact; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7004866"
FT CHAIN 2..142
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104283"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000269|PubMed:7004866"
FT MOD_RES 4
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:7004866"
FT MOD_RES 40
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:7004866"
FT MOD_RES 72
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 81
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT CONFLICT 132
FT /note="T -> S (in Ref. 1; CAA23621)"
FT /evidence="ECO:0000305"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7BL5"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6I0Y"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6I0Y"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7BL5"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:6XZ7"
SQ SEQUENCE 142 AA; 14875 MW; C49226BB2462BE0F CRC64;
MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE KGLPIPVVIT
VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK ISRAQLQEIA QTKAADMTGA
DIEAMTRSIE GTARSMGLVV ED
