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RL14_ECOLI
ID   RL14_ECOLI              Reviewed;         123 AA.
AC   P0ADY3; P02411; Q2M6X5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367};
DE   AltName: Full=Large ribosomal subunit protein uL14 {ECO:0000303|PubMed:24524803};
GN   Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367};
GN   OrderedLocusNames=b3310, JW3272;
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=K;
RX   PubMed=352727; DOI=10.1016/0014-5793(78)80020-9;
RA   Morinaga T., Funatsu G., Funatsu M., Wittmann-Liebold B., Wittmann H.G.;
RT   "Primary structure of protein L14 isolated from Escherichia coli
RT   ribosomes.";
RL   FEBS Lett. 91:74-77(1978).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC   STRAIN=K12;
RX   PubMed=151587; DOI=10.1016/0092-8674(78)90096-x;
RA   Post L.E., Arfsten A.E., Reusser F., Nomura M.;
RT   "DNA sequences of promoter regions for the str and spc ribosomal protein
RT   operons in E. coli.";
RL   Cell 15:215-229(1978).
RN   [6]
RP   PROTEIN SEQUENCE OF 24-28, SUBUNIT, AND CROSS-LINKING TO RRNA.
RC   STRAIN=MRE-600;
RX   PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA   Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT   "Protein-rRNA binding features and their structural and functional
RT   implications in ribosomes as determined by cross-linking studies.";
RL   EMBO J. 14:4578-4588(1995).
RN   [7]
RP   CROSS-LINKING TO L19, AND SUBUNIT.
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   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   [9]
RP   FUNCTION, INTERACTION WITH RSFS, AND MUTAGENESIS OF THR-97; ARG-98; LYS-114
RP   AND SER-117.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=22829778; DOI=10.1371/journal.pgen.1002815;
RA   Hauser R., Pech M., Kijek J., Yamamoto H., Titz B., Naeve F.,
RA   Tovchigrechko A., Yamamoto K., Szaflarski W., Takeuchi N., Stellberger T.,
RA   Diefenbacher M.E., Nierhaus K.H., Uetz P.;
RT   "RsfA (YbeB) proteins are conserved ribosomal silencing factors.";
RL   PLoS Genet. 8:E1002815-E1002815(2012).
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   STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), SUBUNIT, AND
RP   INTERSUBUNIT BRIDGE FORMATION.
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   [13]
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   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 1-122 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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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 protein binds directly to 23S ribosomal RNA. In the
CC       E.coli 70S ribosome it has been modeled to make two contacts with the
CC       16S rRNA of the 30S subunit, forming part of bridges B5 and B8,
CC       connecting the 2 subunits (PubMed:12809609). Although the protein
CC       undergoes significant rotation during the transition from an initiation
CC       to and EF-G bound state, the bridges remain stable. In the 3.5 A
CC       resolved structures L14 and L19 interact and together make contact with
CC       the 16S rRNA in bridges B5 and B8 (PubMed:16272117).
CC       {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117,
CC       ECO:0000269|PubMed:22829778}.
CC   -!- FUNCTION: Can also interact with RsfS, in this case bridge B8 probably
CC       cannot form, and the 30S and 50S ribosomal subunits do not associate,
CC       which represses translation. {ECO:0000269|PubMed:22829778}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:352727,
CC       PubMed:7556101, PubMed:2665813, PubMed:10094780, PubMed:10756104,
CC       PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575,
CC       PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts L19
CC       (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit
CC       in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS,
CC       which then probably inhibits ribosomal subunit association.
CC       {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:10756104,
CC       ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:151587,
CC       ECO:0000269|PubMed:16272117, 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:352727, ECO:0000269|PubMed:7556101}.
CC   -!- MASS SPECTROMETRY: Mass=13540.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01367}.
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DR   EMBL; X01563; CAA25715.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58107.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76335.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77981.1; -; Genomic_DNA.
DR   EMBL; V00357; CAA23653.1; -; Genomic_DNA.
DR   PIR; A65124; R5EC14.
DR   RefSeq; NP_417769.1; NC_000913.3.
DR   RefSeq; WP_000613955.1; NZ_STEB01000038.1.
DR   PDB; 1ML5; EM; 14.00 A; n=1-122.
DR   PDB; 2J28; EM; 8.00 A; K=2-122.
DR   PDB; 2RDO; EM; 9.10 A; K=1-123.
DR   PDB; 3BBX; EM; 10.00 A; K=1-123.
DR   PDB; 3IY9; EM; 14.10 A; K=2-122.
DR   PDB; 3IZZ; EM; 10.80 A; G=2-122.
DR   PDB; 3J5L; EM; 6.60 A; K=1-122.
DR   PDB; 3J7Z; EM; 3.90 A; K=1-123.
DR   PDB; 3J8G; EM; 5.00 A; K=1-123.
DR   PDB; 3J9Y; EM; 3.90 A; K=1-123.
DR   PDB; 3J9Z; EM; 3.60 A; LG=1-123.
DR   PDB; 3JA1; EM; 3.60 A; LM=1-123.
DR   PDB; 3JBU; EM; 3.64 A; k=1-123.
DR   PDB; 3JBV; EM; 3.32 A; k=1-123.
DR   PDB; 3JCD; EM; 3.70 A; K=1-123.
DR   PDB; 3JCE; EM; 3.20 A; K=1-123.
DR   PDB; 3JCJ; EM; 3.70 A; J=1-123.
DR   PDB; 3JCN; EM; 4.60 A; K=1-123.
DR   PDB; 487D; EM; 7.50 A; M=1-122.
DR   PDB; 4CSU; EM; 5.50 A; K=1-123.
DR   PDB; 4U1U; X-ray; 2.95 A; BK/DK=1-122.
DR   PDB; 4U1V; X-ray; 3.00 A; BK/DK=1-122.
DR   PDB; 4U20; X-ray; 2.90 A; BK/DK=1-122.
DR   PDB; 4U24; X-ray; 2.90 A; BK/DK=1-122.
DR   PDB; 4U25; X-ray; 2.90 A; BK/DK=1-122.
DR   PDB; 4U26; X-ray; 2.80 A; BK/DK=1-122.
DR   PDB; 4U27; X-ray; 2.80 A; BK/DK=1-122.
DR   PDB; 4UY8; EM; 3.80 A; K=1-122.
DR   PDB; 4V47; EM; 12.30 A; AI=1-123.
DR   PDB; 4V48; EM; 11.50 A; AI=1-123.
DR   PDB; 4V4H; X-ray; 3.46 A; BK/DK=1-123.
DR   PDB; 4V4Q; X-ray; 3.46 A; BK/DK=1-123.
DR   PDB; 4V4V; EM; 15.00 A; BI=2-123.
DR   PDB; 4V4W; EM; 15.00 A; BI=2-123.
DR   PDB; 4V50; X-ray; 3.22 A; BK/DK=1-123.
DR   PDB; 4V52; X-ray; 3.21 A; BK/DK=1-123.
DR   PDB; 4V53; X-ray; 3.54 A; BK/DK=1-123.
DR   PDB; 4V54; X-ray; 3.30 A; BK/DK=1-123.
DR   PDB; 4V55; X-ray; 4.00 A; BK/DK=1-123.
DR   PDB; 4V56; X-ray; 3.93 A; BK/DK=1-123.
DR   PDB; 4V57; X-ray; 3.50 A; BK/DK=1-123.
DR   PDB; 4V5B; X-ray; 3.74 A; AK/CK=1-123.
DR   PDB; 4V5H; EM; 5.80 A; BK=1-121.
DR   PDB; 4V5Y; X-ray; 4.45 A; BK/DK=1-123.
DR   PDB; 4V64; X-ray; 3.50 A; BK/DK=1-123.
DR   PDB; 4V65; EM; 9.00 A; BD=1-123.
DR   PDB; 4V66; EM; 9.00 A; BD=1-123.
DR   PDB; 4V69; EM; 6.70 A; BK=2-122.
DR   PDB; 4V6C; X-ray; 3.19 A; BK/DK=1-123.
DR   PDB; 4V6D; X-ray; 3.81 A; BK/DK=1-123.
DR   PDB; 4V6E; X-ray; 3.71 A; BK/DK=1-123.
DR   PDB; 4V6K; EM; 8.25 A; AL=1-123.
DR   PDB; 4V6L; EM; 13.20 A; BL=1-123.
DR   PDB; 4V6M; EM; 7.10 A; BK=1-123.
DR   PDB; 4V6N; EM; 12.10 A; AM=1-123.
DR   PDB; 4V6O; EM; 14.70 A; BM=1-123.
DR   PDB; 4V6P; EM; 13.50 A; BM=1-123.
DR   PDB; 4V6Q; EM; 11.50 A; BM=1-123.
DR   PDB; 4V6R; EM; 11.50 A; BM=1-123.
DR   PDB; 4V6S; EM; 13.10 A; AM=1-123.
DR   PDB; 4V6T; EM; 8.30 A; BK=1-122.
DR   PDB; 4V6V; EM; 9.80 A; BO=1-123.
DR   PDB; 4V6Y; EM; 12.00 A; BK=1-122.
DR   PDB; 4V6Z; EM; 12.00 A; BK=1-122.
DR   PDB; 4V70; EM; 17.00 A; BK=1-122.
DR   PDB; 4V71; EM; 20.00 A; BK=1-122.
DR   PDB; 4V72; EM; 13.00 A; BK=1-122.
DR   PDB; 4V73; EM; 15.00 A; BK=1-122.
DR   PDB; 4V74; EM; 17.00 A; BK=1-122.
DR   PDB; 4V75; EM; 12.00 A; BK=1-122.
DR   PDB; 4V76; EM; 17.00 A; BK=1-122.
DR   PDB; 4V77; EM; 17.00 A; BK=1-122.
DR   PDB; 4V78; EM; 20.00 A; BK=1-122.
DR   PDB; 4V79; EM; 15.00 A; BK=1-122.
DR   PDB; 4V7A; EM; 9.00 A; BK=1-122.
DR   PDB; 4V7B; EM; 6.80 A; BK=1-123.
DR   PDB; 4V7C; EM; 7.60 A; BM=1-123.
DR   PDB; 4V7D; EM; 7.60 A; AN=1-123.
DR   PDB; 4V7I; EM; 9.60 A; AK=1-123.
DR   PDB; 4V7S; X-ray; 3.25 A; BK/DK=1-122.
DR   PDB; 4V7T; X-ray; 3.19 A; BK/DK=1-122.
DR   PDB; 4V7U; X-ray; 3.10 A; BK/DK=1-122.
DR   PDB; 4V7V; X-ray; 3.29 A; BK/DK=1-122.
DR   PDB; 4V85; X-ray; 3.20 A; BO=1-123.
DR   PDB; 4V89; X-ray; 3.70 A; BO=1-123.
DR   PDB; 4V9C; X-ray; 3.30 A; BK/DK=1-123.
DR   PDB; 4V9D; X-ray; 3.00 A; CK/DK=1-122.
DR   PDB; 4V9O; X-ray; 2.90 A; AK/CK/EK/GK=1-123.
DR   PDB; 4V9P; X-ray; 2.90 A; AK/CK/EK/GK=1-123.
DR   PDB; 4WF1; X-ray; 3.09 A; BK/DK=1-122.
DR   PDB; 4WOI; X-ray; 3.00 A; BK/CK=1-123.
DR   PDB; 4WWW; X-ray; 3.10 A; RK/YK=1-122.
DR   PDB; 4YBB; X-ray; 2.10 A; CL/DL=1-123.
DR   PDB; 5ADY; EM; 4.50 A; K=1-123.
DR   PDB; 5AFI; EM; 2.90 A; K=1-123.
DR   PDB; 5AKA; EM; 5.70 A; K=1-123.
DR   PDB; 5GAD; EM; 3.70 A; L=1-123.
DR   PDB; 5GAE; EM; 3.33 A; L=1-123.
DR   PDB; 5GAF; EM; 4.30 A; L=1-123.
DR   PDB; 5GAG; EM; 3.80 A; L=1-123.
DR   PDB; 5GAH; EM; 3.80 A; L=1-123.
DR   PDB; 5H5U; EM; 3.00 A; L=1-123.
DR   PDB; 5IQR; EM; 3.00 A; K=1-123.
DR   PDB; 5IT8; X-ray; 3.12 A; CL/DL=1-123.
DR   PDB; 5J5B; X-ray; 2.80 A; CL/DL=1-123.
DR   PDB; 5J7L; X-ray; 3.00 A; CL/DL=1-123.
DR   PDB; 5J88; X-ray; 3.32 A; CL/DL=1-123.
DR   PDB; 5J8A; X-ray; 3.10 A; CL/DL=1-123.
DR   PDB; 5J91; X-ray; 2.96 A; CL/DL=1-123.
DR   PDB; 5JC9; X-ray; 3.03 A; CL/DL=1-123.
DR   PDB; 5JTE; EM; 3.60 A; BK=1-123.
DR   PDB; 5JU8; EM; 3.60 A; BK=1-123.
DR   PDB; 5KCR; EM; 3.60 A; 1O=1-123.
DR   PDB; 5KCS; EM; 3.90 A; 1O=1-123.
DR   PDB; 5KPS; EM; 3.90 A; K=1-123.
DR   PDB; 5KPV; EM; 4.10 A; J=1-123.
DR   PDB; 5KPW; EM; 3.90 A; J=1-123.
DR   PDB; 5KPX; EM; 3.90 A; J=1-123.
DR   PDB; 5L3P; EM; 3.70 A; O=1-123.
DR   PDB; 5LZA; EM; 3.60 A; K=1-122.
DR   PDB; 5LZB; EM; 5.30 A; K=1-122.
DR   PDB; 5LZC; EM; 4.80 A; K=1-122.
DR   PDB; 5LZD; EM; 3.40 A; K=1-122.
DR   PDB; 5LZE; EM; 3.50 A; K=1-122.
DR   PDB; 5LZF; EM; 4.60 A; K=1-122.
DR   PDB; 5MDV; EM; 2.97 A; K=1-123.
DR   PDB; 5MDW; EM; 3.06 A; K=1-123.
DR   PDB; 5MDY; EM; 3.35 A; K=1-123.
DR   PDB; 5MDZ; EM; 3.10 A; K=1-123.
DR   PDB; 5MGP; EM; 3.10 A; K=1-122.
DR   PDB; 5NCO; EM; 4.80 A; L=1-123.
DR   PDB; 5NP6; EM; 3.60 A; i=1-122.
DR   PDB; 5NWY; EM; 2.93 A; X=1-123.
DR   PDB; 5O2R; EM; 3.40 A; K=1-122.
DR   PDB; 5U4I; EM; 3.50 A; L=1-123.
DR   PDB; 5U9F; EM; 3.20 A; 13=1-123.
DR   PDB; 5U9G; EM; 3.20 A; 13=1-123.
DR   PDB; 5UYK; EM; 3.90 A; 13=1-122.
DR   PDB; 5UYL; EM; 3.60 A; 13=1-122.
DR   PDB; 5UYM; EM; 3.20 A; 13=1-122.
DR   PDB; 5UYN; EM; 4.00 A; 13=1-122.
DR   PDB; 5UYP; EM; 3.90 A; 13=1-122.
DR   PDB; 5UYQ; EM; 3.80 A; 13=1-122.
DR   PDB; 5WDT; EM; 3.00 A; K=1-122.
DR   PDB; 5WE4; EM; 3.10 A; K=1-122.
DR   PDB; 5WFK; EM; 3.40 A; K=1-122.
DR   PDB; 6BU8; EM; 3.50 A; 13=1-122.
DR   PDB; 6BY1; X-ray; 3.94 A; CK/DK=1-122.
DR   PDB; 6C4I; EM; 3.24 A; L=1-123.
DR   PDB; 6ENF; EM; 3.20 A; K=1-122.
DR   PDB; 6ENJ; EM; 3.70 A; K=1-122.
DR   PDB; 6ENU; EM; 3.10 A; K=1-122.
DR   PDB; 6GBZ; EM; 3.80 A; K=1-122.
DR   PDB; 6GC0; EM; 3.80 A; K=1-122.
DR   PDB; 6GC4; EM; 4.30 A; K=1-122.
DR   PDB; 6GC6; EM; 4.30 A; K=1-122.
DR   PDB; 6GC7; EM; 4.30 A; K=1-122.
DR   PDB; 6GC8; EM; 3.80 A; K=1-122.
DR   PDB; 6GWT; EM; 3.80 A; K=1-122.
DR   PDB; 6GXM; EM; 3.80 A; K=1-122.
DR   PDB; 6GXN; EM; 3.90 A; K=1-122.
DR   PDB; 6GXO; EM; 3.90 A; K=1-122.
DR   PDB; 6GXP; EM; 4.40 A; K=1-122.
DR   PDB; 6H4N; EM; 3.00 A; K=1-122.
DR   PDB; 6H58; EM; 7.90 A; K/KK=1-122.
DR   PDB; 6HRM; EM; 2.96 A; K=1-123.
DR   PDB; 6I0Y; EM; 3.20 A; K=1-122.
DR   PDB; 6I7V; X-ray; 2.90 A; CL/DL=1-123.
DR   PDB; 6O9J; EM; 3.90 A; K=2-122.
DR   PDB; 6O9K; EM; 4.00 A; K=1-122.
DR   PDB; 6OFX; EM; 3.30 A; k=1-122.
DR   PDB; 6OG7; EM; 3.30 A; k=1-122.
DR   PDB; 6ORE; EM; 2.90 A; K=1-123.
DR   PDB; 6ORL; EM; 3.50 A; K=1-123.
DR   PDB; 6OST; EM; 4.20 A; K=1-123.
DR   PDB; 6OT3; EM; 3.90 A; K=1-123.
DR   PDB; 6OUO; EM; 3.70 A; K=1-123.
DR   PDB; 6Q97; EM; 3.90 A; K=1-123.
DR   PDB; 6Q98; EM; 4.30 A; K=1-123.
DR   PDB; 6Q9A; EM; 3.70 A; K=1-123.
DR   PDB; 6QDW; EM; 2.83 A; k=1-123.
DR   PDB; 6QUL; EM; 3.00 A; L=1-123.
DR   PDB; 6S0K; EM; 3.10 A; L=1-123.
DR   PDB; 6SZS; EM; 3.06 A; K=1-123.
DR   PDB; 6TBV; EM; 2.70 A; L141=1-123.
DR   PDB; 6TC3; EM; 2.70 A; L141=1-123.
DR   PDB; 6VWL; EM; 3.10 A; I=1-123.
DR   PDB; 6VWM; EM; 3.40 A; I=1-123.
DR   PDB; 6VWN; EM; 3.40 A; I=1-123.
DR   PDB; 6WD6; EM; 3.70 A; k=1-122.
DR   PDB; 6WDB; EM; 4.00 A; k=1-122.
DR   PDB; 6WDC; EM; 4.20 A; k=1-122.
DR   PDB; 6WDD; EM; 3.20 A; k=1-122.
DR   PDB; 6WDE; EM; 3.00 A; k=1-122.
DR   PDB; 6WDF; EM; 3.30 A; k=1-122.
DR   PDB; 6WDG; EM; 3.30 A; k=1-122.
DR   PDB; 6WDH; EM; 4.30 A; k=1-122.
DR   PDB; 6WDI; EM; 4.00 A; k=1-122.
DR   PDB; 6WDJ; EM; 3.70 A; k=1-122.
DR   PDB; 6WDK; EM; 3.60 A; k=1-122.
DR   PDB; 6WDL; EM; 3.70 A; k=1-122.
DR   PDB; 6WDM; EM; 3.60 A; k=1-122.
DR   PDB; 6WNT; EM; 3.10 A; k=1-122.
DR   PDB; 6WNV; EM; 3.50 A; k=1-122.
DR   PDB; 6WNW; EM; 3.20 A; k=1-122.
DR   PDB; 6XZ7; EM; 2.10 A; K=1-123.
DR   PDB; 6XZA; EM; 2.66 A; K2=1-123.
DR   PDB; 6XZB; EM; 2.54 A; K2=1-123.
DR   PDB; 6Y69; EM; 2.86 A; K=1-122.
DR   PDB; 6YS3; EM; 2.58 A; k=1-123.
DR   PDB; 6YSR; EM; 3.10 A; K=1-123.
DR   PDB; 6YSS; EM; 2.60 A; K=1-123.
DR   PDB; 6YST; EM; 3.20 A; K=1-123.
DR   PDB; 6YSU; EM; 3.70 A; K=1-123.
DR   PDB; 6ZTJ; EM; 3.40 A; BL=1-123.
DR   PDB; 6ZTL; EM; 3.50 A; BL=1-123.
DR   PDB; 6ZTM; EM; 3.30 A; BL=1-123.
DR   PDB; 6ZTN; EM; 3.90 A; BL=1-123.
DR   PDB; 6ZTO; EM; 3.00 A; BL=1-123.
DR   PDB; 6ZTP; EM; 3.00 A; BL=1-123.
DR   PDB; 6ZU1; EM; 3.00 A; BL=1-123.
DR   PDB; 7ABZ; EM; 3.21 A; K=1-122.
DR   PDB; 7AC7; EM; 3.08 A; K=1-123.
DR   PDB; 7ACJ; EM; 3.20 A; K=1-123.
DR   PDB; 7ACR; EM; 3.44 A; K=1-123.
DR   PDB; 7B5K; EM; 2.90 A; K=1-123.
DR   PDB; 7BL2; EM; 3.70 A; K=1-123.
DR   PDB; 7BL3; EM; 3.50 A; K=1-123.
DR   PDB; 7BL4; EM; 2.40 A; K=1-123.
DR   PDB; 7BL5; EM; 3.30 A; K=1-123.
DR   PDB; 7BL6; EM; 4.00 A; K=1-123.
DR   PDB; 7BV8; EM; 3.14 A; L=1-123.
DR   PDB; 7D6Z; EM; 3.40 A; K=1-123.
DR   PDB; 7D80; EM; 4.10 A; j=1-123.
DR   PDB; 7JSS; EM; 3.70 A; k=1-122.
DR   PDB; 7JSW; EM; 3.80 A; k=1-122.
DR   PDB; 7JSZ; EM; 3.70 A; k=1-122.
DR   PDB; 7JT1; EM; 3.30 A; k=1-122.
DR   PDB; 7JT2; EM; 3.50 A; k=1-122.
DR   PDB; 7JT3; EM; 3.70 A; k=1-122.
DR   PDB; 7K50; EM; 3.40 A; k=1-122.
DR   PDB; 7K51; EM; 3.50 A; k=1-122.
DR   PDB; 7K52; EM; 3.40 A; k=1-122.
DR   PDB; 7K53; EM; 3.20 A; k=1-122.
DR   PDB; 7K54; EM; 3.20 A; k=1-122.
DR   PDB; 7K55; EM; 3.30 A; k=1-122.
DR   PDB; 7LV0; EM; 3.20 A; k=1-122.
DR   PDB; 7N1P; EM; 2.33 A; LN=1-123.
DR   PDB; 7N2C; EM; 2.72 A; LN=1-123.
DR   PDB; 7N2U; EM; 2.53 A; LN=1-123.
DR   PDB; 7N2V; EM; 2.54 A; LN=1-123.
DR   PDB; 7N30; EM; 2.66 A; LN=1-123.
DR   PDB; 7N31; EM; 2.69 A; LN=1-123.
DR   PDB; 7NBU; EM; 3.11 A; j=1-123.
DR   PDB; 7NWT; EM; 2.66 A; K=1-123.
DR   PDB; 7NWW; EM; 3.05 A; J=1-123.
DR   PDB; 7O19; EM; 2.90 A; BK=1-123.
DR   PDB; 7O1A; EM; 2.40 A; BK=1-123.
DR   PDB; 7O1C; EM; 2.60 A; BK=1-123.
DR   PDB; 7OIF; EM; 3.00 A; J=1-123.
DR   PDB; 7OIG; EM; 3.20 A; J=1-123.
DR   PDB; 7OII; EM; 3.00 A; J=1-123.
DR   PDB; 7OIZ; EM; 2.90 A; j=1-123.
DR   PDB; 7OJ0; EM; 3.50 A; j=1-123.
DR   PDB; 7OT5; EM; 2.90 A; J=1-123.
DR   PDB; 7P3K; EM; 2.90 A; j=1-123.
DR   PDB; 7PJS; EM; 2.35 A; K=1-123.
DR   PDB; 7PJT; EM; 6.00 A; K=1-123.
DR   PDB; 7PJV; EM; 3.10 A; K=1-123.
DR   PDB; 7PJW; EM; 4.00 A; K=1-123.
DR   PDB; 7PJX; EM; 6.50 A; K=1-123.
DR   PDB; 7PJY; EM; 3.10 A; K=1-123.
DR   PDB; 7PJZ; EM; 6.00 A; K=1-123.
DR   PDB; 7QG8; EM; 3.97 A; X=1-123.
DR   PDB; 7QGH; EM; 4.48 A; X=1-123.
DR   PDB; 7SS9; EM; 3.90 A; k=1-122.
DR   PDB; 7SSD; EM; 3.30 A; k=1-122.
DR   PDB; 7SSL; EM; 3.80 A; k=1-122.
DR   PDB; 7SSN; EM; 3.20 A; k=1-122.
DR   PDB; 7SSO; EM; 3.20 A; k=1-122.
DR   PDB; 7SSW; EM; 3.80 A; k=1-122.
DR   PDB; 7ST2; EM; 2.90 A; k=1-122.
DR   PDB; 7ST6; EM; 3.00 A; k=1-122.
DR   PDB; 7ST7; EM; 3.20 A; k=1-122.
DR   PDBsum; 1ML5; -.
DR   PDBsum; 2J28; -.
DR   PDBsum; 2RDO; -.
DR   PDBsum; 3BBX; -.
DR   PDBsum; 3IY9; -.
DR   PDBsum; 3IZZ; -.
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; 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; 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; 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; 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; 6QDW; -.
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; 7NWW; -.
DR   PDBsum; 7O19; -.
DR   PDBsum; 7O1A; -.
DR   PDBsum; 7O1C; -.
DR   PDBsum; 7OIF; -.
DR   PDBsum; 7OIG; -.
DR   PDBsum; 7OII; -.
DR   PDBsum; 7OIZ; -.
DR   PDBsum; 7OJ0; -.
DR   PDBsum; 7OT5; -.
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; P0ADY3; -.
DR   SMR; P0ADY3; -.
DR   BioGRID; 852121; 1.
DR   ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR   DIP; DIP-35798N; -.
DR   IntAct; P0ADY3; 64.
DR   STRING; 511145.b3310; -.
DR   MoonProt; P0ADY3; -.
DR   jPOST; P0ADY3; -.
DR   PaxDb; P0ADY3; -.
DR   PRIDE; P0ADY3; -.
DR   EnsemblBacteria; AAC76335; AAC76335; b3310.
DR   EnsemblBacteria; BAE77981; BAE77981; BAE77981.
DR   GeneID; 67415351; -.
DR   GeneID; 947809; -.
DR   KEGG; ecj:JW3272; -.
DR   KEGG; eco:b3310; -.
DR   PATRIC; fig|1411691.4.peg.3421; -.
DR   EchoBASE; EB0868; -.
DR   eggNOG; COG0093; Bacteria.
DR   HOGENOM; CLU_095071_2_1_6; -.
DR   InParanoid; P0ADY3; -.
DR   OMA; AKEVLCI; -.
DR   PhylomeDB; P0ADY3; -.
DR   BioCyc; EcoCyc:EG10875-MON; -.
DR   BioCyc; MetaCyc:EG10875-MON; -.
DR   EvolutionaryTrace; P0ADY3; -.
DR   PRO; PR:P0ADY3; -.
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:0070180; F:large ribosomal subunit rRNA binding; IDA:EcoCyc.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR   Gene3D; 2.40.150.20; -; 1.
DR   HAMAP; MF_01367; Ribosomal_L14; 1.
DR   InterPro; IPR036853; Ribosomal_L14_sf.
DR   InterPro; IPR000218; Ribosomal_L14P.
DR   InterPro; IPR005745; Ribosomal_L14P_bac-type.
DR   InterPro; IPR019972; Ribosomal_L14P_CS.
DR   PANTHER; PTHR11761; PTHR11761; 1.
DR   Pfam; PF00238; Ribosomal_L14; 1.
DR   SMART; SM01374; Ribosomal_L14; 1.
DR   SUPFAM; SSF50193; SSF50193; 1.
DR   TIGRFAMs; TIGR01067; rplN_bact; 1.
DR   PROSITE; PS00049; RIBOSOMAL_L14; 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..123
FT                   /note="50S ribosomal protein L14"
FT                   /id="PRO_0000128540"
FT   MUTAGEN         97
FT                   /note="T->A: Reduced RsfS binding."
FT                   /evidence="ECO:0000269|PubMed:22829778"
FT   MUTAGEN         98
FT                   /note="R->A: Reduced RsfS binding."
FT                   /evidence="ECO:0000269|PubMed:22829778"
FT   MUTAGEN         114
FT                   /note="K->A: Reduced RsfS binding."
FT                   /evidence="ECO:0000269|PubMed:22829778"
FT   MUTAGEN         117
FT                   /note="S->A: No change in RsfS binding."
FT                   /evidence="ECO:0000269|PubMed:22829778"
FT   CONFLICT        63
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="C -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90..91
FT                   /note="NS -> TD (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          12..24
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          38..46
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:6I0Y"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:6QUL"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:6YS3"
FT   HELIX           113..118
FT                   /evidence="ECO:0007829|PDB:6XZ7"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:6QUL"
SQ   SEQUENCE   123 AA;  13541 MW;  192ACB1623979510 CRC64;
     MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG KVKKGDVLKA
     VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF GPVTRELRSE KFMKIISLAP
     EVL
 
 
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