RL22_ECOLI
ID RL22_ECOLI Reviewed; 110 AA.
AC P61175; P02423; Q2M6Y0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=50S ribosomal protein L22;
DE AltName: Full=Large ribosomal subunit protein uL22 {ECO:0000303|PubMed:24524803};
GN Name=rplV; Synonyms=eryB; OrderedLocusNames=b3315, JW3277;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RX PubMed=7007072; DOI=10.1016/0014-5793(80)81276-2;
RA Wittmann-Liebold B., Greuer B.;
RT "Amino acid sequence of protein L22 from the large subunit of the
RT Escherichia coli ribosome.";
RL FEBS Lett. 121:105-112(1980).
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 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 [6]
RP CHARACTERIZATION OF ERYTHROMYCIN-RESISTANT VARIANT N281.
RC STRAIN=N281;
RX PubMed=4589347; DOI=10.1007/bf00333665;
RA Wittmann H.G., Stoffler G., Apirion D., Rosen L., Tanaka K., Tamaki M.,
RA Takata R., Dekio S., Otaka E.;
RT "Biochemical and genetic studies on two different types of erythromycin
RT resistant mutants of Escherichia coli with altered ribosomal proteins.";
RL Mol. Gen. Genet. 127:175-189(1973).
RN [7]
RP TEMPERATURE-SENSITIVE VARIANT.
RC STRAIN=SK1048;
RX PubMed=7729693; DOI=10.1007/bf01429216;
RA Burnette-Vick B., Champney W.S., Musich P.R.;
RT "A temperature-sensitive mutant of Escherichia coli with an alteration in
RT ribosomal protein L22.";
RL Genetica 94:17-25(1994).
RN [8]
RP IDENTIFICATION OF CHANGES IN ERYTHROMYCIN-RESISTANT VARIANT N281.
RC STRAIN=N281;
RX PubMed=7928988; DOI=10.1128/jb.176.20.6192-6198.1994;
RA Chittum H.S., Champney W.S.;
RT "Ribosomal protein gene sequence changes in erythromycin-resistant mutants
RT of Escherichia coli.";
RL J. Bacteriol. 176:6192-6198(1994).
RN [9]
RP ERYTHROMYCIN AND RIBOSOME ASSEMBLY.
RC STRAIN=N281, and SK901;
RX PubMed=7766155; DOI=10.1007/bf00295501;
RA Chittum H.S., Champney W.S.;
RT "Erythromycin inhibits the assembly of the large ribosomal subunit in
RT growing Escherichia coli cells.";
RL Curr. Microbiol. 30:273-279(1995).
RN [10]
RP MUTAGENESIS OF GLY-91 AND ALA-93.
RX PubMed=11893334; DOI=10.1016/s0092-8674(02)00649-9;
RA Nakatogawa H., Ito K.;
RT "The ribosomal exit tunnel functions as a discriminating gate.";
RL Cell 108:629-636(2002).
RN [11]
RP MUTAGENESIS TO EXAMINE REQUIREMENTS FOR RIBOSOME ASSEMBLY.
RC STRAIN=K12 / LL308;
RX PubMed=13130133; DOI=10.1261/rna.5400703;
RA Zengel J.M., Jerauld A., Walker A., Wahl M.C., Lindahl L.;
RT "The extended loops of ribosomal proteins L4 and L22 are not required for
RT ribosome assembly or L4-mediated autogenous control.";
RL RNA 9:1188-1197(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 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 [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (17.1 ANGSTROMS), EFFECT OF THE
RP ERYTHROMYCIN-RESISTANT VARIANT ON THE POLYPEPTIDE EXIT TUNNEL, AND SUBUNIT.
RC STRAIN=N281;
RX PubMed=11511371; DOI=10.1016/s1097-2765(01)00293-3;
RA Gabashvili I.S., Gregory S.T., Valle M., Grassucci R., Worbs M., Wahl M.C.,
RA Dahlberg A.E., Frank J.;
RT "The polypeptide tunnel system in the ribosome and its gating in
RT erythromycin resistance mutants of L4 and L22.";
RL Mol. Cell 8:181-188(2001).
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 TNAC-STALLED 50S
RP 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 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 [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: This protein binds specifically to 23S rRNA; its binding is
CC stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is
CC important during the early stages of 50S assembly. It makes multiple
CC contacts with different domains of the 23S rRNA in the assembled 50S
CC subunit and ribosome. {ECO:0000269|PubMed:7766155}.
CC -!- FUNCTION: The globular domain of the protein is one of the proteins
CC that surrounds the polypeptide exit tunnel on the outside of the
CC subunit, while an extended beta-hairpin is found that penetrates into
CC the center of the 70S ribosome where it lines the wall of the exit
CC tunnel. Removal of most of this hairpin (residues 85-95) does not
CC prevent its incorporation into 70S ribosomes. Two of the hairpin
CC residues (91 and 93) seem to be involved in translation elongation
CC arrest of the SecM protein, as their replacement by larger amino acids
CC alleviates the arrest. {ECO:0000269|PubMed:11893334,
CC ECO:0000269|PubMed:13130133}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:11511371,
CC ECO:0000269|PubMed:12809609, 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:7007072}.
CC -!- INTERACTION:
CC P61175; P0A6K3: def; NbExp=3; IntAct=EBI-542255, EBI-548913;
CC P61175; P17993: ubiG; NbExp=3; IntAct=EBI-542255, EBI-559367;
CC -!- MASS SPECTROMETRY: Mass=12225.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: The wild-type allele (erythromycin sensitive) is
CC dominant over the resistant allele, and is also dominant over the
CC temperature-sensitive allele at both low and high temperatures.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02613; CAA26465.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58112.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76340.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77976.1; -; Genomic_DNA.
DR PIR; G23129; R5EC22.
DR RefSeq; NP_417774.1; NC_000913.3.
DR RefSeq; WP_000447529.1; NZ_STEB01000038.1.
DR PDB; 2J28; EM; 8.00 A; S=1-110.
DR PDB; 2RDO; EM; 9.10 A; S=1-110.
DR PDB; 3BBX; EM; 10.00 A; S=1-110.
DR PDB; 3J5L; EM; 6.60 A; S=1-110.
DR PDB; 3J7Z; EM; 3.90 A; S=1-110.
DR PDB; 3J8G; EM; 5.00 A; S=1-110.
DR PDB; 3J9Y; EM; 3.90 A; S=1-110.
DR PDB; 3J9Z; EM; 3.60 A; LQ=1-110.
DR PDB; 3JA1; EM; 3.60 A; LU=1-110.
DR PDB; 3JBU; EM; 3.64 A; s=1-110.
DR PDB; 3JBV; EM; 3.32 A; s=1-110.
DR PDB; 3JCD; EM; 3.70 A; S=1-110.
DR PDB; 3JCE; EM; 3.20 A; S=1-110.
DR PDB; 3JCJ; EM; 3.70 A; R=1-110.
DR PDB; 3JCN; EM; 4.60 A; S=1-110.
DR PDB; 4CSU; EM; 5.50 A; S=1-110.
DR PDB; 4U1U; X-ray; 2.95 A; BS/DS=1-110.
DR PDB; 4U1V; X-ray; 3.00 A; BS/DS=1-110.
DR PDB; 4U20; X-ray; 2.90 A; BS/DS=1-110.
DR PDB; 4U24; X-ray; 2.90 A; BS/DS=1-110.
DR PDB; 4U25; X-ray; 2.90 A; BS/DS=1-110.
DR PDB; 4U26; X-ray; 2.80 A; BS/DS=1-110.
DR PDB; 4U27; X-ray; 2.80 A; BS/DS=1-110.
DR PDB; 4UY8; EM; 3.80 A; S=1-110.
DR PDB; 4V47; EM; 12.30 A; AQ=1-110.
DR PDB; 4V48; EM; 11.50 A; AQ=1-110.
DR PDB; 4V4H; X-ray; 3.46 A; BS/DS=1-110.
DR PDB; 4V4Q; X-ray; 3.46 A; BS/DS=1-110.
DR PDB; 4V4V; EM; 15.00 A; BQ=5-110.
DR PDB; 4V4W; EM; 15.00 A; BQ=5-110.
DR PDB; 4V50; X-ray; 3.22 A; BS/DS=1-110.
DR PDB; 4V52; X-ray; 3.21 A; BS/DS=1-110.
DR PDB; 4V53; X-ray; 3.54 A; BS/DS=1-110.
DR PDB; 4V54; X-ray; 3.30 A; BS/DS=1-110.
DR PDB; 4V55; X-ray; 4.00 A; BS/DS=1-110.
DR PDB; 4V56; X-ray; 3.93 A; BS/DS=1-110.
DR PDB; 4V57; X-ray; 3.50 A; BS/DS=1-110.
DR PDB; 4V5B; X-ray; 3.74 A; AS/CS=1-110.
DR PDB; 4V5H; EM; 5.80 A; BS=1-110.
DR PDB; 4V5Y; X-ray; 4.45 A; BS/DS=1-110.
DR PDB; 4V64; X-ray; 3.50 A; BS/DS=1-110.
DR PDB; 4V65; EM; 9.00 A; BL=1-110.
DR PDB; 4V66; EM; 9.00 A; BL=1-110.
DR PDB; 4V69; EM; 6.70 A; BS=1-110.
DR PDB; 4V6C; X-ray; 3.19 A; BS/DS=1-110.
DR PDB; 4V6D; X-ray; 3.81 A; BS/DS=1-110.
DR PDB; 4V6E; X-ray; 3.71 A; BS/DS=1-110.
DR PDB; 4V6K; EM; 8.25 A; AT=1-110.
DR PDB; 4V6L; EM; 13.20 A; BT=1-110.
DR PDB; 4V6M; EM; 7.10 A; BS=1-110.
DR PDB; 4V6N; EM; 12.10 A; AU=1-110.
DR PDB; 4V6O; EM; 14.70 A; BU=1-110.
DR PDB; 4V6P; EM; 13.50 A; BU=1-110.
DR PDB; 4V6Q; EM; 11.50 A; BU=1-110.
DR PDB; 4V6R; EM; 11.50 A; BU=1-110.
DR PDB; 4V6S; EM; 13.10 A; AU=1-110.
DR PDB; 4V6T; EM; 8.30 A; BS=1-110.
DR PDB; 4V6V; EM; 9.80 A; BW=1-110.
DR PDB; 4V6Y; EM; 12.00 A; BS=1-110.
DR PDB; 4V6Z; EM; 12.00 A; BS=1-110.
DR PDB; 4V70; EM; 17.00 A; BS=1-110.
DR PDB; 4V71; EM; 20.00 A; BS=1-110.
DR PDB; 4V72; EM; 13.00 A; BS=1-110.
DR PDB; 4V73; EM; 15.00 A; BS=1-110.
DR PDB; 4V74; EM; 17.00 A; BS=1-110.
DR PDB; 4V75; EM; 12.00 A; BS=1-110.
DR PDB; 4V76; EM; 17.00 A; BS=1-110.
DR PDB; 4V77; EM; 17.00 A; BS=1-110.
DR PDB; 4V78; EM; 20.00 A; BS=1-110.
DR PDB; 4V79; EM; 15.00 A; BS=1-110.
DR PDB; 4V7A; EM; 9.00 A; BS=1-110.
DR PDB; 4V7B; EM; 6.80 A; BS=1-110.
DR PDB; 4V7C; EM; 7.60 A; BU=1-110.
DR PDB; 4V7D; EM; 7.60 A; AV=1-110.
DR PDB; 4V7I; EM; 9.60 A; AS=1-110.
DR PDB; 4V7S; X-ray; 3.25 A; BS/DS=1-110.
DR PDB; 4V7T; X-ray; 3.19 A; BS/DS=1-110.
DR PDB; 4V7U; X-ray; 3.10 A; BS/DS=1-110.
DR PDB; 4V7V; X-ray; 3.29 A; BS/DS=1-110.
DR PDB; 4V85; X-ray; 3.20 A; BW=1-110.
DR PDB; 4V89; X-ray; 3.70 A; BW=1-110.
DR PDB; 4V9C; X-ray; 3.30 A; BS/DS=1-110.
DR PDB; 4V9D; X-ray; 3.00 A; CS/DS=1-110.
DR PDB; 4V9O; X-ray; 2.90 A; AS/CS/ES/GS=1-110.
DR PDB; 4V9P; X-ray; 2.90 A; AS/CS/ES/GS=1-110.
DR PDB; 4WF1; X-ray; 3.09 A; BS/DS=1-110.
DR PDB; 4WOI; X-ray; 3.00 A; BS/CS=1-110.
DR PDB; 4WWW; X-ray; 3.10 A; RS/YS=1-110.
DR PDB; 4YBB; X-ray; 2.10 A; CT/DT=1-110.
DR PDB; 5ADY; EM; 4.50 A; S=1-110.
DR PDB; 5AFI; EM; 2.90 A; S=1-110.
DR PDB; 5AKA; EM; 5.70 A; S=1-110.
DR PDB; 5GAD; EM; 3.70 A; T=1-110.
DR PDB; 5GAE; EM; 3.33 A; T=1-110.
DR PDB; 5GAF; EM; 4.30 A; T=1-110.
DR PDB; 5GAG; EM; 3.80 A; T=1-110.
DR PDB; 5GAH; EM; 3.80 A; T=1-110.
DR PDB; 5H5U; EM; 3.00 A; T=1-110.
DR PDB; 5IQR; EM; 3.00 A; S=1-110.
DR PDB; 5IT8; X-ray; 3.12 A; CT/DT=1-110.
DR PDB; 5J5B; X-ray; 2.80 A; CT/DT=1-110.
DR PDB; 5J7L; X-ray; 3.00 A; CT/DT=1-110.
DR PDB; 5J88; X-ray; 3.32 A; CT/DT=1-110.
DR PDB; 5J8A; X-ray; 3.10 A; CT/DT=1-110.
DR PDB; 5J91; X-ray; 2.96 A; CT/DT=1-110.
DR PDB; 5JC9; X-ray; 3.03 A; CT/DT=1-110.
DR PDB; 5JTE; EM; 3.60 A; BS=1-110.
DR PDB; 5JU8; EM; 3.60 A; BS=1-110.
DR PDB; 5KCR; EM; 3.60 A; 1W=1-110.
DR PDB; 5KCS; EM; 3.90 A; 1W=1-110.
DR PDB; 5KPS; EM; 3.90 A; S=1-110.
DR PDB; 5KPV; EM; 4.10 A; R=1-110.
DR PDB; 5KPW; EM; 3.90 A; R=1-110.
DR PDB; 5KPX; EM; 3.90 A; R=1-110.
DR PDB; 5L3P; EM; 3.70 A; W=1-110.
DR PDB; 5LZA; EM; 3.60 A; S=1-110.
DR PDB; 5LZB; EM; 5.30 A; S=1-110.
DR PDB; 5LZC; EM; 4.80 A; S=1-110.
DR PDB; 5LZD; EM; 3.40 A; S=1-110.
DR PDB; 5LZE; EM; 3.50 A; S=1-110.
DR PDB; 5LZF; EM; 4.60 A; S=1-110.
DR PDB; 5MDV; EM; 2.97 A; S=1-110.
DR PDB; 5MDW; EM; 3.06 A; S=1-110.
DR PDB; 5MDY; EM; 3.35 A; S=1-110.
DR PDB; 5MDZ; EM; 3.10 A; S=1-110.
DR PDB; 5MGP; EM; 3.10 A; S=1-110.
DR PDB; 5NCO; EM; 4.80 A; T=1-110.
DR PDB; 5NP6; EM; 3.60 A; q=1-110.
DR PDB; 5NWY; EM; 2.93 A; f=1-110.
DR PDB; 5O2R; EM; 3.40 A; S=1-110.
DR PDB; 5U4I; EM; 3.50 A; T=1-110.
DR PDB; 5U9F; EM; 3.20 A; 21=1-110.
DR PDB; 5U9G; EM; 3.20 A; 21=1-110.
DR PDB; 5UYK; EM; 3.90 A; 21=1-110.
DR PDB; 5UYL; EM; 3.60 A; 21=1-110.
DR PDB; 5UYM; EM; 3.20 A; 21=1-110.
DR PDB; 5UYN; EM; 4.00 A; 21=1-110.
DR PDB; 5UYP; EM; 3.90 A; 21=1-110.
DR PDB; 5UYQ; EM; 3.80 A; 21=1-110.
DR PDB; 5WDT; EM; 3.00 A; S=1-109.
DR PDB; 5WE4; EM; 3.10 A; S=1-109.
DR PDB; 5WE6; EM; 3.40 A; S=1-109.
DR PDB; 5WFK; EM; 3.40 A; S=1-109.
DR PDB; 6BU8; EM; 3.50 A; 21=1-110.
DR PDB; 6BY1; X-ray; 3.94 A; CS/DS=1-110.
DR PDB; 6C4I; EM; 3.24 A; T=1-110.
DR PDB; 6ENF; EM; 3.20 A; S=1-110.
DR PDB; 6ENJ; EM; 3.70 A; S=1-110.
DR PDB; 6ENU; EM; 3.10 A; S=1-110.
DR PDB; 6GBZ; EM; 3.80 A; S=1-110.
DR PDB; 6GC0; EM; 3.80 A; S=1-110.
DR PDB; 6GC4; EM; 4.30 A; S=1-110.
DR PDB; 6GC6; EM; 4.30 A; S=1-110.
DR PDB; 6GC7; EM; 4.30 A; S=1-110.
DR PDB; 6GC8; EM; 3.80 A; S=1-110.
DR PDB; 6GWT; EM; 3.80 A; S=1-110.
DR PDB; 6GXM; EM; 3.80 A; S=1-110.
DR PDB; 6GXN; EM; 3.90 A; S=1-110.
DR PDB; 6GXO; EM; 3.90 A; S=1-110.
DR PDB; 6GXP; EM; 4.40 A; S=1-110.
DR PDB; 6H4N; EM; 3.00 A; S=1-110.
DR PDB; 6H58; EM; 7.90 A; S/SS=1-110.
DR PDB; 6HRM; EM; 2.96 A; S=1-110.
DR PDB; 6I0Y; EM; 3.20 A; S=1-110.
DR PDB; 6I7V; X-ray; 2.90 A; CT/DT=1-110.
DR PDB; 6O9J; EM; 3.90 A; S=1-110.
DR PDB; 6O9K; EM; 4.00 A; S=1-110.
DR PDB; 6OFX; EM; 3.30 A; s=1-110.
DR PDB; 6OG7; EM; 3.30 A; s=1-110.
DR PDB; 6ORE; EM; 2.90 A; S=1-110.
DR PDB; 6ORL; EM; 3.50 A; S=1-110.
DR PDB; 6OST; EM; 4.20 A; S=1-110.
DR PDB; 6OT3; EM; 3.90 A; S=1-110.
DR PDB; 6OUO; EM; 3.70 A; S=1-110.
DR PDB; 6Q98; EM; 4.30 A; S=1-110.
DR PDB; 6Q9A; EM; 3.70 A; S=1-109.
DR PDB; 6QDW; EM; 2.83 A; s=1-110.
DR PDB; 6QUL; EM; 3.00 A; T=1-110.
DR PDB; 6S0K; EM; 3.10 A; T=1-110.
DR PDB; 6SZS; EM; 3.06 A; S=1-110.
DR PDB; 6TBV; EM; 2.70 A; L221=1-110.
DR PDB; 6TC3; EM; 2.70 A; L221=1-110.
DR PDB; 6VWL; EM; 3.10 A; Q=1-110.
DR PDB; 6VWM; EM; 3.40 A; Q=1-110.
DR PDB; 6VWN; EM; 3.40 A; Q=1-110.
DR PDB; 6WD6; EM; 3.70 A; s=1-110.
DR PDB; 6WDB; EM; 4.00 A; s=1-110.
DR PDB; 6WDC; EM; 4.20 A; s=1-110.
DR PDB; 6WDD; EM; 3.20 A; s=1-110.
DR PDB; 6WDE; EM; 3.00 A; s=1-110.
DR PDB; 6WDF; EM; 3.30 A; s=1-110.
DR PDB; 6WDG; EM; 3.30 A; s=1-110.
DR PDB; 6WDH; EM; 4.30 A; s=1-110.
DR PDB; 6WDI; EM; 4.00 A; s=1-110.
DR PDB; 6WDJ; EM; 3.70 A; s=1-110.
DR PDB; 6WDK; EM; 3.60 A; s=1-110.
DR PDB; 6WDL; EM; 3.70 A; s=1-110.
DR PDB; 6WDM; EM; 3.60 A; s=1-110.
DR PDB; 6WNT; EM; 3.10 A; s=1-110.
DR PDB; 6WNV; EM; 3.50 A; s=1-110.
DR PDB; 6WNW; EM; 3.20 A; s=1-110.
DR PDB; 6XZ7; EM; 2.10 A; S=1-110.
DR PDB; 6XZA; EM; 2.66 A; S2=1-110.
DR PDB; 6XZB; EM; 2.54 A; S2=1-110.
DR PDB; 6Y69; EM; 2.86 A; S=1-110.
DR PDB; 6YS3; EM; 2.58 A; s=1-110.
DR PDB; 6YSR; EM; 3.10 A; S=1-110.
DR PDB; 6YSS; EM; 2.60 A; S=1-110.
DR PDB; 6YST; EM; 3.20 A; S=1-110.
DR PDB; 6YSU; EM; 3.70 A; S=1-110.
DR PDB; 6ZTJ; EM; 3.40 A; BT=1-110.
DR PDB; 6ZTL; EM; 3.50 A; BT=1-110.
DR PDB; 6ZTM; EM; 3.30 A; BT=1-110.
DR PDB; 6ZTN; EM; 3.90 A; BT=1-110.
DR PDB; 6ZTO; EM; 3.00 A; BT=1-110.
DR PDB; 6ZTP; EM; 3.00 A; BT=1-110.
DR PDB; 6ZU1; EM; 3.00 A; BT=1-110.
DR PDB; 7ABZ; EM; 3.21 A; S=1-110.
DR PDB; 7AC7; EM; 3.08 A; S=2-110.
DR PDB; 7ACJ; EM; 3.20 A; S=1-110.
DR PDB; 7ACR; EM; 3.44 A; S=1-110.
DR PDB; 7B5K; EM; 2.90 A; S=1-110.
DR PDB; 7BL2; EM; 3.70 A; S=1-110.
DR PDB; 7BL3; EM; 3.50 A; S=1-110.
DR PDB; 7BL4; EM; 2.40 A; S=1-110.
DR PDB; 7BL5; EM; 3.30 A; S=1-110.
DR PDB; 7BL6; EM; 4.00 A; S=1-110.
DR PDB; 7BV8; EM; 3.14 A; T=1-110.
DR PDB; 7D6Z; EM; 3.40 A; S=1-110.
DR PDB; 7D80; EM; 4.10 A; r=1-110.
DR PDB; 7JSS; EM; 3.70 A; s=1-110.
DR PDB; 7JSW; EM; 3.80 A; s=1-110.
DR PDB; 7JSZ; EM; 3.70 A; s=1-110.
DR PDB; 7JT1; EM; 3.30 A; s=1-110.
DR PDB; 7JT2; EM; 3.50 A; s=1-110.
DR PDB; 7JT3; EM; 3.70 A; s=1-110.
DR PDB; 7K50; EM; 3.40 A; s=1-110.
DR PDB; 7K51; EM; 3.50 A; s=1-110.
DR PDB; 7K52; EM; 3.40 A; s=1-110.
DR PDB; 7K53; EM; 3.20 A; s=1-110.
DR PDB; 7K54; EM; 3.20 A; s=1-110.
DR PDB; 7K55; EM; 3.30 A; s=1-110.
DR PDB; 7LV0; EM; 3.20 A; s=1-110.
DR PDB; 7N1P; EM; 2.33 A; LV=1-110.
DR PDB; 7N2C; EM; 2.72 A; LV=1-110.
DR PDB; 7N2U; EM; 2.53 A; LV=1-110.
DR PDB; 7N2V; EM; 2.54 A; LV=1-110.
DR PDB; 7N30; EM; 2.66 A; LV=1-110.
DR PDB; 7N31; EM; 2.69 A; LV=1-110.
DR PDB; 7NBU; EM; 3.11 A; r=1-110.
DR PDB; 7NSO; EM; 2.90 A; S=1-110.
DR PDB; 7NSP; EM; 3.50 A; S=1-110.
DR PDB; 7NSQ; EM; 3.10 A; S=1-110.
DR PDB; 7NWT; EM; 2.66 A; S=1-110.
DR PDB; 7NWW; EM; 3.05 A; R=1-110.
DR PDB; 7O19; EM; 2.90 A; BS=1-110.
DR PDB; 7O1A; EM; 2.40 A; BS=1-110.
DR PDB; 7O1C; EM; 2.60 A; BS=1-110.
DR PDB; 7OIF; EM; 3.00 A; R=1-110.
DR PDB; 7OIG; EM; 3.20 A; R=1-110.
DR PDB; 7OII; EM; 3.00 A; R=1-110.
DR PDB; 7OIZ; EM; 2.90 A; r=1-110.
DR PDB; 7OJ0; EM; 3.50 A; r=1-110.
DR PDB; 7OT5; EM; 2.90 A; R=1-110.
DR PDB; 7P3K; EM; 2.90 A; r=1-110.
DR PDB; 7PJS; EM; 2.35 A; S=1-110.
DR PDB; 7PJT; EM; 6.00 A; S=1-110.
DR PDB; 7PJV; EM; 3.10 A; S=1-110.
DR PDB; 7PJW; EM; 4.00 A; S=1-110.
DR PDB; 7PJX; EM; 6.50 A; S=1-110.
DR PDB; 7PJY; EM; 3.10 A; S=1-110.
DR PDB; 7PJZ; EM; 6.00 A; S=1-110.
DR PDB; 7QG8; EM; 3.97 A; f=1-110.
DR PDB; 7QGH; EM; 4.48 A; f=1-110.
DR PDB; 7SS9; EM; 3.90 A; s=1-110.
DR PDB; 7SSD; EM; 3.30 A; s=1-110.
DR PDB; 7SSL; EM; 3.80 A; s=1-110.
DR PDB; 7SSN; EM; 3.20 A; s=1-110.
DR PDB; 7SSO; EM; 3.20 A; s=1-110.
DR PDB; 7SSW; EM; 3.80 A; s=1-110.
DR PDB; 7ST2; EM; 2.90 A; s=1-110.
DR PDB; 7ST6; EM; 3.00 A; s=1-110.
DR PDB; 7ST7; EM; 3.20 A; s=1-110.
DR PDBsum; 2J28; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3BBX; -.
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; 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; 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; 7NSO; -.
DR PDBsum; 7NSP; -.
DR PDBsum; 7NSQ; -.
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; P61175; -.
DR SMR; P61175; -.
DR BioGRID; 852125; 1.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35983N; -.
DR IntAct; P61175; 142.
DR STRING; 511145.b3315; -.
DR jPOST; P61175; -.
DR PaxDb; P61175; -.
DR PRIDE; P61175; -.
DR EnsemblBacteria; AAC76340; AAC76340; b3315.
DR EnsemblBacteria; BAE77976; BAE77976; BAE77976.
DR GeneID; 60373126; -.
DR GeneID; 67415356; -.
DR GeneID; 947813; -.
DR KEGG; ecj:JW3277; -.
DR KEGG; eco:b3315; -.
DR PATRIC; fig|1411691.4.peg.3416; -.
DR EchoBASE; EB0875; -.
DR eggNOG; COG0091; Bacteria.
DR HOGENOM; CLU_083987_3_3_6; -.
DR InParanoid; P61175; -.
DR OMA; KRIQPRA; -.
DR PhylomeDB; P61175; -.
DR BioCyc; EcoCyc:EG10882-MON; -.
DR BioCyc; MetaCyc:EG10882-MON; -.
DR EvolutionaryTrace; P61175; -.
DR PRO; PR:P61175; -.
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:0015934; C:large ribosomal subunit; IMP:CAFA.
DR GO; GO:0042788; C:polysomal ribosome; IMP:CAFA.
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:1902626; P:assembly of large subunit precursor of preribosome; IMP:EcoCyc.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0042255; P:ribosome assembly; IMP:CAFA.
DR GO; GO:0006412; P:translation; IMP:EcoCyc.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR PANTHER; PTHR13501; PTHR13501; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01044; rplV_bact; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..110
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000125153"
FT VARIANT 8
FT /note="R -> C (in strain: SK1048; decreases translational
FT rate, tRNA binding and subunit association at 44 degrees
FT Celsius; does not alter 23S rRNA or L4 interactions; not
FT erythromycin resistant)"
FT /evidence="ECO:0000269|PubMed:7729693"
FT VARIANT 82..84
FT /note="Missing (in strain: N281; confers erythromycin
FT resistance; ribosomes bind erythromycin normally and have
FT normal peptidyltransferase activity; 50S subunits assemble
FT normally, even in the presence of drug; the protein is
FT incorporated into ribosomes in vivo; abolishes translation
FT elongation arrest of SecM)"
FT /evidence="ECO:0000269|PubMed:7766155,
FT ECO:0000269|PubMed:7928988"
FT MUTAGEN 82..99
FT /note="Missing: Incorporated into ribosomes in vivo, but is
FT easily removed by a salt wash."
FT /evidence="ECO:0000269|PubMed:13130133"
FT MUTAGEN 85..95
FT /note="Missing: Incorporates into ribosomes in vivo."
FT /evidence="ECO:0000269|PubMed:13130133"
FT MUTAGEN 91
FT /note="G->A,D,S: Abolishes translation elongation arrest of
FT SecM."
FT /evidence="ECO:0000269|PubMed:11893334"
FT MUTAGEN 93
FT /note="A->S,T,V: Abolishes translation elongation arrest of
FT SecM."
FT /evidence="ECO:0000269|PubMed:11893334"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 42..60
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:6XZ7"
SQ SEQUENCE 110 AA; 12226 MW; F0E0C6982772277C CRC64;
METIAKHRHA RSSAQKVRLV ADLIRGKKVS QALDILTYTN KKAAVLVKKV LESAIANAEH
NDGADIDDLK VTKIFVDEGP SMKRIMPRAK GRADRILKRT SHITVVVSDR
