RS7_ECOLI
ID RS7_ECOLI Reviewed; 179 AA.
AC P02359; Q2M706;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=30S ribosomal protein S7;
DE AltName: Full=Small ribosomal subunit protein uS7 {ECO:0000303|PubMed:24524803};
GN Name=rpsG; OrderedLocusNames=b3341, JW3303;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-179, AND SUBUNIT.
RC STRAIN=B, and K;
RX PubMed=385062; DOI=10.1016/s0300-9084(79)80207-2;
RA Reinbolt J., Tritsch D., Wittmann-Liebold B.;
RT "The primary structure of ribosomal protein S7 from E. coli strains K and
RT B.";
RL Biochimie 61:501-522(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81 AND 148-179.
RC STRAIN=K12;
RX PubMed=6989816; DOI=10.1016/s0021-9258(19)85545-x;
RA Post L.E., Nomura M.;
RT "DNA sequences from the str operon of Escherichia coli.";
RL J. Biol. Chem. 255:4660-4666(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC STRAIN=B/R;
RX PubMed=1552908; DOI=10.1007/bf00299141;
RA Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.;
RT "Mutant sequences in the rpsL gene of Escherichia coli B/r: mechanistic
RT implications for spontaneous and ultraviolet light mutagenesis.";
RL Mol. Gen. Genet. 232:89-96(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-173.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1398129; DOI=10.1016/0378-1119(92)90014-g;
RA Johanson U., Hughes D.;
RT "Comparison of the complete sequence of the str operon in Salmonella
RT typhimurium and Escherichia coli.";
RL Gene 120:93-98(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-156.
RC STRAIN=L44;
RA Weigel C.T.O.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 111-131, CROSS-LINKING TO RRNA, AND SUBUNIT.
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 [9]
RP CROSS-LINKING TO IF3.
RC STRAIN=B;
RX PubMed=7000779; DOI=10.1016/s0021-9258(19)70495-5;
RA MacKeen L.A., Kahan L., Wahba A.J., Schwartz I.;
RT "Photochemical cross-linking of initiation factor-3 to Escherichia coli 30
RT S ribosomal subunits.";
RL J. Biol. Chem. 255:10526-10531(1980).
RN [10]
RP CROSS-LINKING TO IF3.
RC STRAIN=MRE-600;
RX PubMed=6349681; DOI=10.1021/bi00282a020;
RA Boileau G., Butler P., Hershey J.W.B., Traut R.R.;
RT "Direct cross-links between initiation factors 1, 2, and 3 and ribosomal
RT proteins promoted by 2-iminothiolane.";
RL Biochemistry 22:3162-3170(1983).
RN [11]
RP ROLE IN SUBUNIT ASSEMBLY.
RC STRAIN=K12 / D10;
RX PubMed=2461734; DOI=10.1021/bi00418a057;
RA Nowotny V., Nierhaus K.H.;
RT "Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two
RT assembly domains which are initiated by S4 and S7.";
RL Biochemistry 27:7051-7055(1988).
RN [12]
RP MECHANISM OF TRANSLATION REGULATION.
RC STRAIN=K12;
RX PubMed=7507167; DOI=10.1016/s0022-2836(05)80020-8;
RA Saito K., Mattheakis L.C., Nomura M.;
RT "Post-transcriptional regulation of the str operon in Escherichia coli.
RT Ribosomal protein S7 inhibits coupled translation of S7 but not its
RT independent translation.";
RL J. Mol. Biol. 235:111-124(1994).
RN [13]
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 [14]
RP CROSS-LINKING TO MRNA.
RC STRAIN=B, and K;
RX PubMed=10606263; DOI=10.1017/s1355838299991550;
RA Greuer B., Thiede B., Brimacombe R.;
RT "The cross-link from the upstream region of mRNA to ribosomal protein S7 is
RT located in the C-terminal peptide: experimental verification of a
RT prediction from modeling studies.";
RL RNA 5:1521-1525(1999).
RN [15]
RP MUTAGENESIS OF CONSERVED SURFACE RESIDUES, AND MUTAGENESIS OF 2-PRO--PHE-18
RP AND LYS-36.
RC STRAIN=K;
RX PubMed=10772857; DOI=10.1006/jmbi.2000.3563;
RA Fredrick K., Dunny G.M., Noller H.F.;
RT "Tagging ribosomal protein S7 allows rapid identification of mutants
RT defective in assembly and function of 30S subunits.";
RL J. Mol. Biol. 298:379-394(2000).
RN [16]
RP MUTAGENESIS OF CONSERVED RESIDUES, AND MUTAGENESIS OF MET-116.
RC STRAIN=K12;
RX PubMed=11160889; DOI=10.1093/nar/29.3.677;
RA Robert F., Brakier-Gingras L.;
RT "Ribosomal protein S7 from Escherichia coli uses the same determinants to
RT bind 16S ribosomal RNA and its messenger RNA.";
RL Nucleic Acids Res. 29:677-682(2001).
RN [17]
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 [18]
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 [19]
RP MODELING OF IF-3/30S SUBUNIT INTERACTION.
RX PubMed=11684020; DOI=10.1016/s1097-2765(01)00356-2;
RA Dallas A., Noller H.F.;
RT "Interaction of translation initiation factor 3 with the 30S ribosomal
RT subunit.";
RL Mol. Cell 8:855-864(2001).
RN [20]
RP 3D-STRUCTURE MODELING, AND SUBUNIT.
RX PubMed=12244297; DOI=10.1038/nsb841;
RA Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
RT "All-atom homology model of the Escherichia coli 30S ribosomal subunit.";
RL Nat. Struct. Biol. 9:750-755(2002).
RN [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=28077875; DOI=10.1038/nature21053;
RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA Jin H.;
RT "Structural basis of co-translational quality control by ArfA and RF2 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the head domain of the 30S
CC subunit (PubMed:2461734). Is located at the subunit interface close to
CC the decoding center, where it has been shown to contact mRNA
CC (PubMed:10606263). Has been shown to contact tRNA in both the P and E
CC sites; it probably blocks exit of the E site tRNA (PubMed:8524654).
CC {ECO:0000269|PubMed:10606263, ECO:0000269|PubMed:2461734,
CC ECO:0000269|PubMed:8524654}.
CC -!- FUNCTION: Protein S7 is also a translational repressor protein; it
CC regulates the expression of the str operon members to different degrees
CC by binding to its mRNA. {ECO:0000269|PubMed:7507167}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:385062,
CC PubMed:7556101, PubMed:10094780, PubMed:12809609, PubMed:16272117,
CC PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161,
CC PubMed:28077875). Contacts proteins S9 and S11 (By similarity). Cross-
CC links to IF3 and the P and E site tRNAs (PubMed:7000779,
CC PubMed:6349681, PubMed:8524654). {ECO:0000250|UniProtKB:P17291,
CC ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12244297,
CC ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117,
CC ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875,
CC ECO:0000269|PubMed:385062, ECO:0000269|PubMed:7556101,
CC ECO:0000269|PubMed:8524654, ECO:0000305|PubMed:6349681,
CC ECO:0000305|PubMed:7000779}.
CC -!- INTERACTION:
CC P02359; P0A707: infC; NbExp=4; IntAct=EBI-543074, EBI-546262;
CC P02359; P37765: rluB; NbExp=4; IntAct=EBI-543074, EBI-561550;
CC P02359; P0A850: tig; NbExp=4; IntAct=EBI-543074, EBI-544862;
CC -!- MASS SPECTROMETRY: Mass=19888.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: The strain K12 sequence is shown.
CC -!- MISCELLANEOUS: Has been predicted to contact the N-terminal domain of
CC IF-3 based on footprint studies; exactly how IF-3 interacts with the
CC 30S subunit is controversial (PubMed:7000779, PubMed:6349681,
CC PubMed:11684020). {ECO:0000305|PubMed:11684020,
CC ECO:0000305|PubMed:6349681, ECO:0000305|PubMed:7000779}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000305}.
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DR EMBL; U18997; AAA58138.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76366.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77950.1; -; Genomic_DNA.
DR EMBL; V00355; CAA23649.1; -; Genomic_DNA.
DR EMBL; J01689; AAA50990.1; -; Genomic_DNA.
DR EMBL; X64592; CAA45881.1; -; Genomic_DNA.
DR EMBL; X65735; CAA46644.1; -; Genomic_DNA.
DR EMBL; J01688; AAA50989.1; -; Genomic_DNA.
DR PIR; H65127; R3EC7K.
DR RefSeq; NP_417800.1; NC_000913.3.
DR RefSeq; WP_001138045.1; NZ_LN832404.1.
DR PDB; 1EG0; EM; 11.50 A; D=1-146.
DR PDB; 1ML5; EM; 14.00 A; J=1-156.
DR PDB; 2YKR; EM; 9.80 A; G=2-152.
DR PDB; 3J5S; EM; 7.50 A; I=2-152.
DR PDB; 3J9Y; EM; 3.90 A; g=1-179.
DR PDB; 3J9Z; EM; 3.60 A; SG=2-179.
DR PDB; 3JA1; EM; 3.60 A; SG=2-179.
DR PDB; 3JBU; EM; 3.64 A; G=1-156.
DR PDB; 3JBV; EM; 3.32 A; G=1-156.
DR PDB; 3JCD; EM; 3.70 A; g=1-179.
DR PDB; 3JCE; EM; 3.20 A; g=1-179.
DR PDB; 3JCJ; EM; 3.70 A; m=1-179.
DR PDB; 3JCN; EM; 4.60 A; h=1-179.
DR PDB; 4A2I; EM; 16.50 A; G=3-152.
DR PDB; 4ADV; EM; 13.50 A; G=2-179.
DR PDB; 4U1U; X-ray; 2.95 A; AG/CG=2-152.
DR PDB; 4U1V; X-ray; 3.00 A; AG/CG=2-152.
DR PDB; 4U20; X-ray; 2.90 A; AG/CG=2-152.
DR PDB; 4U24; X-ray; 2.90 A; AG/CG=2-152.
DR PDB; 4U25; X-ray; 2.90 A; AG/CG=2-152.
DR PDB; 4U26; X-ray; 2.80 A; AG/CG=2-152.
DR PDB; 4U27; X-ray; 2.80 A; AG/CG=2-152.
DR PDB; 4V47; EM; 12.30 A; BG=2-179.
DR PDB; 4V48; EM; 11.50 A; BG=2-179.
DR PDB; 4V4H; X-ray; 3.46 A; AG/CG=1-179.
DR PDB; 4V4Q; X-ray; 3.46 A; AG/CG=2-179.
DR PDB; 4V4V; EM; 15.00 A; AG=20-156.
DR PDB; 4V4W; EM; 15.00 A; AG=20-156.
DR PDB; 4V50; X-ray; 3.22 A; AG/CG=2-179.
DR PDB; 4V52; X-ray; 3.21 A; AG/CG=2-179.
DR PDB; 4V53; X-ray; 3.54 A; AG/CG=2-179.
DR PDB; 4V54; X-ray; 3.30 A; AG/CG=2-179.
DR PDB; 4V55; X-ray; 4.00 A; AG/CG=2-179.
DR PDB; 4V56; X-ray; 3.93 A; AG/CG=2-179.
DR PDB; 4V57; X-ray; 3.50 A; AG/CG=2-179.
DR PDB; 4V5B; X-ray; 3.74 A; BG/DG=2-179.
DR PDB; 4V5H; EM; 5.80 A; AG=3-152.
DR PDB; 4V5Y; X-ray; 4.45 A; AG/CG=2-179.
DR PDB; 4V64; X-ray; 3.50 A; AG/CG=2-179.
DR PDB; 4V65; EM; 9.00 A; AU=1-179.
DR PDB; 4V66; EM; 9.00 A; AU=1-179.
DR PDB; 4V69; EM; 6.70 A; AG=3-152.
DR PDB; 4V6C; X-ray; 3.19 A; AG/CG=1-179.
DR PDB; 4V6D; X-ray; 3.81 A; AG/CG=1-179.
DR PDB; 4V6E; X-ray; 3.71 A; AG/CG=1-179.
DR PDB; 4V6K; EM; 8.25 A; BK=1-179.
DR PDB; 4V6L; EM; 13.20 A; AK=1-179.
DR PDB; 4V6M; EM; 7.10 A; AG=2-179.
DR PDB; 4V6N; EM; 12.10 A; BJ=2-179.
DR PDB; 4V6O; EM; 14.70 A; AJ=2-179.
DR PDB; 4V6P; EM; 13.50 A; AJ=2-179.
DR PDB; 4V6Q; EM; 11.50 A; AJ=2-179.
DR PDB; 4V6R; EM; 11.50 A; AJ=2-179.
DR PDB; 4V6S; EM; 13.10 A; BI=2-179.
DR PDB; 4V6T; EM; 8.30 A; AG=2-152.
DR PDB; 4V6V; EM; 9.80 A; AG=2-179.
DR PDB; 4V6Y; EM; 12.00 A; AG=3-152.
DR PDB; 4V6Z; EM; 12.00 A; AG=3-152.
DR PDB; 4V70; EM; 17.00 A; AG=3-152.
DR PDB; 4V71; EM; 20.00 A; AG=3-152.
DR PDB; 4V72; EM; 13.00 A; AG=3-152.
DR PDB; 4V73; EM; 15.00 A; AG=3-152.
DR PDB; 4V74; EM; 17.00 A; AG=3-152.
DR PDB; 4V75; EM; 12.00 A; AG=3-152.
DR PDB; 4V76; EM; 17.00 A; AG=3-152.
DR PDB; 4V77; EM; 17.00 A; AG=3-152.
DR PDB; 4V78; EM; 20.00 A; AG=3-152.
DR PDB; 4V79; EM; 15.00 A; AG=3-152.
DR PDB; 4V7A; EM; 9.00 A; AG=3-152.
DR PDB; 4V7B; EM; 6.80 A; AG=1-179.
DR PDB; 4V7C; EM; 7.60 A; AG=2-179.
DR PDB; 4V7D; EM; 7.60 A; BG=2-179.
DR PDB; 4V7I; EM; 9.60 A; BG=1-179.
DR PDB; 4V7S; X-ray; 3.25 A; AG=2-152, CG=3-152.
DR PDB; 4V7T; X-ray; 3.19 A; AG=2-152, CG=3-152.
DR PDB; 4V7U; X-ray; 3.10 A; AG/CG=2-152.
DR PDB; 4V7V; X-ray; 3.29 A; AG=2-152, CG=3-152.
DR PDB; 4V85; X-ray; 3.20 A; AG=1-156.
DR PDB; 4V89; X-ray; 3.70 A; AG=1-179.
DR PDB; 4V9C; X-ray; 3.30 A; AG/CG=1-179.
DR PDB; 4V9D; X-ray; 3.00 A; AG/BG=2-152.
DR PDB; 4V9O; X-ray; 2.90 A; BG/DG/FG/HG=1-179.
DR PDB; 4V9P; X-ray; 2.90 A; BG/DG/FG/HG=1-179.
DR PDB; 4WF1; X-ray; 3.09 A; AG/CG=2-152.
DR PDB; 4WOI; X-ray; 3.00 A; AG/DG=1-179.
DR PDB; 4WWW; X-ray; 3.10 A; QG/XG=2-152.
DR PDB; 4YBB; X-ray; 2.10 A; AG/BG=2-152.
DR PDB; 5AFI; EM; 2.90 A; g=1-179.
DR PDB; 5H5U; EM; 3.00 A; n=2-179.
DR PDB; 5IQR; EM; 3.00 A; l=1-179.
DR PDB; 5IT8; X-ray; 3.12 A; AG/BG=2-152.
DR PDB; 5J5B; X-ray; 2.80 A; AG/BG=2-152.
DR PDB; 5J7L; X-ray; 3.00 A; AG/BG=2-152.
DR PDB; 5J88; X-ray; 3.32 A; AG/BG=2-152.
DR PDB; 5J8A; X-ray; 3.10 A; AG/BG=2-152.
DR PDB; 5J91; X-ray; 2.96 A; AG/BG=2-152.
DR PDB; 5JC9; X-ray; 3.03 A; AG/BG=2-152.
DR PDB; 5JTE; EM; 3.60 A; AG=1-179.
DR PDB; 5JU8; EM; 3.60 A; AG=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; 12=1-179.
DR PDB; 5KPV; EM; 4.10 A; 11=1-179.
DR PDB; 5KPW; EM; 3.90 A; 11=1-179.
DR PDB; 5KPX; EM; 3.90 A; 11=1-179.
DR PDB; 5L3P; EM; 3.70 A; g=1-179.
DR PDB; 5LZA; EM; 3.60 A; g=2-152.
DR PDB; 5LZB; EM; 5.30 A; g=2-152.
DR PDB; 5LZC; EM; 4.80 A; g=2-152.
DR PDB; 5LZD; EM; 3.40 A; g=2-152.
DR PDB; 5LZE; EM; 3.50 A; g=2-152.
DR PDB; 5LZF; EM; 4.60 A; g=2-152.
DR PDB; 5MDV; EM; 2.97 A; l=1-179.
DR PDB; 5MDW; EM; 3.06 A; l=1-179.
DR PDB; 5MDY; EM; 3.35 A; l=1-179.
DR PDB; 5MDZ; EM; 3.10 A; l=1-179.
DR PDB; 5ME0; EM; 13.50 A; G=1-156.
DR PDB; 5ME1; EM; 13.50 A; G=1-156.
DR PDB; 5MGP; EM; 3.10 A; g=2-152.
DR PDB; 5MY1; EM; 7.60 A; G=2-179.
DR PDB; 5NO2; EM; 5.16 A; G=2-131.
DR PDB; 5NO3; EM; 5.16 A; G=2-131.
DR PDB; 5NO4; EM; 5.16 A; G=2-131.
DR PDB; 5NP6; EM; 3.60 A; J=2-152.
DR PDB; 5NWY; EM; 2.93 A; 6=1-156.
DR PDB; 5O2R; EM; 3.40 A; g=2-152.
DR PDB; 5U4I; EM; 3.50 A; g=1-179.
DR PDB; 5U9F; EM; 3.20 A; G=1-156.
DR PDB; 5U9G; EM; 3.20 A; G=1-156.
DR PDB; 5UYK; EM; 3.90 A; G=2-152.
DR PDB; 5UYL; EM; 3.60 A; G=2-152.
DR PDB; 5UYM; EM; 3.20 A; G=2-152.
DR PDB; 5UYN; EM; 4.00 A; G=2-152.
DR PDB; 5UYP; EM; 3.90 A; G=2-152.
DR PDB; 5UYQ; EM; 3.80 A; G=2-152.
DR PDB; 5UZ4; EM; 5.80 A; G=1-179.
DR PDB; 5WDT; EM; 3.00 A; g=2-152.
DR PDB; 5WE4; EM; 3.10 A; g=2-152.
DR PDB; 5WE6; EM; 3.40 A; g=2-152.
DR PDB; 5WFK; EM; 3.40 A; g=2-152.
DR PDB; 6BU8; EM; 3.50 A; G=2-152.
DR PDB; 6BY1; X-ray; 3.94 A; AG/BG=1-179.
DR PDB; 6C4I; EM; 3.24 A; g=1-179.
DR PDB; 6ENF; EM; 3.20 A; g=2-152.
DR PDB; 6ENJ; EM; 3.70 A; g=2-152.
DR PDB; 6ENU; EM; 3.10 A; g=2-152.
DR PDB; 6GWT; EM; 3.80 A; g=2-152.
DR PDB; 6GXM; EM; 3.80 A; g=2-152.
DR PDB; 6GXN; EM; 3.90 A; g=2-152.
DR PDB; 6GXO; EM; 3.90 A; g=2-152.
DR PDB; 6GXP; EM; 4.40 A; g=2-152.
DR PDB; 6H4N; EM; 3.00 A; g=2-162.
DR PDB; 6H58; EM; 7.90 A; g/gg=2-162.
DR PDB; 6HRM; EM; 2.96 A; l=2-152.
DR PDB; 6I7V; X-ray; 2.90 A; AG/BG=2-152.
DR PDB; 6O9J; EM; 3.90 A; g=3-152.
DR PDB; 6O9K; EM; 4.00 A; g=2-152.
DR PDB; 6OFX; EM; 3.30 A; L=2-152.
DR PDB; 6OG7; EM; 3.30 A; L=2-152.
DR PDB; 6ORE; EM; 2.90 A; l=2-152.
DR PDB; 6ORL; EM; 3.50 A; l=2-152.
DR PDB; 6OST; EM; 4.20 A; l=2-152.
DR PDB; 6OT3; EM; 3.90 A; l=2-152.
DR PDB; 6OUO; EM; 3.70 A; l=2-152.
DR PDB; 6Q97; EM; 3.90 A; l=2-152.
DR PDB; 6Q98; EM; 4.30 A; l=1-179.
DR PDB; 6Q9A; EM; 3.70 A; l=2-153.
DR PDB; 6SZS; EM; 3.06 A; g=1-179.
DR PDB; 6TBV; EM; 2.70 A; S071=1-179.
DR PDB; 6TC3; EM; 2.70 A; S071=1-179.
DR PDB; 6VWL; EM; 3.10 A; f=1-179.
DR PDB; 6VWM; EM; 3.40 A; f=1-179.
DR PDB; 6VWN; EM; 3.40 A; f=1-179.
DR PDB; 6W7M; EM; 3.80 A; G=1-179.
DR PDB; 6WD6; EM; 3.70 A; L=2-152.
DR PDB; 6WDB; EM; 4.00 A; L=2-152.
DR PDB; 6WDC; EM; 4.20 A; L=2-152.
DR PDB; 6WDD; EM; 3.20 A; L=2-152.
DR PDB; 6WDE; EM; 3.00 A; L=2-152.
DR PDB; 6WDF; EM; 3.30 A; L=2-152.
DR PDB; 6WDG; EM; 3.30 A; L=2-152.
DR PDB; 6WDH; EM; 4.30 A; L=2-152.
DR PDB; 6WDI; EM; 4.00 A; L=2-152.
DR PDB; 6WDJ; EM; 3.70 A; L=2-152.
DR PDB; 6WDK; EM; 3.60 A; L=2-152.
DR PDB; 6WDL; EM; 3.70 A; L=2-152.
DR PDB; 6WDM; EM; 3.60 A; L=2-152.
DR PDB; 6WNV; EM; 3.50 A; L=2-152.
DR PDB; 6WNW; EM; 3.20 A; L=2-152.
DR PDB; 6XE0; EM; 6.80 A; F=2-152.
DR PDB; 6XZA; EM; 2.66 A; G1=2-152.
DR PDB; 6XZB; EM; 2.54 A; G1=2-152.
DR PDB; 6Y69; EM; 2.86 A; g=2-156.
DR PDB; 6ZTJ; EM; 3.40 A; AG=1-156.
DR PDB; 6ZTL; EM; 3.50 A; AG=1-156.
DR PDB; 6ZTM; EM; 3.30 A; AG=1-156.
DR PDB; 6ZTN; EM; 3.90 A; AG=1-156.
DR PDB; 6ZTO; EM; 3.00 A; AG=1-156.
DR PDB; 6ZTP; EM; 3.00 A; AG=1-156.
DR PDB; 6ZU1; EM; 3.00 A; AG=1-156.
DR PDB; 7ABZ; EM; 3.21 A; l=2-152.
DR PDB; 7AC7; EM; 3.08 A; l=2-152.
DR PDB; 7ACJ; EM; 3.20 A; l=2-152.
DR PDB; 7ACR; EM; 3.44 A; l=2-152.
DR PDB; 7AF3; EM; 2.82 A; G=1-179.
DR PDB; 7AF5; EM; 2.96 A; G=1-179.
DR PDB; 7AF8; EM; 2.75 A; G=1-179.
DR PDB; 7AFA; EM; 2.95 A; G=1-179.
DR PDB; 7AFD; EM; 3.44 A; G=1-179.
DR PDB; 7AFH; EM; 3.59 A; G=1-179.
DR PDB; 7AFK; EM; 4.90 A; G=1-179.
DR PDB; 7AFN; EM; 3.86 A; G=1-179.
DR PDB; 7B5K; EM; 2.90 A; g=2-152.
DR PDB; 7BOE; EM; 2.90 A; G=1-179.
DR PDB; 7BOH; EM; 2.82 A; G=1-179.
DR PDB; 7D6Z; EM; 3.40 A; n=1-179.
DR PDB; 7D80; EM; 4.10 A; H=1-179.
DR PDB; 7JSS; EM; 3.70 A; L=2-152.
DR PDB; 7JSW; EM; 3.80 A; L=2-152.
DR PDB; 7JSZ; EM; 3.70 A; L=2-152.
DR PDB; 7JT1; EM; 3.30 A; L=2-152.
DR PDB; 7JT2; EM; 3.50 A; L=2-152.
DR PDB; 7JT3; EM; 3.70 A; L=2-152.
DR PDB; 7K50; EM; 3.40 A; L=2-152.
DR PDB; 7K51; EM; 3.50 A; L=2-152.
DR PDB; 7K52; EM; 3.40 A; L=2-152.
DR PDB; 7K53; EM; 3.20 A; L=2-152.
DR PDB; 7K54; EM; 3.20 A; L=2-152.
DR PDB; 7K55; EM; 3.30 A; L=2-152.
DR PDB; 7LV0; EM; 3.20 A; L=2-152.
DR PDB; 7N1P; EM; 2.33 A; SG=1-179.
DR PDB; 7N2C; EM; 2.72 A; SG=1-179.
DR PDB; 7N2U; EM; 2.53 A; SG=1-179.
DR PDB; 7N2V; EM; 2.54 A; SG=1-179.
DR PDB; 7N30; EM; 2.66 A; SG=1-179.
DR PDB; 7N31; EM; 2.69 A; SG=1-179.
DR PDB; 7NAR; EM; 3.00 A; G=1-179.
DR PDB; 7NAT; EM; 3.59 A; G=1-179.
DR PDB; 7NAU; EM; 3.78 A; G=1-179.
DR PDB; 7NAV; EM; 4.80 A; G=1-179.
DR PDB; 7NSO; EM; 2.90 A; g=2-152.
DR PDB; 7NSP; EM; 3.50 A; g=2-152.
DR PDB; 7NSQ; EM; 3.10 A; g=2-152.
DR PDB; 7NWT; EM; 2.66 A; l=1-179.
DR PDB; 7NWW; EM; 3.05 A; k=2-152.
DR PDB; 7O19; EM; 2.90 A; AG=1-179.
DR PDB; 7O1A; EM; 2.40 A; AG=1-179.
DR PDB; 7O1C; EM; 2.60 A; AG=1-179.
DR PDB; 7OE0; EM; 2.69 A; G=2-179.
DR PDB; 7OE1; EM; 3.05 A; G=2-179.
DR PDB; 7OIF; EM; 3.00 A; k=2-152.
DR PDB; 7OIG; EM; 3.20 A; k=2-152.
DR PDB; 7OII; EM; 3.00 A; k=2-152.
DR PDB; 7OIZ; EM; 2.90 A; G=1-179.
DR PDB; 7OJ0; EM; 3.50 A; G=1-179.
DR PDB; 7OT5; EM; 2.90 A; k=2-152.
DR PDB; 7P3K; EM; 2.90 A; G=1-179.
DR PDB; 7PJS; EM; 2.35 A; g=1-179.
DR PDB; 7PJT; EM; 6.00 A; g=1-179.
DR PDB; 7PJV; EM; 3.10 A; g=1-179.
DR PDB; 7PJW; EM; 4.00 A; g=1-179.
DR PDB; 7PJX; EM; 6.50 A; g=1-179.
DR PDB; 7PJY; EM; 3.10 A; g=1-179.
DR PDB; 7PJZ; EM; 6.00 A; g=1-179.
DR PDB; 7QG8; EM; 3.97 A; 6=1-156.
DR PDB; 7QGH; EM; 4.48 A; 6=1-152.
DR PDB; 7S1G; EM; 2.48 A; n=1-179.
DR PDB; 7S1H; EM; 2.35 A; n=1-179.
DR PDB; 7S1I; EM; 2.48 A; n=1-179.
DR PDB; 7S1J; EM; 2.47 A; n=1-179.
DR PDB; 7S1K; EM; 2.42 A; n=1-179.
DR PDB; 7SS9; EM; 3.90 A; L=2-152.
DR PDB; 7SSD; EM; 3.30 A; L=2-152.
DR PDB; 7SSL; EM; 3.80 A; L=2-152.
DR PDB; 7SSN; EM; 3.20 A; L=2-152.
DR PDB; 7SSO; EM; 3.20 A; L=2-152.
DR PDB; 7SSW; EM; 3.80 A; L=2-152.
DR PDB; 7ST2; EM; 2.90 A; L=2-152.
DR PDB; 7ST6; EM; 3.00 A; L=2-152.
DR PDB; 7ST7; EM; 3.20 A; L=2-152.
DR PDBsum; 1EG0; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 2YKR; -.
DR PDBsum; 3J5S; -.
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; 4A2I; -.
DR PDBsum; 4ADV; -.
DR PDBsum; 4U1U; -.
DR PDBsum; 4U1V; -.
DR PDBsum; 4U20; -.
DR PDBsum; 4U24; -.
DR PDBsum; 4U25; -.
DR PDBsum; 4U26; -.
DR PDBsum; 4U27; -.
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; 5AFI; -.
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; 5ME0; -.
DR PDBsum; 5ME1; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5MY1; -.
DR PDBsum; 5NO2; -.
DR PDBsum; 5NO3; -.
DR PDBsum; 5NO4; -.
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; 5UZ4; -.
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; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
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; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6W7M; -.
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; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6XE0; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 6Y69; -.
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; 7AF3; -.
DR PDBsum; 7AF5; -.
DR PDBsum; 7AF8; -.
DR PDBsum; 7AFA; -.
DR PDBsum; 7AFD; -.
DR PDBsum; 7AFH; -.
DR PDBsum; 7AFK; -.
DR PDBsum; 7AFN; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BOE; -.
DR PDBsum; 7BOH; -.
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; 7NAR; -.
DR PDBsum; 7NAT; -.
DR PDBsum; 7NAU; -.
DR PDBsum; 7NAV; -.
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; 7OE0; -.
DR PDBsum; 7OE1; -.
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; 7S1G; -.
DR PDBsum; 7S1H; -.
DR PDBsum; 7S1I; -.
DR PDBsum; 7S1J; -.
DR PDBsum; 7S1K; -.
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; P02359; -.
DR SMR; P02359; -.
DR BioGRID; 852157; 1.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR DIP; DIP-10783N; -.
DR IntAct; P02359; 167.
DR STRING; 511145.b3341; -.
DR DrugBank; DB09093; Chlortetracycline.
DR DrugBank; DB13092; Meclocycline.
DR DrugBank; DB12455; Omadacycline.
DR DrugBank; DB00759; Tetracycline.
DR MoonProt; P02359; -.
DR jPOST; P02359; -.
DR PaxDb; P02359; -.
DR PRIDE; P02359; -.
DR EnsemblBacteria; AAC76366; AAC76366; b3341.
DR EnsemblBacteria; BAE77950; BAE77950; BAE77950.
DR GeneID; 947846; -.
DR KEGG; ecj:JW3303; -.
DR KEGG; eco:b3341; -.
DR PATRIC; fig|1411691.4.peg.3390; -.
DR EchoBASE; EB0899; -.
DR eggNOG; COG0049; Bacteria.
DR HOGENOM; CLU_072226_1_1_6; -.
DR InParanoid; P02359; -.
DR OMA; NVMPHVE; -.
DR PhylomeDB; P02359; -.
DR BioCyc; EcoCyc:EG10906-MON; -.
DR BioCyc; MetaCyc:EG10906-MON; -.
DR EvolutionaryTrace; P02359; -.
DR PRO; PR:P02359; -.
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:0022627; C:cytosolic small ribosomal subunit; IDA:CAFA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:CAFA.
DR GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0017148; P:negative regulation of translation; IDA:CAFA.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 1.10.455.10; -; 1.
DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005717; Ribosomal_S7_bac/org-type.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01029; rpsG_bact; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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:385062"
FT CHAIN 2..179
FT /note="30S ribosomal protein S7"
FT /id="PRO_0000124259"
FT VARIANT 157..179
FT /note="Missing (in strain: B and L44)"
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 2..18
FT /note="Missing: Defective in ribosome assembly; accumulates
FT to abnormally high levels on polysomes; significantly
FT decreases affinity for its own mRNA."
FT /evidence="ECO:0000269|PubMed:10772857"
FT MUTAGEN 36
FT /note="K->A,E: Defective in ribosome assembly."
FT /evidence="ECO:0000269|PubMed:10772857"
FT MUTAGEN 116
FT /note="M->G: Significantly decreases affinity for its own
FT mRNA."
FT /evidence="ECO:0000269|PubMed:11160889"
FT CONFLICT 92
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7OE1"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:7AF8"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:7AF8"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:7AF8"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:7AF8"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:7OE1"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:7AF8"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7AF8"
SQ SEQUENCE 179 AA; 20019 MW; 8627DB380C4A9C0D CRC64;
MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL AQRSGKSELE
AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA MRWIVEAARK RGDKSMALRL
ANELSDAAEN KGTAVKKRED VHRMAEANKA FAHYRWLSLR SFSHQAGASS KQPALGYLN
