RS4_ECOLI
ID RS4_ECOLI Reviewed; 206 AA.
AC P0A7V8; P02354; Q2M6W1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=30S ribosomal protein S4;
DE AltName: Full=Small ribosomal subunit protein uS4 {ECO:0000303|PubMed:24524803};
GN Name=rpsD; Synonyms=ramA; OrderedLocusNames=b3296, JW3258;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989779; DOI=10.1093/nar/13.11.3891;
RA Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H.,
RA Zengel J.M., Lindahl L.;
RT "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia
RT coli.";
RL Nucleic Acids Res. 13:3891-3903(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-206, AND SUBUNIT.
RC STRAIN=AB774;
RX PubMed=4587210; DOI=10.1016/0014-5793(73)80383-7;
RA Reinbolt J., Schiltz E.;
RT "The primary structure of ribosomal protein S4 from Escherichia coli.";
RL FEBS Lett. 36:250-252(1973).
RN [5]
RP PROTEIN SEQUENCE OF 2-206, AND SUBUNIT.
RC STRAIN=K;
RX PubMed=1100394; DOI=10.1111/j.1432-1033.1975.tb02253.x;
RA Schiltz E., Reinbolt J.;
RT "Determination of the complete amino-acid sequence of protein S4 from
RT Escherichia coli ribosomes.";
RL Eur. J. Biochem. 56:467-481(1975).
RN [6]
RP PROTEIN SEQUENCE OF 78-91, 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 PROTEIN SEQUENCE OF 84-97 AND 129-146, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Barblan J., Quadroni M.;
RL Submitted (JAN-2004) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-206.
RX PubMed=387752; DOI=10.1016/s0021-9258(19)86562-6;
RA Post L.E., Nomura M.;
RT "Nucleotide sequence of the intercistronic region preceding the gene for
RT RNA polymerase subunit alpha in Escherichia coli.";
RL J. Biol. Chem. 254:10604-10606(1979).
RN [9]
RP MECHANISM OF TRANSLATION REGULATION.
RX PubMed=3309351; DOI=10.1016/0022-2836(87)90694-2;
RA Thomas M.S., Bedwell D.M., Nomura M.;
RT "Regulation of alpha operon gene expression in Escherichia coli. A novel
RT form of translational coupling.";
RL J. Mol. Biol. 196:333-345(1987).
RN [10]
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 [11]
RP EFFECT OF MUTATIONS ON RRNA FOLDING.
RC STRAIN=UD1A1;
RX PubMed=2477554; DOI=10.1016/0022-2836(89)90509-3;
RA Allen P.N., Noller H.F.;
RT "Mutations in ribosomal proteins S4 and S12 influence the higher order
RT structure of 16 S ribosomal RNA.";
RL J. Mol. Biol. 208:457-468(1989).
RN [12]
RP BINDING TO MRNA.
RX PubMed=7559430; DOI=10.1074/jbc.270.39.22939;
RA Baker A.M., Draper D.E.;
RT "Messenger RNA recognition by fragments of ribosomal protein S4.";
RL J. Biol. Chem. 270:22939-22945(1995).
RN [13]
RP CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
RX PubMed=9716382; DOI=10.1046/j.1432-1327.1998.2550409.x;
RA Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.;
RT "Flexibility of the nascent polypeptide chain within the ribosome
RT -- contacts from the peptide N-terminus to a specific region of the 30S
RT subunit.";
RL Eur. J. Biochem. 255:409-413(1998).
RN [14]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [15]
RP VARIANTS THAT AFFECTS TERMINATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11018284; DOI=10.1016/s0300-9084(00)01160-3;
RA Dahlgren A., Ryden-Aulin M.;
RT "A novel mutation in ribosomal protein S4 that affects the function of a
RT mutated RF1.";
RL Biochimie 82:683-691(2000).
RN [16]
RP RHO-DEPENDENT RIBOSOMAL RNA ANTITERMINATION FUNCTION.
RX PubMed=11447122; DOI=10.1093/emboj/20.14.3811;
RA Torres M., Condon C., Balada J.-M., Squires C., Squires C.L.;
RT "Ribosomal protein S4 is a transcription factor with properties remarkably
RT similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA
RT antitermination.";
RL EMBO J. 20:3811-3820(2001).
RN [17]
RP ROLE IN MRNA HELICASE ACTIVITY, AND MUTAGENESIS.
RC STRAIN=MRE-600;
RX PubMed=15652481; DOI=10.1016/j.cell.2004.11.042;
RA Takyar S., Hickerson R.P., Noller H.F.;
RT "mRNA helicase activity of the ribosome.";
RL Cell 120:49-58(2005).
RN [18]
RP MASS SPECTROMETRY.
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 [19]
RP REVIEW ON TRANSLATIONAL ACCURACY.
RA Kurland C.G., Hughes D., Ehrenberg M.;
RT "Limitations of translational accuracy.";
RL (In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
RL Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
RL Umbarger H.E. (eds.);
RL Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.),
RL pp.979-1004, American Society for Microbiology Press, Washington D.C.
RL (1996).
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] {ECO:0007744|PDB:4V47}
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] {ECO:0007744|PDB:4V4Q}
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] {ECO:0007744|PDB:5H5U}
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] {ECO:0007744|PDB:5MGP}
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] {ECO:0007744|PDB:5MDV, ECO:0007744|PDB:5MDW, ECO:0007744|PDB:5MDY, ECO:0007744|PDB:5MDZ}
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] {ECO:0007744|PDB:5U4I, ECO:0007744|PDB:5U4J}
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).
RN [27] {ECO:0007744|PDB:6TQO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA
RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEX, FUNCTION, AND SUBUNIT.
RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010;
RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C.,
RA Said N., Wahl M.C.;
RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine
RT Required for Ribosome Biosynthesis.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: One of two assembly initiator proteins for the 30S subunit,
CC it binds directly to 16S rRNA where it nucleates assembly of the body
CC of the 30S subunit. {ECO:0000269|PubMed:2461734}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy; many suppressors of streptomycin-dependent mutants of protein
CC S12 are found in this protein, some but not all of which decrease
CC translational accuracy (ram, ribosomal ambiguity mutations).
CC -!- FUNCTION: Plays a role in mRNA unwinding by the ribosome, possibly by
CC forming part of a processivity clamp. {ECO:0000269|PubMed:15652481}.
CC -!- FUNCTION: Protein S4 is also a translational repressor protein, it
CC controls the translation of the alpha-operon (which codes for S13, S11,
CC S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.
CC {ECO:0000269|PubMed:3309351}.
CC -!- FUNCTION: Also functions as a rho-dependent antiterminator of rRNA
CC transcription, increasing the synthesis of rRNA under conditions of
CC excess protein, allowing a more rapid return to homeostasis. Binds
CC directly to RNA polymerase. {ECO:0000269|PubMed:11447122}.
CC -!- FUNCTION: Part of the processive rRNA transcription and antitermination
CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the
CC RNA exit tunnel of RNA polymerase (RNAP). It supports rapid
CC transcription and antitermination of rRNA operons, cotranscriptional
CC rRNA folding, and annealing of distal rRNA regions to allow correct
CC ribosome biogenesis. This subunit may play a particular role in long-
CC distance rRNA annealing needed for pre-rRNA processing.
CC {ECO:0000269|PubMed:32871103}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:4587210,
CC PubMed:1100394, PubMed:7556101, PubMed:12809609, PubMed:16272117,
CC PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160,
CC PubMed:27906161, PubMed:28077875). Contacts protein S5. With proteins
CC S3 and S5 encircles the mRNA as it enters the ribosome, which may play
CC a role in mRNA helicase processivity (PubMed:15652481). Some nascent
CC polypeptide chains are able to cross-link to this protein in situ
CC (PubMed:9716382). The rRNA transcription and antitermination complex
CC (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB,
CC ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than
CC other subunits (PubMed:32871103). {ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:1100394, ECO:0000269|PubMed:12244297,
CC ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:15652481,
CC ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:28077875, ECO:0000269|PubMed:32871103,
CC ECO:0000269|PubMed:4587210, ECO:0000269|PubMed:7556101,
CC ECO:0000269|PubMed:9716382}.
CC -!- INTERACTION:
CC P0A7V8; P0A9J0: rng; NbExp=2; IntAct=EBI-543939, EBI-545964;
CC -!- MASS SPECTROMETRY: Mass=23339.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; X02543; CAA26394.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58094.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76321.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77995.1; -; Genomic_DNA.
DR EMBL; V00353; CAA23645.1; -; Genomic_DNA.
DR EMBL; J01685; AAA24576.1; -; Genomic_DNA.
DR PIR; C23807; R3EC4.
DR RefSeq; NP_417755.1; NC_000913.3.
DR RefSeq; WP_000135224.1; NZ_STEB01000038.1.
DR PDB; 1EG0; EM; 11.50 A; A=43-200.
DR PDB; 2YKR; EM; 9.80 A; D=2-206.
DR PDB; 3J9Y; EM; 3.90 A; d=1-206.
DR PDB; 3J9Z; EM; 3.60 A; SD=2-206.
DR PDB; 3JA1; EM; 3.60 A; SD=2-206.
DR PDB; 3JBU; EM; 3.64 A; D=1-206.
DR PDB; 3JBV; EM; 3.32 A; D=1-206.
DR PDB; 3JCD; EM; 3.70 A; d=1-206.
DR PDB; 3JCE; EM; 3.20 A; d=1-206.
DR PDB; 3JCJ; EM; 3.70 A; l=1-206.
DR PDB; 3JCN; EM; 4.60 A; g=1-206.
DR PDB; 4A2I; EM; 16.50 A; D=2-206.
DR PDB; 4ADV; EM; 13.50 A; D=2-206.
DR PDB; 4U1U; X-ray; 2.95 A; AD/CD=2-206.
DR PDB; 4U1V; X-ray; 3.00 A; AD/CD=2-206.
DR PDB; 4U20; X-ray; 2.90 A; AD/CD=2-206.
DR PDB; 4U24; X-ray; 2.90 A; AD/CD=2-206.
DR PDB; 4U25; X-ray; 2.90 A; AD/CD=2-206.
DR PDB; 4U26; X-ray; 2.80 A; AD/CD=2-206.
DR PDB; 4U27; X-ray; 2.80 A; AD/CD=2-206.
DR PDB; 4V47; EM; 12.30 A; BD=2-206.
DR PDB; 4V48; EM; 11.50 A; BD=2-206.
DR PDB; 4V4H; X-ray; 3.46 A; AD/CD=1-206.
DR PDB; 4V4Q; X-ray; 3.46 A; AD/CD=2-206.
DR PDB; 4V4V; EM; 15.00 A; AD=3-206.
DR PDB; 4V4W; EM; 15.00 A; AD=3-206.
DR PDB; 4V50; X-ray; 3.22 A; AD/CD=2-206.
DR PDB; 4V52; X-ray; 3.21 A; AD/CD=2-206.
DR PDB; 4V53; X-ray; 3.54 A; AD/CD=2-206.
DR PDB; 4V54; X-ray; 3.30 A; AD/CD=2-206.
DR PDB; 4V55; X-ray; 4.00 A; AD/CD=2-206.
DR PDB; 4V56; X-ray; 3.93 A; AD/CD=2-206.
DR PDB; 4V57; X-ray; 3.50 A; AD/CD=2-206.
DR PDB; 4V5B; X-ray; 3.74 A; BD/DD=2-206.
DR PDB; 4V5H; EM; 5.80 A; AD=2-206.
DR PDB; 4V5Y; X-ray; 4.45 A; AD/CD=2-206.
DR PDB; 4V64; X-ray; 3.50 A; AD/CD=2-206.
DR PDB; 4V65; EM; 9.00 A; AR=1-206.
DR PDB; 4V66; EM; 9.00 A; AR=1-206.
DR PDB; 4V69; EM; 6.70 A; AD=2-206.
DR PDB; 4V6C; X-ray; 3.19 A; AD/CD=1-206.
DR PDB; 4V6D; X-ray; 3.81 A; AD/CD=1-206.
DR PDB; 4V6E; X-ray; 3.71 A; AD/CD=1-206.
DR PDB; 4V6K; EM; 8.25 A; BH=1-206.
DR PDB; 4V6L; EM; 13.20 A; AH=1-206.
DR PDB; 4V6M; EM; 7.10 A; AD=2-206.
DR PDB; 4V6N; EM; 12.10 A; BG=2-206.
DR PDB; 4V6O; EM; 14.70 A; AG=2-206.
DR PDB; 4V6P; EM; 13.50 A; AG=2-206.
DR PDB; 4V6Q; EM; 11.50 A; AG=2-206.
DR PDB; 4V6R; EM; 11.50 A; AG=2-206.
DR PDB; 4V6S; EM; 13.10 A; BF=2-206.
DR PDB; 4V6T; EM; 8.30 A; AD=2-206.
DR PDB; 4V6V; EM; 9.80 A; AD=2-206.
DR PDB; 4V6Y; EM; 12.00 A; AD=1-206.
DR PDB; 4V6Z; EM; 12.00 A; AD=1-206.
DR PDB; 4V70; EM; 17.00 A; AD=1-206.
DR PDB; 4V71; EM; 20.00 A; AD=1-206.
DR PDB; 4V72; EM; 13.00 A; AD=1-206.
DR PDB; 4V73; EM; 15.00 A; AD=1-206.
DR PDB; 4V74; EM; 17.00 A; AD=1-206.
DR PDB; 4V75; EM; 12.00 A; AD=1-206.
DR PDB; 4V76; EM; 17.00 A; AD=1-206.
DR PDB; 4V77; EM; 17.00 A; AD=1-206.
DR PDB; 4V78; EM; 20.00 A; AD=1-206.
DR PDB; 4V79; EM; 15.00 A; AD=1-206.
DR PDB; 4V7A; EM; 9.00 A; AD=1-206.
DR PDB; 4V7B; EM; 6.80 A; AD=1-206.
DR PDB; 4V7C; EM; 7.60 A; AD=2-206.
DR PDB; 4V7D; EM; 7.60 A; BD=2-206.
DR PDB; 4V7I; EM; 9.60 A; BD=1-206.
DR PDB; 4V7S; X-ray; 3.25 A; AD/CD=2-206.
DR PDB; 4V7T; X-ray; 3.19 A; AD/CD=2-206.
DR PDB; 4V7U; X-ray; 3.10 A; AD/CD=2-206.
DR PDB; 4V7V; X-ray; 3.29 A; AD/CD=2-206.
DR PDB; 4V85; X-ray; 3.20 A; AD=1-206.
DR PDB; 4V89; X-ray; 3.70 A; AD=1-206.
DR PDB; 4V9C; X-ray; 3.30 A; AD/CD=1-206.
DR PDB; 4V9D; X-ray; 3.00 A; AD/BD=2-206.
DR PDB; 4V9O; X-ray; 2.90 A; BD/DD/FD/HD=1-206.
DR PDB; 4V9P; X-ray; 2.90 A; BD/DD/FD/HD=1-206.
DR PDB; 4WF1; X-ray; 3.09 A; AD/CD=2-206.
DR PDB; 4WOI; X-ray; 3.00 A; AD/DD=1-206.
DR PDB; 4WWW; X-ray; 3.10 A; QD/XD=2-206.
DR PDB; 4YBB; X-ray; 2.10 A; AD/BD=2-206.
DR PDB; 5AFI; EM; 2.90 A; d=1-206.
DR PDB; 5H5U; EM; 3.00 A; k=2-206.
DR PDB; 5IQR; EM; 3.00 A; i=1-206.
DR PDB; 5IT8; X-ray; 3.12 A; AD/BD=2-206.
DR PDB; 5J5B; X-ray; 2.80 A; AD/BD=2-206.
DR PDB; 5J7L; X-ray; 3.00 A; AD/BD=2-206.
DR PDB; 5J88; X-ray; 3.32 A; AD/BD=2-206.
DR PDB; 5J8A; X-ray; 3.10 A; AD/BD=2-206.
DR PDB; 5J91; X-ray; 2.96 A; AD/BD=2-206.
DR PDB; 5JC9; X-ray; 3.03 A; AD/BD=2-206.
DR PDB; 5JTE; EM; 3.60 A; AD=1-206.
DR PDB; 5JU8; EM; 3.60 A; AD=1-206.
DR PDB; 5KCR; EM; 3.60 A; 1d=1-206.
DR PDB; 5KCS; EM; 3.90 A; 1d=1-206.
DR PDB; 5KPS; EM; 3.90 A; 9=1-206.
DR PDB; 5KPV; EM; 4.10 A; 8=1-206.
DR PDB; 5KPW; EM; 3.90 A; 8=1-206.
DR PDB; 5KPX; EM; 3.90 A; 8=1-206.
DR PDB; 5L3P; EM; 3.70 A; d=1-206.
DR PDB; 5LZA; EM; 3.60 A; d=2-206.
DR PDB; 5LZB; EM; 5.30 A; d=2-206.
DR PDB; 5LZC; EM; 4.80 A; d=2-206.
DR PDB; 5LZD; EM; 3.40 A; d=2-206.
DR PDB; 5LZE; EM; 3.50 A; d=2-206.
DR PDB; 5LZF; EM; 4.60 A; d=2-206.
DR PDB; 5MDV; EM; 2.97 A; i=1-206.
DR PDB; 5MDW; EM; 3.06 A; i=1-206.
DR PDB; 5MDY; EM; 3.35 A; i=1-206.
DR PDB; 5MDZ; EM; 3.10 A; i=1-206.
DR PDB; 5ME0; EM; 13.50 A; D=1-206.
DR PDB; 5ME1; EM; 13.50 A; D=1-206.
DR PDB; 5MGP; EM; 3.10 A; d=2-206.
DR PDB; 5MY1; EM; 7.60 A; D=2-206.
DR PDB; 5NO2; EM; 5.16 A; D=2-206.
DR PDB; 5NO3; EM; 5.16 A; D=2-206.
DR PDB; 5NO4; EM; 5.16 A; D=2-206.
DR PDB; 5NP6; EM; 3.60 A; G=2-206.
DR PDB; 5NWY; EM; 2.93 A; 3=1-206.
DR PDB; 5O2R; EM; 3.40 A; d=2-206.
DR PDB; 5U4I; EM; 3.50 A; d=1-206.
DR PDB; 5U4J; EM; 3.70 A; d=1-206.
DR PDB; 5U9F; EM; 3.20 A; D=1-206.
DR PDB; 5U9G; EM; 3.20 A; D=1-206.
DR PDB; 5UYK; EM; 3.90 A; D=2-206.
DR PDB; 5UYL; EM; 3.60 A; D=2-206.
DR PDB; 5UYM; EM; 3.20 A; D=2-206.
DR PDB; 5UYN; EM; 4.00 A; D=2-206.
DR PDB; 5UYP; EM; 3.90 A; D=2-206.
DR PDB; 5UYQ; EM; 3.80 A; D=2-206.
DR PDB; 5UZ4; EM; 5.80 A; D=1-206.
DR PDB; 5WDT; EM; 3.00 A; d=2-206.
DR PDB; 5WE4; EM; 3.10 A; d=2-206.
DR PDB; 5WE6; EM; 3.40 A; d=2-206.
DR PDB; 5WFK; EM; 3.40 A; d=2-206.
DR PDB; 6BU8; EM; 3.50 A; D=2-206.
DR PDB; 6BY1; X-ray; 3.94 A; AD/BD=2-206.
DR PDB; 6C4I; EM; 3.24 A; d=1-206.
DR PDB; 6ENF; EM; 3.20 A; d=2-206.
DR PDB; 6ENJ; EM; 3.70 A; d=2-206.
DR PDB; 6ENU; EM; 3.10 A; d=2-206.
DR PDB; 6GWT; EM; 3.80 A; d=2-206.
DR PDB; 6GXM; EM; 3.80 A; d=2-206.
DR PDB; 6GXN; EM; 3.90 A; d=2-206.
DR PDB; 6GXO; EM; 3.90 A; d=2-206.
DR PDB; 6GXP; EM; 4.40 A; d=2-206.
DR PDB; 6H4N; EM; 3.00 A; d=2-206.
DR PDB; 6H58; EM; 7.90 A; d/dd=2-206.
DR PDB; 6HRM; EM; 2.96 A; i=2-206.
DR PDB; 6I7V; X-ray; 2.90 A; AD/BD=2-206.
DR PDB; 6NQB; EM; 3.80 A; D=2-206.
DR PDB; 6O9J; EM; 3.90 A; d=2-206.
DR PDB; 6O9K; EM; 4.00 A; d=2-206.
DR PDB; 6OFX; EM; 3.30 A; I=2-206.
DR PDB; 6OG7; EM; 3.30 A; I=2-206.
DR PDB; 6ORE; EM; 2.90 A; i=2-206.
DR PDB; 6ORL; EM; 3.50 A; i=2-206.
DR PDB; 6OST; EM; 4.20 A; i=2-206.
DR PDB; 6OT3; EM; 3.90 A; i=2-206.
DR PDB; 6OUO; EM; 3.70 A; i=2-206.
DR PDB; 6Q97; EM; 3.90 A; i=2-206.
DR PDB; 6Q98; EM; 4.30 A; i=1-206.
DR PDB; 6Q9A; EM; 3.70 A; i=2-206.
DR PDB; 6SZS; EM; 3.06 A; d=1-206.
DR PDB; 6TBV; EM; 2.70 A; S041=1-206.
DR PDB; 6TC3; EM; 2.70 A; S041=1-206.
DR PDB; 6TQO; EM; 4.00 A; C=1-206.
DR PDB; 6VWL; EM; 3.10 A; c=1-206.
DR PDB; 6VWM; EM; 3.40 A; c=1-206.
DR PDB; 6VWN; EM; 3.40 A; c=1-206.
DR PDB; 6W6K; EM; 3.60 A; D=1-206.
DR PDB; 6W77; EM; 3.60 A; D=1-206.
DR PDB; 6W7M; EM; 3.80 A; D=1-206.
DR PDB; 6W7N; EM; 3.40 A; D=1-206.
DR PDB; 6W7W; EM; 3.90 A; C=1-206.
DR PDB; 6WD6; EM; 3.70 A; I=2-206.
DR PDB; 6WDB; EM; 4.00 A; I=2-206.
DR PDB; 6WDC; EM; 4.20 A; I=2-206.
DR PDB; 6WDD; EM; 3.20 A; I=2-206.
DR PDB; 6WDE; EM; 3.00 A; I=2-206.
DR PDB; 6WDF; EM; 3.30 A; I=2-206.
DR PDB; 6WDG; EM; 3.30 A; I=2-206.
DR PDB; 6WDH; EM; 4.30 A; I=2-206.
DR PDB; 6WDI; EM; 4.00 A; I=2-206.
DR PDB; 6WDJ; EM; 3.70 A; I=2-206.
DR PDB; 6WDK; EM; 3.60 A; I=2-206.
DR PDB; 6WDL; EM; 3.70 A; I=2-206.
DR PDB; 6WDM; EM; 3.60 A; I=2-206.
DR PDB; 6WNV; EM; 3.50 A; I=2-206.
DR PDB; 6WNW; EM; 3.20 A; I=2-206.
DR PDB; 6XE0; EM; 6.80 A; C=2-206.
DR PDB; 6XZA; EM; 2.66 A; D1=2-206.
DR PDB; 6XZB; EM; 2.54 A; D1=2-206.
DR PDB; 6Y69; EM; 2.86 A; d=2-206.
DR PDB; 6ZTL; EM; 3.50 A; AD=1-206.
DR PDB; 7ABZ; EM; 3.21 A; i=2-206.
DR PDB; 7AC7; EM; 3.08 A; i=2-206.
DR PDB; 7ACJ; EM; 3.20 A; i=2-206.
DR PDB; 7ACR; EM; 3.44 A; i=2-206.
DR PDB; 7AFI; EM; 3.53 A; D=1-206.
DR PDB; 7AFL; EM; 4.20 A; D=1-206.
DR PDB; 7AFO; EM; 3.93 A; D=1-206.
DR PDB; 7B5K; EM; 2.90 A; d=2-206.
DR PDB; 7BOD; EM; 2.88 A; D=1-206.
DR PDB; 7BOE; EM; 2.90 A; D=1-206.
DR PDB; 7BOF; EM; 2.92 A; D=1-206.
DR PDB; 7BOG; EM; 2.75 A; D=1-206.
DR PDB; 7BOH; EM; 2.82 A; D=1-206.
DR PDB; 7BOI; EM; 2.98 A; D=1-206.
DR PDB; 7D6Z; EM; 3.40 A; k=1-206.
DR PDB; 7D80; EM; 4.10 A; E=1-206.
DR PDB; 7JSS; EM; 3.70 A; I=2-206.
DR PDB; 7JSW; EM; 3.80 A; I=2-206.
DR PDB; 7JSZ; EM; 3.70 A; I=2-206.
DR PDB; 7JT1; EM; 3.30 A; I=2-206.
DR PDB; 7JT2; EM; 3.50 A; I=2-206.
DR PDB; 7JT3; EM; 3.70 A; I=2-206.
DR PDB; 7K50; EM; 3.40 A; I=2-206.
DR PDB; 7K51; EM; 3.50 A; I=2-206.
DR PDB; 7K52; EM; 3.40 A; I=2-206.
DR PDB; 7K53; EM; 3.20 A; I=2-206.
DR PDB; 7K54; EM; 3.20 A; I=2-206.
DR PDB; 7K55; EM; 3.30 A; I=2-206.
DR PDB; 7LV0; EM; 3.20 A; I=2-206.
DR PDB; 7N1P; EM; 2.33 A; SD=1-206.
DR PDB; 7N2C; EM; 2.72 A; SD=1-206.
DR PDB; 7N2U; EM; 2.53 A; SD=1-206.
DR PDB; 7N2V; EM; 2.54 A; SD=1-206.
DR PDB; 7N30; EM; 2.66 A; SD=1-206.
DR PDB; 7N31; EM; 2.69 A; SD=1-206.
DR PDB; 7NAR; EM; 3.00 A; D=1-206.
DR PDB; 7NAS; EM; 3.31 A; D=1-206.
DR PDB; 7NAT; EM; 3.59 A; D=1-206.
DR PDB; 7NAU; EM; 3.78 A; D=1-206.
DR PDB; 7NAV; EM; 4.80 A; D=1-206.
DR PDB; 7NBU; EM; 3.11 A; D=2-206.
DR PDB; 7O19; EM; 2.90 A; AD=1-206.
DR PDB; 7O1A; EM; 2.40 A; AD=1-206.
DR PDB; 7O1C; EM; 2.60 A; AD=1-206.
DR PDB; 7O5H; EM; 3.10 A; D=2-206.
DR PDB; 7OE0; EM; 2.69 A; D=2-206.
DR PDB; 7OE1; EM; 3.05 A; D=2-206.
DR PDB; 7OI0; EM; 2.76 A; D=2-206.
DR PDB; 7OIZ; EM; 2.90 A; D=1-206.
DR PDB; 7OJ0; EM; 3.50 A; D=1-206.
DR PDB; 7P3K; EM; 2.90 A; D=1-206.
DR PDB; 7PJV; EM; 3.10 A; d=1-206.
DR PDB; 7PJY; EM; 3.10 A; d=1-206.
DR PDB; 7QG8; EM; 3.97 A; 3=1-206.
DR PDB; 7QGH; EM; 4.48 A; 3=1-206.
DR PDB; 7S1I; EM; 2.48 A; F=1-206.
DR PDB; 7S1J; EM; 2.47 A; F=1-206.
DR PDB; 7S1K; EM; 2.42 A; F=1-206.
DR PDB; 7SS9; EM; 3.90 A; I=2-206.
DR PDB; 7SSD; EM; 3.30 A; I=2-206.
DR PDB; 7SSL; EM; 3.80 A; I=2-206.
DR PDB; 7SSN; EM; 3.20 A; I=2-206.
DR PDB; 7SSO; EM; 3.20 A; I=2-206.
DR PDB; 7SSW; EM; 3.80 A; I=2-206.
DR PDB; 7ST2; EM; 2.90 A; I=2-206.
DR PDB; 7ST6; EM; 3.00 A; I=2-206.
DR PDB; 7ST7; EM; 3.20 A; I=2-206.
DR PDBsum; 1EG0; -.
DR PDBsum; 2YKR; -.
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; 5U4J; -.
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; 6NQB; -.
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; 6TQO; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6W6K; -.
DR PDBsum; 6W77; -.
DR PDBsum; 6W7M; -.
DR PDBsum; 6W7N; -.
DR PDBsum; 6W7W; -.
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; 6ZTL; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7AFI; -.
DR PDBsum; 7AFL; -.
DR PDBsum; 7AFO; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BOD; -.
DR PDBsum; 7BOE; -.
DR PDBsum; 7BOF; -.
DR PDBsum; 7BOG; -.
DR PDBsum; 7BOH; -.
DR PDBsum; 7BOI; -.
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; 7NAS; -.
DR PDBsum; 7NAT; -.
DR PDBsum; 7NAU; -.
DR PDBsum; 7NAV; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7O5H; -.
DR PDBsum; 7OE0; -.
DR PDBsum; 7OE1; -.
DR PDBsum; 7OI0; -.
DR PDBsum; 7OIZ; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
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; P0A7V8; -.
DR SMR; P0A7V8; -.
DR BioGRID; 852105; 3.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR DIP; DIP-35794N; -.
DR IntAct; P0A7V8; 233.
DR MINT; P0A7V8; -.
DR STRING; 511145.b3296; -.
DR DrugBank; DB00453; Clomocycline.
DR DrugBank; DB12329; Eravacycline.
DR DrugBank; DB00256; Lymecycline.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB00595; Oxytetracycline.
DR DrugCentral; P0A7V8; -.
DR MoonProt; P0A7V8; -.
DR jPOST; P0A7V8; -.
DR PaxDb; P0A7V8; -.
DR PRIDE; P0A7V8; -.
DR EnsemblBacteria; AAC76321; AAC76321; b3296.
DR EnsemblBacteria; BAE77995; BAE77995; BAE77995.
DR GeneID; 67415337; -.
DR GeneID; 947793; -.
DR KEGG; ecj:JW3258; -.
DR KEGG; eco:b3296; -.
DR PATRIC; fig|1411691.4.peg.3435; -.
DR EchoBASE; EB0896; -.
DR eggNOG; COG0522; Bacteria.
DR HOGENOM; CLU_092403_0_2_6; -.
DR InParanoid; P0A7V8; -.
DR OMA; NVVFRMG; -.
DR PhylomeDB; P0A7V8; -.
DR BioCyc; EcoCyc:EG10903-MON; -.
DR BioCyc; MetaCyc:EG10903-MON; -.
DR EvolutionaryTrace; P0A7V8; -.
DR PRO; PR:P0A7V8; -.
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:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IMP:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IDA:EcoliWiki.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:EcoCyc.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
DR GO; GO:0031564; P:transcription antitermination; IDA:EcoCyc.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR PANTHER; PTHR11831:SF4; PTHR11831:SF4; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation;
KW Transcription termination; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1100394,
FT ECO:0000269|PubMed:4587210"
FT CHAIN 2..206
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132380"
FT DOMAIN 96..156
FT /note="S4 RNA-binding"
FT VARIANT 51
FT /note="Y -> D (in rpsD101; suppresses a temperature-
FT sensitive mutant of release factor 1, R137P. Not a ram
FT mutation)"
FT /evidence="ECO:0000269|PubMed:11018284"
FT VARIANT 170..206
FT /note="Missing (in rpsD16; suppresses streptomycin
FT dependence in protein S12. A ram mutation)"
FT /evidence="ECO:0000269|PubMed:11018284"
FT VARIANT 177..206
FT /note="KMEGTFKRKPERSDLSADINEHLIVELYSK -> GRYV (in rpsD12;
FT suppresses streptomycin dependence in protein S12. A ram
FT mutation)"
FT /evidence="ECO:0000269|PubMed:11018284"
FT VARIANT 179..206
FT /note="EGTFKRKPERSDLSADINEHLIVELYSK -> ARYV (in rpsD14;
FT suppresses streptomycin dependence in protein S12. A ram
FT mutation)"
FT /evidence="ECO:0000269|PubMed:11018284"
FT MUTAGEN 44..47
FT /note="RKPR->AKPA: Decreases mRNA unwinding ability of the
FT ribosome."
FT /evidence="ECO:0000269|PubMed:15652481"
FT CONFLICT 91
FT /note="Missing (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="E -> Q (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..144
FT /note="SPNDVVS -> DPNSVV (in Ref. 4; AA sequence and 5; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Q -> E (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> Q (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:7OI0"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6W7N"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:7OI0"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:7O5H"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:7OE0"
SQ SEQUENCE 206 AA; 23469 MW; 4015969DF8E582BB CRC64;
MARYLGPKLK LSRREGTDLF LKSGVRAIDT KCKIEQAPGQ HGARKPRLSD YGVQLREKQK
VRRIYGVLER QFRNYYKEAA RLKGNTGENL LALLEGRLDN VVYRMGFGAT RAEARQLVSH
KAIMVNGRVV NIASYQVSPN DVVSIREKAK KQSRVKAALE LAEQREKPTW LEVDAGKMEG
TFKRKPERSD LSADINEHLI VELYSK
