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Database: UniProt
Entry: P0A7V8
LinkDB: P0A7V8
Original site: P0A7V8 
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   30-AUG-2017, entry version 135.
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
RT   Escherichia 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.,
RA   Mau B., 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
RT   MG1655 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
RT   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;
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;
RA   Post L.E., Nomura M.;
RT   "Nucleotide sequence of the intercistronic region preceding the gene
RT   for 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
RT   novel 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
RT   via two 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   VARIANT 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
RT   a 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
RT   remarkably similar to NusA, a protein involved in both non-ribosomal
RT   and ribosomal RNA 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
RL   ed.), pp.979-1004, American Society for Microbiology Press, Washington
RL   D.C. (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
RT   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.,
RA   Frank J.;
RT   "Study of the structural dynamics of the E. coli 70S ribosome using
RT   real-space refinement.";
RL   Cell 113:789-801(2003).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP   STRUCTURES, 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.,
RA   Vila-Sanjurjo A., 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
RP   COMPLEX 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
RT   ArfA and RF2.";
RL   Nature 541:550-553(2017).
RN   [24]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27906161; DOI=10.1038/nature20821;
RA   Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O.,
RA   Beckmann R., Wilson D.N.;
RT   "Structural basis for ArfA-RF2-mediated translation termination on
RT   mRNAs 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
RT   bound to ribosome.";
RL   Nature 541:554-557(2017).
CC   -!- FUNCTION: One of two assembly initiator proteins for the 30S
CC       subunit, it binds directly to 16S rRNA where it nucleates assembly
CC       of the body 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
CC       protein S12 are found in this protein, some but not all of which
CC       decrease translational accuracy (ram, ribosomal ambiguity
CC       mutations).
CC   -!- FUNCTION: Plays a role in mRNA unwinding by the ribosome, possibly
CC       by forming part of a processivity clamp.
CC       {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,
CC       S11, S4, RNA polymerase alpha subunit, and L17) by binding to its
CC       mRNA. {ECO:0000269|PubMed:3309351}.
CC   -!- FUNCTION: Also functions as a rho-dependent antiterminator of rRNA
CC       transcription, increasing the synthesis of rRNA under conditions
CC       of excess protein, allowing a more rapid return to homeostasis.
CC       Binds directly to RNA polymerase. {ECO:0000269|PubMed:11447122}.
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,
CC       PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts
CC       protein S5. With proteins S3 and S5 encircles the mRNA as it
CC       enters the ribosome, which may play a role in mRNA helicase
CC       processivity (PubMed:15652481). Some nascent polypeptide chains
CC       are able to cross-link to this protein in situ (PubMed:9716382).
CC       {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:1100394,
CC       ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12809609,
CC       ECO:0000269|PubMed:15652481, 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:4587210, ECO:0000269|PubMed:7556101,
CC       ECO:0000269|PubMed:9716382}.
CC   -!- MASS SPECTROMETRY: Mass=23339.5; Method=MALDI; Range=2-206;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
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_LN832404.1.
DR   PDB; 1EG0; EM; 11.50 A; A=43-200.
DR   PDB; 1M5G; Model; -; D=2-206.
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; 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   PDBsum; 1EG0; -.
DR   PDBsum; 1M5G; -.
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; 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   ProteinModelPortal; P0A7V8; -.
DR   SMR; P0A7V8; -.
DR   BioGrid; 852105; 1.
DR   DIP; DIP-35794N; -.
DR   IntAct; P0A7V8; 214.
DR   MINT; MINT-6478162; -.
DR   STRING; 316385.ECDH10B_3471; -.
DR   DrugBank; DB00453; Clomocycline.
DR   DrugBank; DB00618; Demeclocycline.
DR   DrugBank; DB00254; Doxycycline.
DR   DrugBank; DB00256; Lymecycline.
DR   DrugBank; DB01017; Minocycline.
DR   DrugBank; DB00595; Oxytetracycline.
DR   MoonProt; P0A7V8; -.
DR   PaxDb; P0A7V8; -.
DR   PRIDE; P0A7V8; -.
DR   EnsemblBacteria; AAC76321; AAC76321; b3296.
DR   EnsemblBacteria; BAE77995; BAE77995; BAE77995.
DR   GeneID; 32366218; -.
DR   GeneID; 947793; -.
DR   KEGG; ecj:JW3258; -.
DR   KEGG; eco:b3296; -.
DR   PATRIC; fig|1411691.4.peg.3435; -.
DR   EchoBASE; EB0896; -.
DR   EcoGene; EG10903; rpsD.
DR   eggNOG; ENOG4105G6W; Bacteria.
DR   eggNOG; COG0522; LUCA.
DR   HOGENOM; HOG000221003; -.
DR   InParanoid; P0A7V8; -.
DR   KO; K02986; -.
DR   PhylomeDB; P0A7V8; -.
DR   BioCyc; EcoCyc:EG10903-MONOMER; -.
DR   BioCyc; MetaCyc:EG10903-MONOMER; -.
DR   EvolutionaryTrace; P0A7V8; -.
DR   PRO; PR:P0A7V8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:CAFA.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
DR   GO; GO:0019843; F:rRNA binding; IDA:EcoliWiki.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR   GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IMP:EcoCyc.
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   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   PANTHER; PTHR11831; PTHR11831; 1.
DR   PANTHER; PTHR11831:SF17; PTHR11831:SF17; 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; Complete proteome;
KW   Direct protein sequencing; Reference proteome; Repressor;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   Transcription; Transcription regulation; Transcription termination;
KW   Translation regulation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:1100394,
FT                                ECO:0000269|PubMed:4587210}.
FT   CHAIN         2    206       30S ribosomal protein S4.
FT                                /FTId=PRO_0000132380.
FT   DOMAIN       96    156       S4 RNA-binding.
FT   VARIANT      51     51       Y -> D (in rpsD101; suppresses a
FT                                temperature-sensitive mutant of release
FT                                factor 1, R137P. Not a ram mutation).
FT   VARIANT     170    206       Missing (in rpsD16; suppresses
FT                                streptomycin dependence in protein S12. A
FT                                ram mutation).
FT   VARIANT     177    206       KMEGTFKRKPERSDLSADINEHLIVELYSK -> GRYV
FT                                (in rpsD12; suppresses streptomycin
FT                                dependence in protein S12. A ram
FT                                mutation).
FT   VARIANT     179    206       EGTFKRKPERSDLSADINEHLIVELYSK -> ARYV (in
FT                                rpsD14; suppresses streptomycin
FT                                dependence in protein S12. A ram
FT                                mutation).
FT   MUTAGEN      44     47       RKPR->AKPA: Decreases mRNA unwinding
FT                                ability of the ribosome.
FT                                {ECO:0000269|PubMed:15652481}.
FT   CONFLICT     91     91       Missing (in Ref. 4; AA sequence and 5; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT     95     95       E -> Q (in Ref. 4; AA sequence and 5; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    138    144       SPNDVVS -> DPNSVV (in Ref. 4; AA sequence
FT                                and 5; AA sequence). {ECO:0000305}.
FT   CONFLICT    152    152       Q -> E (in Ref. 4; AA sequence and 5; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    166    166       E -> Q (in Ref. 4; AA sequence and 5; AA
FT                                sequence). {ECO:0000305}.
FT   HELIX         9     15       {ECO:0000244|PDB:4U26}.
FT   STRAND       20     22       {ECO:0000244|PDB:4V9O}.
FT   STRAND       24     26       {ECO:0000244|PDB:4V9O}.
FT   STRAND       28     32       {ECO:0000244|PDB:4U27}.
FT   STRAND       34     36       {ECO:0000244|PDB:4U26}.
FT   STRAND       38     41       {ECO:0000244|PDB:4U26}.
FT   STRAND       42     44       {ECO:0000244|PDB:4V50}.
FT   HELIX        50     65       {ECO:0000244|PDB:4U26}.
FT   HELIX        69     81       {ECO:0000244|PDB:4U26}.
FT   STRAND       82     84       {ECO:0000244|PDB:4U26}.
FT   HELIX        86     95       {ECO:0000244|PDB:4U26}.
FT   HELIX        98    104       {ECO:0000244|PDB:4U26}.
FT   STRAND      107    110       {ECO:0000244|PDB:4U26}.
FT   HELIX       111    119       {ECO:0000244|PDB:4U26}.
FT   TURN        120    122       {ECO:0000244|PDB:4V6C}.
FT   STRAND      124    129       {ECO:0000244|PDB:4U26}.
FT   STRAND      132    134       {ECO:0000244|PDB:4V9C}.
FT   STRAND      142    144       {ECO:0000244|PDB:4U26}.
FT   TURN        147    151       {ECO:0000244|PDB:4U26}.
FT   HELIX       153    164       {ECO:0000244|PDB:4U26}.
FT   STRAND      169    172       {ECO:0000244|PDB:4U26}.
FT   STRAND      175    177       {ECO:0000244|PDB:4U26}.
FT   STRAND      179    182       {ECO:0000244|PDB:4U26}.
FT   HELIX       188    190       {ECO:0000244|PDB:4U26}.
FT   STRAND      193    195       {ECO:0000244|PDB:4V9C}.
FT   HELIX       197    203       {ECO:0000244|PDB:4U26}.
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
//
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