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Entry: P0A7V8
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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   16-APR-2014, entry version 103.
DE   RecName: Full=30S ribosomal protein S4;
GN   Name=rpsD; Synonyms=ramA; OrderedLocusNames=b3296, JW3258;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
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.
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.
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, 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   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   [15]
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   [16]
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   [17]
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   [18]
RP   3D-STRUCTURE MODELING.
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   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
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   [20]
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   [21]
RP   X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP   STRUCTURES.
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).
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.
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   -!- 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.
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.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5.
CC       With proteins S3 and S5 encircles the mRNA as it enters the
CC       ribosome, which may play a role in mRNA helicase processivity.
CC       Some nascent polypeptide chains are able to cross-link to this
CC       protein in situ.
CC   -!- MASS SPECTROMETRY: Mass=23339.5; Method=MALDI; Range=2-206;
CC       Source=PubMed:10094780;
CC   -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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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; YP_492136.1; NC_007779.1.
DR   PDB; 1EG0; EM; 11.50 A; A=43-200.
DR   PDB; 1M5G; Model; -; D=2-206.
DR   PDB; 1P6G; EM; 12.30 A; D=2-206.
DR   PDB; 1P87; EM; 11.50 A; D=2-206.
DR   PDB; 1VS5; X-ray; 3.46 A; D=1-206.
DR   PDB; 1VS7; X-ray; 3.46 A; D=1-206.
DR   PDB; 2AVY; X-ray; 3.46 A; D=2-206.
DR   PDB; 2AW7; X-ray; 3.46 A; D=2-206.
DR   PDB; 2GY9; EM; 15.00 A; D=3-205.
DR   PDB; 2GYB; EM; 15.00 A; D=3-205.
DR   PDB; 2I2P; X-ray; 3.22 A; D=2-205.
DR   PDB; 2I2U; X-ray; 3.22 A; D=2-205.
DR   PDB; 2QAL; X-ray; 3.21 A; D=2-206.
DR   PDB; 2QAN; X-ray; 3.21 A; D=2-206.
DR   PDB; 2QB9; X-ray; 3.54 A; D=2-206.
DR   PDB; 2QBB; X-ray; 3.54 A; D=2-206.
DR   PDB; 2QBD; X-ray; 3.30 A; D=2-206.
DR   PDB; 2QBF; X-ray; 3.30 A; D=2-206.
DR   PDB; 2QBH; X-ray; 4.00 A; D=2-206.
DR   PDB; 2QBJ; X-ray; 4.00 A; D=2-206.
DR   PDB; 2QOU; X-ray; 3.93 A; D=2-206.
DR   PDB; 2QOW; X-ray; 3.93 A; D=2-206.
DR   PDB; 2QOY; X-ray; 3.50 A; D=2-206.
DR   PDB; 2QP0; X-ray; 3.50 A; D=2-206.
DR   PDB; 2VHP; X-ray; 3.74 A; D=2-206.
DR   PDB; 2WWL; EM; 5.80 A; D=2-206.
DR   PDB; 2YKR; EM; 9.80 A; D=2-206.
DR   PDB; 2Z4K; X-ray; 4.45 A; D=2-206.
DR   PDB; 2Z4M; X-ray; 4.45 A; D=2-206.
DR   PDB; 3DF1; X-ray; 3.50 A; D=2-205.
DR   PDB; 3DF3; X-ray; 3.50 A; D=2-205.
DR   PDB; 3E1A; EM; -; R=1-206.
DR   PDB; 3E1C; EM; -; R=1-206.
DR   PDB; 3FIH; EM; 6.70 A; D=2-206.
DR   PDB; 3I1M; X-ray; 3.19 A; D=1-206.
DR   PDB; 3I1O; X-ray; 3.19 A; D=1-206.
DR   PDB; 3I1Q; X-ray; 3.81 A; D=1-206.
DR   PDB; 3I1S; X-ray; 3.81 A; D=1-206.
DR   PDB; 3I1Z; X-ray; 3.71 A; D=1-206.
DR   PDB; 3I21; X-ray; 3.71 A; D=1-206.
DR   PDB; 3IZV; EM; -; H=1-206.
DR   PDB; 3IZW; EM; -; H=1-206.
DR   PDB; 3J00; EM; -; D=2-206.
DR   PDB; 3J0U; EM; 12.10 A; G=2-206.
DR   PDB; 3J0V; EM; 14.70 A; G=2-206.
DR   PDB; 3J0X; EM; 13.50 A; G=2-206.
DR   PDB; 3J0Z; EM; 11.50 A; G=2-206.
DR   PDB; 3J10; EM; 11.50 A; G=2-206.
DR   PDB; 3J13; EM; 13.10 A; F=2-206.
DR   PDB; 3J18; EM; 8.30 A; D=2-206.
DR   PDB; 3J36; EM; 9.80 A; D=2-206.
DR   PDB; 3J4V; EM; 12.00 A; D=1-206.
DR   PDB; 3J4W; EM; 12.00 A; D=1-206.
DR   PDB; 3J4Y; EM; 17.00 A; D=1-206.
DR   PDB; 3J4Z; EM; 20.00 A; D=1-206.
DR   PDB; 3J53; EM; 13.00 A; D=1-206.
DR   PDB; 3J55; EM; 15.00 A; D=1-206.
DR   PDB; 3J57; EM; 17.00 A; D=1-206.
DR   PDB; 3J59; EM; 12.00 A; D=1-206.
DR   PDB; 3J5B; EM; 17.00 A; D=1-206.
DR   PDB; 3J5D; EM; 17.00 A; D=1-206.
DR   PDB; 3J5F; EM; 20.00 A; D=1-206.
DR   PDB; 3J5H; EM; 15.00 A; D=1-206.
DR   PDB; 3J5J; EM; 9.00 A; D=1-206.
DR   PDB; 3J5N; EM; 6.80 A; D=1-206.
DR   PDB; 3J5T; EM; 7.60 A; D=2-206.
DR   PDB; 3J5X; EM; 7.60 A; D=2-206.
DR   PDB; 3KC4; EM; -; D=1-206.
DR   PDB; 3OAQ; X-ray; 3.25 A; D=2-206.
DR   PDB; 3OAR; X-ray; 3.25 A; D=2-206.
DR   PDB; 3OFA; X-ray; 3.19 A; D=2-206.
DR   PDB; 3OFB; X-ray; 3.19 A; D=2-206.
DR   PDB; 3OFO; X-ray; 3.10 A; D=2-206.
DR   PDB; 3OFP; X-ray; 3.10 A; D=2-206.
DR   PDB; 3OFX; X-ray; 3.29 A; D=2-206.
DR   PDB; 3OFY; X-ray; 3.29 A; D=2-206.
DR   PDB; 3OR9; X-ray; 3.30 A; D=1-206.
DR   PDB; 3ORA; X-ray; 3.30 A; D=1-206.
DR   PDB; 3SFS; X-ray; 3.20 A; D=1-206.
DR   PDB; 3UOQ; X-ray; 3.70 A; D=1-206.
DR   PDB; 4A2I; EM; 16.50 A; D=2-206.
DR   PDB; 4ADV; EM; 13.50 A; D=2-206.
DR   PDB; 4GAQ; X-ray; 3.30 A; D=1-206.
DR   PDB; 4GAS; X-ray; 3.30 A; D=1-206.
DR   PDB; 4GD1; X-ray; 3.00 A; D=2-206.
DR   PDB; 4GD2; X-ray; 3.00 A; D=2-206.
DR   PDB; 4KIY; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJ0; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJ2; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJ4; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJ6; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJ8; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJA; X-ray; 2.90 A; D=1-206.
DR   PDB; 4KJC; X-ray; 2.90 A; D=1-206.
DR   PDBsum; 1EG0; -.
DR   PDBsum; 1M5G; -.
DR   PDBsum; 1P6G; -.
DR   PDBsum; 1P87; -.
DR   PDBsum; 1VS5; -.
DR   PDBsum; 1VS7; -.
DR   PDBsum; 2AVY; -.
DR   PDBsum; 2AW7; -.
DR   PDBsum; 2GY9; -.
DR   PDBsum; 2GYB; -.
DR   PDBsum; 2I2P; -.
DR   PDBsum; 2I2U; -.
DR   PDBsum; 2QAL; -.
DR   PDBsum; 2QAN; -.
DR   PDBsum; 2QB9; -.
DR   PDBsum; 2QBB; -.
DR   PDBsum; 2QBD; -.
DR   PDBsum; 2QBF; -.
DR   PDBsum; 2QBH; -.
DR   PDBsum; 2QBJ; -.
DR   PDBsum; 2QOU; -.
DR   PDBsum; 2QOW; -.
DR   PDBsum; 2QOY; -.
DR   PDBsum; 2QP0; -.
DR   PDBsum; 2VHP; -.
DR   PDBsum; 2WWL; -.
DR   PDBsum; 2YKR; -.
DR   PDBsum; 2Z4K; -.
DR   PDBsum; 2Z4M; -.
DR   PDBsum; 3DF1; -.
DR   PDBsum; 3DF3; -.
DR   PDBsum; 3E1A; -.
DR   PDBsum; 3E1C; -.
DR   PDBsum; 3FIH; -.
DR   PDBsum; 3I1M; -.
DR   PDBsum; 3I1O; -.
DR   PDBsum; 3I1Q; -.
DR   PDBsum; 3I1S; -.
DR   PDBsum; 3I1Z; -.
DR   PDBsum; 3I21; -.
DR   PDBsum; 3IZV; -.
DR   PDBsum; 3IZW; -.
DR   PDBsum; 3J00; -.
DR   PDBsum; 3J0U; -.
DR   PDBsum; 3J0V; -.
DR   PDBsum; 3J0X; -.
DR   PDBsum; 3J0Z; -.
DR   PDBsum; 3J10; -.
DR   PDBsum; 3J13; -.
DR   PDBsum; 3J18; -.
DR   PDBsum; 3J36; -.
DR   PDBsum; 3J4V; -.
DR   PDBsum; 3J4W; -.
DR   PDBsum; 3J4Y; -.
DR   PDBsum; 3J4Z; -.
DR   PDBsum; 3J53; -.
DR   PDBsum; 3J55; -.
DR   PDBsum; 3J57; -.
DR   PDBsum; 3J59; -.
DR   PDBsum; 3J5B; -.
DR   PDBsum; 3J5D; -.
DR   PDBsum; 3J5F; -.
DR   PDBsum; 3J5H; -.
DR   PDBsum; 3J5J; -.
DR   PDBsum; 3J5N; -.
DR   PDBsum; 3J5T; -.
DR   PDBsum; 3J5X; -.
DR   PDBsum; 3KC4; -.
DR   PDBsum; 3OAQ; -.
DR   PDBsum; 3OAR; -.
DR   PDBsum; 3OFA; -.
DR   PDBsum; 3OFB; -.
DR   PDBsum; 3OFO; -.
DR   PDBsum; 3OFP; -.
DR   PDBsum; 3OFX; -.
DR   PDBsum; 3OFY; -.
DR   PDBsum; 3OR9; -.
DR   PDBsum; 3ORA; -.
DR   PDBsum; 3SFS; -.
DR   PDBsum; 3UOQ; -.
DR   PDBsum; 4A2I; -.
DR   PDBsum; 4ADV; -.
DR   PDBsum; 4GAQ; -.
DR   PDBsum; 4GAS; -.
DR   PDBsum; 4GD1; -.
DR   PDBsum; 4GD2; -.
DR   PDBsum; 4KIY; -.
DR   PDBsum; 4KJ0; -.
DR   PDBsum; 4KJ2; -.
DR   PDBsum; 4KJ4; -.
DR   PDBsum; 4KJ6; -.
DR   PDBsum; 4KJ8; -.
DR   PDBsum; 4KJA; -.
DR   PDBsum; 4KJC; -.
DR   ProteinModelPortal; P0A7V8; -.
DR   SMR; P0A7V8; 2-206.
DR   BioGrid; 852105; 1.
DR   DIP; DIP-35794N; -.
DR   IntAct; P0A7V8; 214.
DR   MINT; MINT-6478162; -.
DR   STRING; 511145.b3296; -.
DR   ChEMBL; CHEMBL2363135; -.
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   DrugBank; DB00759; Tetracycline.
DR   DrugBank; DB00560; Tigecycline.
DR   PaxDb; P0A7V8; -.
DR   PRIDE; P0A7V8; -.
DR   EnsemblBacteria; AAC76321; AAC76321; b3296.
DR   EnsemblBacteria; BAE77995; BAE77995; BAE77995.
DR   GeneID; 12934394; -.
DR   GeneID; 947793; -.
DR   KEGG; ecj:Y75_p3880; -.
DR   KEGG; eco:b3296; -.
DR   PATRIC; 32122024; VBIEscCol129921_3389.
DR   EchoBASE; EB0896; -.
DR   EcoGene; EG10903; rpsD.
DR   eggNOG; COG0522; -.
DR   HOGENOM; HOG000221003; -.
DR   KO; K02986; -.
DR   OMA; THGHILV; -.
DR   OrthoDB; EOG6N3CXM; -.
DR   ProtClustDB; PRK05327; -.
DR   BioCyc; EcoCyc:EG10903-MONOMER; -.
DR   BioCyc; ECOL316407:JW3258-MONOMER; -.
DR   EvolutionaryTrace; P0A7V8; -.
DR   PRO; PR:P0A7V8; -.
DR   Genevestigator; P0A7V8; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
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; IEA:InterPro.
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:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0031564; P:transcription antitermination; IDA:EcoCyc.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1050.10; -; 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   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; 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.
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   CONFLICT     91     91       Missing (in Ref. 4; AA sequence and 5; AA
FT                                sequence).
FT   CONFLICT     95     95       E -> Q (in Ref. 4; AA sequence and 5; AA
FT                                sequence).
FT   CONFLICT    138    144       SPNDVVS -> DPNSVV (in Ref. 4; AA sequence
FT                                and 5; AA sequence).
FT   CONFLICT    152    152       Q -> E (in Ref. 4; AA sequence and 5; AA
FT                                sequence).
FT   CONFLICT    166    166       E -> Q (in Ref. 4; AA sequence and 5; AA
FT                                sequence).
FT   HELIX         9     15
FT   STRAND       20     22
FT   STRAND       24     26
FT   STRAND       30     32
FT   STRAND       34     36
FT   STRAND       38     41
FT   STRAND       42     44
FT   HELIX        50     65
FT   HELIX        69     81
FT   STRAND       82     84
FT   HELIX        86     96
FT   HELIX        98    104
FT   STRAND      107    110
FT   HELIX       111    119
FT   TURN        120    122
FT   STRAND      123    129
FT   STRAND      132    134
FT   STRAND      142    145
FT   HELIX       147    149
FT   HELIX       153    163
FT   TURN        164    166
FT   STRAND      169    172
FT   STRAND      175    177
FT   STRAND      179    182
FT   HELIX       188    190
FT   STRAND      193    195
FT   HELIX       198    205
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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