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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   26-NOV-2014, entry version 108.
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       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- SIMILARITY: Belongs to the ribosomal protein S4P family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {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; 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=3-206.
DR   PDB; 2GYB; EM; 15.00 A; D=3-206.
DR   PDB; 2I2P; X-ray; 3.22 A; D=2-206.
DR   PDB; 2I2U; X-ray; 3.22 A; D=2-206.
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   PDB; 4PE9; X-ray; 2.95 A; D=2-206.
DR   PDB; 4PEA; X-ray; 2.95 A; D=2-206.
DR   PDB; 4TOL; X-ray; 3.00 A; D=2-206.
DR   PDB; 4TON; X-ray; 3.00 A; D=2-206.
DR   PDB; 4TOU; X-ray; 2.90 A; D=2-206.
DR   PDB; 4TOW; X-ray; 2.90 A; D=2-206.
DR   PDB; 4TP0; X-ray; 2.90 A; D=2-206.
DR   PDB; 4TP2; X-ray; 2.90 A; D=2-206.
DR   PDB; 4TP4; X-ray; 2.90 A; D=2-206.
DR   PDB; 4TP6; X-ray; 2.90 A; D=2-206.
DR   PDB; 4TP8; X-ray; 2.80 A; D=2-206.
DR   PDB; 4TPA; X-ray; 2.80 A; D=2-206.
DR   PDB; 4TPC; X-ray; 2.80 A; D=2-206.
DR   PDB; 4TPE; X-ray; 2.80 A; D=2-206.
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   PDBsum; 4PE9; -.
DR   PDBsum; 4PEA; -.
DR   PDBsum; 4TOL; -.
DR   PDBsum; 4TON; -.
DR   PDBsum; 4TOU; -.
DR   PDBsum; 4TOW; -.
DR   PDBsum; 4TP0; -.
DR   PDBsum; 4TP2; -.
DR   PDBsum; 4TP4; -.
DR   PDBsum; 4TP6; -.
DR   PDBsum; 4TP8; -.
DR   PDBsum; 4TPA; -.
DR   PDBsum; 4TPC; -.
DR   PDBsum; 4TPE; -.
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   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   InParanoid; P0A7V8; -.
DR   KO; K02986; -.
DR   OMA; TCKLSRR; -.
DR   OrthoDB; EOG6N3CXM; -.
DR   PhylomeDB; P0A7V8; -.
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. {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:4TP8}.
FT   STRAND       20     22       {ECO:0000244|PDB:4KIY}.
FT   STRAND       24     26       {ECO:0000244|PDB:4KJ0}.
FT   STRAND       28     32       {ECO:0000244|PDB:4TPE}.
FT   STRAND       34     36       {ECO:0000244|PDB:4TPA}.
FT   STRAND       38     41       {ECO:0000244|PDB:4TPA}.
FT   STRAND       42     44       {ECO:0000244|PDB:2I2P}.
FT   HELIX        50     65       {ECO:0000244|PDB:4TP8}.
FT   HELIX        69     81       {ECO:0000244|PDB:4TP8}.
FT   STRAND       82     84       {ECO:0000244|PDB:4TP8}.
FT   HELIX        86     95       {ECO:0000244|PDB:4TP8}.
FT   HELIX        98    104       {ECO:0000244|PDB:4TP8}.
FT   STRAND      107    110       {ECO:0000244|PDB:4TP8}.
FT   HELIX       111    119       {ECO:0000244|PDB:4TP8}.
FT   TURN        120    122       {ECO:0000244|PDB:3I1O}.
FT   STRAND      124    129       {ECO:0000244|PDB:4TP8}.
FT   STRAND      132    134       {ECO:0000244|PDB:4GAQ}.
FT   STRAND      142    144       {ECO:0000244|PDB:4TP8}.
FT   TURN        147    151       {ECO:0000244|PDB:4TPA}.
FT   HELIX       153    164       {ECO:0000244|PDB:4TP8}.
FT   STRAND      169    172       {ECO:0000244|PDB:4TP8}.
FT   STRAND      175    177       {ECO:0000244|PDB:4TP8}.
FT   STRAND      179    182       {ECO:0000244|PDB:4TP8}.
FT   HELIX       188    190       {ECO:0000244|PDB:4TPA}.
FT   STRAND      193    195       {ECO:0000244|PDB:4GAS}.
FT   HELIX       197    203       {ECO:0000244|PDB:4TP8}.
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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