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 01-MAY-2013, entry version 95.
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 277:1453-1474(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 MASS 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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_000913.2.
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; 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 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; 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 ProteinModelPortal; P0A7V8; -.
DR SMR; P0A7V8; 2-206.
DR DIP; DIP-35794N; -.
DR IntAct; P0A7V8; 211.
DR STRING; 511145.b3296; -.
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 ProtClustDB; PRK05327; -.
DR BioCyc; EcoCyc:EG10903-MONOMER; -.
DR BioCyc; ECOL316407:JW3258-MONOMER; -.
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 EvolutionaryTrace; P0A7V8; -.
DR Genevestigator; P0A7V8; -.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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-dependent 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: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 95
FT STRAND 97 99
FT HELIX 100 103
FT TURN 104 106
FT STRAND 107 110
FT HELIX 111 119
FT TURN 120 122
FT STRAND 124 129
FT STRAND 132 134
FT STRAND 141 144
FT STRAND 147 149
FT STRAND 150 152
FT HELIX 153 162
FT TURN 164 166
FT STRAND 169 172
FT STRAND 175 177
FT STRAND 179 182
FT STRAND 188 191
FT STRAND 193 195
FT HELIX 199 205
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
//
