Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

30S ribosomal protein S4 (Small ribosomal subunit protein uS4)

 RS4_ECOLI               Reviewed;         206 AA.
P0A7V8; P02354; Q2M6W1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
07-NOV-2018, entry version 147.
RecName: Full=30S ribosomal protein S4;
AltName: Full=Small ribosomal subunit protein uS4 {ECO:0000303|PubMed:24524803};
Name=rpsD; Synonyms=ramA; OrderedLocusNames=b3296, JW3258;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2989779; DOI=10.1093/nar/13.11.3891;
Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H.,
Zengel J.M., Lindahl L.;
"Nucleotide sequence of the alpha ribosomal protein operon of
Escherichia coli.";
Nucleic Acids Res. 13:3891-3903(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 2-206, AND SUBUNIT.
STRAIN=AB774;
PubMed=4587210; DOI=10.1016/0014-5793(73)80383-7;
Reinbolt J., Schiltz E.;
"The primary structure of ribosomal protein S4 from Escherichia
coli.";
FEBS Lett. 36:250-252(1973).
[5]
PROTEIN SEQUENCE OF 2-206, AND SUBUNIT.
STRAIN=K;
PubMed=1100394; DOI=10.1111/j.1432-1033.1975.tb02253.x;
Schiltz E., Reinbolt J.;
"Determination of the complete amino-acid sequence of protein S4 from
Escherichia coli ribosomes.";
Eur. J. Biochem. 56:467-481(1975).
[6]
PROTEIN SEQUENCE OF 78-91, SUBUNIT, AND CROSS-LINKING TO RRNA.
STRAIN=MRE-600;
PubMed=7556101;
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
"Protein-rRNA binding features and their structural and functional
implications in ribosomes as determined by cross-linking studies.";
EMBO J. 14:4578-4588(1995).
[7]
PROTEIN SEQUENCE OF 84-97 AND 129-146, AND IDENTIFICATION BY MASS
SPECTROMETRY.
Bienvenut W.V., Barblan J., Quadroni M.;
Submitted (JAN-2004) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-206.
PubMed=387752;
Post L.E., Nomura M.;
"Nucleotide sequence of the intercistronic region preceding the gene
for RNA polymerase subunit alpha in Escherichia coli.";
J. Biol. Chem. 254:10604-10606(1979).
[9]
MECHANISM OF TRANSLATION REGULATION.
PubMed=3309351; DOI=10.1016/0022-2836(87)90694-2;
Thomas M.S., Bedwell D.M., Nomura M.;
"Regulation of alpha operon gene expression in Escherichia coli. A
novel form of translational coupling.";
J. Mol. Biol. 196:333-345(1987).
[10]
ROLE IN SUBUNIT ASSEMBLY.
STRAIN=K12 / D10;
PubMed=2461734; DOI=10.1021/bi00418a057;
Nowotny V., Nierhaus K.H.;
"Assembly of the 30S subunit from Escherichia coli ribosomes occurs
via two assembly domains which are initiated by S4 and S7.";
Biochemistry 27:7051-7055(1988).
[11]
EFFECT OF MUTATIONS ON RRNA FOLDING.
STRAIN=UD1A1;
PubMed=2477554; DOI=10.1016/0022-2836(89)90509-3;
Allen P.N., Noller H.F.;
"Mutations in ribosomal proteins S4 and S12 influence the higher order
structure of 16 S ribosomal RNA.";
J. Mol. Biol. 208:457-468(1989).
[12]
BINDING TO MRNA.
PubMed=7559430; DOI=10.1074/jbc.270.39.22939;
Baker A.M., Draper D.E.;
"Messenger RNA recognition by fragments of ribosomal protein S4.";
J. Biol. Chem. 270:22939-22945(1995).
[13]
CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
PubMed=9716382; DOI=10.1046/j.1432-1327.1998.2550409.x;
Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.;
"Flexibility of the nascent polypeptide chain within the ribosome
-- contacts from the peptide N-terminus to a specific region of the
30S subunit.";
Eur. J. Biochem. 255:409-413(1998).
[14]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[15]
VARIANT THAT AFFECTS TERMINATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=11018284; DOI=10.1016/S0300-9084(00)01160-3;
Dahlgren A., Ryden-Aulin M.;
"A novel mutation in ribosomal protein S4 that affects the function of
a mutated RF1.";
Biochimie 82:683-691(2000).
[16]
RHO-DEPENDENT RIBOSOMAL RNA ANTITERMINATION FUNCTION.
PubMed=11447122; DOI=10.1093/emboj/20.14.3811;
Torres M., Condon C., Balada J.-M., Squires C., Squires C.L.;
"Ribosomal protein S4 is a transcription factor with properties
remarkably similar to NusA, a protein involved in both non-ribosomal
and ribosomal RNA antitermination.";
EMBO J. 20:3811-3820(2001).
[17]
ROLE IN MRNA HELICASE ACTIVITY, AND MUTAGENESIS.
STRAIN=MRE-600;
PubMed=15652481; DOI=10.1016/j.cell.2004.11.042;
Takyar S., Hickerson R.P., Noller H.F.;
"mRNA helicase activity of the ribosome.";
Cell 120:49-58(2005).
[18]
MASS SPECTROMETRY.
STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
PubMed=10094780; DOI=10.1006/abio.1998.3077;
Arnold R.J., Reilly J.P.;
"Observation of Escherichia coli ribosomal proteins and their
posttranslational modifications by mass spectrometry.";
Anal. Biochem. 269:105-112(1999).
[19]
REVIEW ON TRANSLATIONAL ACCURACY.
Kurland C.G., Hughes D., Ehrenberg M.;
"Limitations of translational accuracy.";
(In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
Umbarger H.E. (eds.);
Escherichia coli and Salmonella: Cellular and molecular biology (2nd
ed.), pp.979-1004, American Society for Microbiology Press, Washington
D.C. (1996).
[20]
3D-STRUCTURE MODELING, AND SUBUNIT.
PubMed=12244297; DOI=10.1038/nsb841;
Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
"All-atom homology model of the Escherichia coli 30S ribosomal
subunit.";
Nat. Struct. Biol. 9:750-755(2002).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
STRAIN=MRE-600;
PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6;
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S.,
Frank J.;
"Study of the structural dynamics of the E. coli 70S ribosome using
real-space refinement.";
Cell 113:789-801(2003).
[22]
X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
STRUCTURES, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=16272117; DOI=10.1126/science.1117230;
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W.,
Vila-Sanjurjo A., Holton J.M., Cate J.H.D.;
"Structures of the bacterial ribosome at 3.5 A resolution.";
Science 310:827-834(2005).
[23]
STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27906160; DOI=10.1038/nature20822;
Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
"Mechanistic insights into the alternative translation termination by
ArfA and RF2.";
Nature 541:550-553(2017).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27906161; DOI=10.1038/nature20821;
Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O.,
Beckmann R., Wilson D.N.;
"Structural basis for ArfA-RF2-mediated translation termination on
mRNAs lacking stop codons.";
Nature 541:546-549(2017).
[25]
STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27934701; DOI=10.1126/science.aai9127;
James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
"Translational termination without a stop codon.";
Science 354:1437-1440(2016).
[26]
STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=28077875; DOI=10.1038/nature21053;
Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
Jin H.;
"Structural basis of co-translational quality control by ArfA and RF2
bound to ribosome.";
Nature 541:554-557(2017).
-!- FUNCTION: One of two assembly initiator proteins for the 30S
subunit, it binds directly to 16S rRNA where it nucleates assembly
of the body of the 30S subunit. {ECO:0000269|PubMed:2461734}.
-!- FUNCTION: With S5 and S12 plays an important role in translational
accuracy; many suppressors of streptomycin-dependent mutants of
protein S12 are found in this protein, some but not all of which
decrease translational accuracy (ram, ribosomal ambiguity
mutations).
-!- FUNCTION: Plays a role in mRNA unwinding by the ribosome, possibly
by forming part of a processivity clamp.
{ECO:0000269|PubMed:15652481}.
-!- FUNCTION: Protein S4 is also a translational repressor protein, it
controls the translation of the alpha-operon (which codes for S13,
S11, S4, RNA polymerase alpha subunit, and L17) by binding to its
mRNA. {ECO:0000269|PubMed:3309351}.
-!- FUNCTION: Also functions as a rho-dependent antiterminator of rRNA
transcription, increasing the synthesis of rRNA under conditions
of excess protein, allowing a more rapid return to homeostasis.
Binds directly to RNA polymerase. {ECO:0000269|PubMed:11447122}.
-!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:4587210,
PubMed:1100394, PubMed:7556101, PubMed:12809609, PubMed:16272117,
PubMed:27934701, PubMed:10094780, PubMed:12244297,
PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts
protein S5. With proteins S3 and S5 encircles the mRNA as it
enters the ribosome, which may play a role in mRNA helicase
processivity (PubMed:15652481). Some nascent polypeptide chains
are able to cross-link to this protein in situ (PubMed:9716382).
{ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:1100394,
ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12809609,
ECO:0000269|PubMed:15652481, ECO:0000269|PubMed:16272117,
ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875,
ECO:0000269|PubMed:4587210, ECO:0000269|PubMed:7556101,
ECO:0000269|PubMed:9716382}.
-!- INTERACTION:
P0A9J0:rng; NbExp=2; IntAct=EBI-543939, EBI-545964;
-!- MASS SPECTROMETRY: Mass=23339.5; Method=MALDI; Range=2-206;
Evidence={ECO:0000269|PubMed:10094780};
-!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X02543; CAA26394.1; -; Genomic_DNA.
EMBL; U18997; AAA58094.1; -; Genomic_DNA.
EMBL; U00096; AAC76321.1; -; Genomic_DNA.
EMBL; AP009048; BAE77995.1; -; Genomic_DNA.
EMBL; V00353; CAA23645.1; -; Genomic_DNA.
EMBL; J01685; AAA24576.1; -; Genomic_DNA.
PIR; C23807; R3EC4.
RefSeq; NP_417755.1; NC_000913.3.
RefSeq; WP_000135224.1; NZ_LN832404.1.
PDB; 1EG0; EM; 11.50 A; A=43-200.
PDB; 1M5G; Model; -; D=2-206.
PDB; 2YKR; EM; 9.80 A; D=2-206.
PDB; 3J9Y; EM; 3.90 A; d=1-206.
PDB; 3J9Z; EM; 3.60 A; SD=2-206.
PDB; 3JA1; EM; 3.60 A; SD=2-206.
PDB; 3JBU; EM; 3.64 A; D=1-206.
PDB; 3JBV; EM; 3.32 A; D=1-206.
PDB; 3JCD; EM; 3.70 A; d=1-206.
PDB; 3JCE; EM; 3.20 A; d=1-206.
PDB; 3JCJ; EM; 3.70 A; l=1-206.
PDB; 3JCN; EM; 4.60 A; g=1-206.
PDB; 4A2I; EM; 16.50 A; D=2-206.
PDB; 4ADV; EM; 13.50 A; D=2-206.
PDB; 4U1U; X-ray; 2.95 A; AD/CD=2-206.
PDB; 4U1V; X-ray; 3.00 A; AD/CD=2-206.
PDB; 4U20; X-ray; 2.90 A; AD/CD=2-206.
PDB; 4U24; X-ray; 2.90 A; AD/CD=2-206.
PDB; 4U25; X-ray; 2.90 A; AD/CD=2-206.
PDB; 4U26; X-ray; 2.80 A; AD/CD=2-206.
PDB; 4U27; X-ray; 2.80 A; AD/CD=2-206.
PDB; 4V47; EM; 12.30 A; BD=2-206.
PDB; 4V48; EM; 11.50 A; BD=2-206.
PDB; 4V4H; X-ray; 3.46 A; AD/CD=1-206.
PDB; 4V4Q; X-ray; 3.46 A; AD/CD=2-206.
PDB; 4V4V; EM; 15.00 A; AD=3-206.
PDB; 4V4W; EM; 15.00 A; AD=3-206.
PDB; 4V50; X-ray; 3.22 A; AD/CD=2-206.
PDB; 4V52; X-ray; 3.21 A; AD/CD=2-206.
PDB; 4V53; X-ray; 3.54 A; AD/CD=2-206.
PDB; 4V54; X-ray; 3.30 A; AD/CD=2-206.
PDB; 4V55; X-ray; 4.00 A; AD/CD=2-206.
PDB; 4V56; X-ray; 3.93 A; AD/CD=2-206.
PDB; 4V57; X-ray; 3.50 A; AD/CD=2-206.
PDB; 4V5B; X-ray; 3.74 A; BD/DD=2-206.
PDB; 4V5H; EM; 5.80 A; AD=2-206.
PDB; 4V5Y; X-ray; 4.45 A; AD/CD=2-206.
PDB; 4V64; X-ray; 3.50 A; AD/CD=2-206.
PDB; 4V65; EM; 9.00 A; AR=1-206.
PDB; 4V66; EM; 9.00 A; AR=1-206.
PDB; 4V69; EM; 6.70 A; AD=2-206.
PDB; 4V6C; X-ray; 3.19 A; AD/CD=1-206.
PDB; 4V6D; X-ray; 3.81 A; AD/CD=1-206.
PDB; 4V6E; X-ray; 3.71 A; AD/CD=1-206.
PDB; 4V6K; EM; 8.25 A; BH=1-206.
PDB; 4V6L; EM; 13.20 A; AH=1-206.
PDB; 4V6M; EM; 7.10 A; AD=2-206.
PDB; 4V6N; EM; 12.10 A; BG=2-206.
PDB; 4V6O; EM; 14.70 A; AG=2-206.
PDB; 4V6P; EM; 13.50 A; AG=2-206.
PDB; 4V6Q; EM; 11.50 A; AG=2-206.
PDB; 4V6R; EM; 11.50 A; AG=2-206.
PDB; 4V6S; EM; 13.10 A; BF=2-206.
PDB; 4V6T; EM; 8.30 A; AD=2-206.
PDB; 4V6V; EM; 9.80 A; AD=2-206.
PDB; 4V6Y; EM; 12.00 A; AD=1-206.
PDB; 4V6Z; EM; 12.00 A; AD=1-206.
PDB; 4V70; EM; 17.00 A; AD=1-206.
PDB; 4V71; EM; 20.00 A; AD=1-206.
PDB; 4V72; EM; 13.00 A; AD=1-206.
PDB; 4V73; EM; 15.00 A; AD=1-206.
PDB; 4V74; EM; 17.00 A; AD=1-206.
PDB; 4V75; EM; 12.00 A; AD=1-206.
PDB; 4V76; EM; 17.00 A; AD=1-206.
PDB; 4V77; EM; 17.00 A; AD=1-206.
PDB; 4V78; EM; 20.00 A; AD=1-206.
PDB; 4V79; EM; 15.00 A; AD=1-206.
PDB; 4V7A; EM; 9.00 A; AD=1-206.
PDB; 4V7B; EM; 6.80 A; AD=1-206.
PDB; 4V7C; EM; 7.60 A; AD=2-206.
PDB; 4V7D; EM; 7.60 A; BD=2-206.
PDB; 4V7I; EM; 9.60 A; BD=1-206.
PDB; 4V7S; X-ray; 3.25 A; AD/CD=2-206.
PDB; 4V7T; X-ray; 3.19 A; AD/CD=2-206.
PDB; 4V7U; X-ray; 3.10 A; AD/CD=2-206.
PDB; 4V7V; X-ray; 3.29 A; AD/CD=2-206.
PDB; 4V85; X-ray; 3.20 A; AD=1-206.
PDB; 4V89; X-ray; 3.70 A; AD=1-206.
PDB; 4V9C; X-ray; 3.30 A; AD/CD=1-206.
PDB; 4V9D; X-ray; 3.00 A; AD/BD=2-206.
PDB; 4V9O; X-ray; 2.90 A; BD/DD/FD/HD=1-206.
PDB; 4V9P; X-ray; 2.90 A; BD/DD/FD/HD=1-206.
PDB; 4WF1; X-ray; 3.09 A; AD/CD=2-206.
PDB; 4WOI; X-ray; 3.00 A; AD/DD=1-206.
PDB; 4WWW; X-ray; 3.10 A; QD/XD=2-206.
PDB; 4YBB; X-ray; 2.10 A; AD/BD=2-206.
PDB; 5AFI; EM; 2.90 A; d=1-206.
PDB; 5H5U; EM; 3.00 A; k=2-206.
PDB; 5IQR; EM; 3.00 A; i=1-206.
PDB; 5IT8; X-ray; 3.12 A; AD/BD=2-206.
PDB; 5J5B; X-ray; 2.80 A; AD/BD=2-206.
PDB; 5J7L; X-ray; 3.00 A; AD/BD=2-206.
PDB; 5J88; X-ray; 3.32 A; AD/BD=2-206.
PDB; 5J8A; X-ray; 3.10 A; AD/BD=2-206.
PDB; 5J91; X-ray; 2.96 A; AD/BD=2-206.
PDB; 5JC9; X-ray; 3.03 A; AD/BD=2-206.
PDB; 5JTE; EM; 3.60 A; AD=1-206.
PDB; 5JU8; EM; 3.60 A; AD=1-206.
PDB; 5KCR; EM; 3.60 A; 1d=1-206.
PDB; 5KCS; EM; 3.90 A; 1d=1-206.
PDB; 5KPS; EM; 3.90 A; 9=1-206.
PDB; 5KPV; EM; 4.10 A; 8=1-206.
PDB; 5KPW; EM; 3.90 A; 8=1-206.
PDB; 5KPX; EM; 3.90 A; 8=1-206.
PDB; 5L3P; EM; 3.70 A; d=1-206.
PDB; 5LZA; EM; 3.60 A; d=2-206.
PDB; 5LZB; EM; 5.30 A; d=2-206.
PDB; 5LZC; EM; 4.80 A; d=2-206.
PDB; 5LZD; EM; 3.40 A; d=2-206.
PDB; 5LZE; EM; 3.50 A; d=2-206.
PDB; 5LZF; EM; 4.60 A; d=2-206.
PDB; 5MDV; EM; 2.97 A; i=1-206.
PDB; 5MDW; EM; 3.06 A; i=1-206.
PDB; 5MDY; EM; 3.35 A; i=1-206.
PDB; 5MDZ; EM; 3.10 A; i=1-206.
PDB; 5ME0; EM; 13.50 A; D=1-206.
PDB; 5ME1; EM; 13.50 A; D=1-206.
PDB; 5MGP; EM; 3.10 A; d=2-206.
PDB; 5MY1; EM; 7.60 A; D=2-206.
PDB; 5NO2; EM; 5.16 A; D=2-206.
PDB; 5NO3; EM; 5.16 A; D=2-206.
PDB; 5NO4; EM; 5.16 A; D=2-206.
PDB; 5NP6; EM; 3.60 A; G=2-206.
PDB; 5NWY; EM; 2.93 A; 3=1-206.
PDB; 5O2R; EM; 3.40 A; d=2-206.
PDB; 5U4I; EM; 3.50 A; d=1-206.
PDB; 5U4J; EM; 3.70 A; d=1-206.
PDB; 5U9F; EM; 3.20 A; D=1-206.
PDB; 5U9G; EM; 3.20 A; D=1-206.
PDB; 5UYK; EM; 3.90 A; D=2-206.
PDB; 5UYL; EM; 3.60 A; D=2-206.
PDB; 5UYM; EM; 3.20 A; D=2-206.
PDB; 5UYN; EM; 4.00 A; D=2-206.
PDB; 5UYP; EM; 3.90 A; D=2-206.
PDB; 5UYQ; EM; 3.80 A; D=2-206.
PDB; 5UZ4; EM; 5.80 A; D=1-206.
PDB; 5WDT; EM; 3.00 A; d=2-206.
PDB; 5WE4; EM; 3.10 A; d=2-206.
PDB; 5WE6; EM; 3.40 A; d=2-206.
PDB; 5WFK; EM; 3.40 A; d=2-206.
PDB; 6BU8; EM; 3.50 A; D=2-206.
PDB; 6C4I; EM; 3.24 A; d=1-206.
PDB; 6ENF; EM; 3.20 A; d=2-206.
PDB; 6ENJ; EM; 3.70 A; d=2-206.
PDB; 6ENU; EM; 3.10 A; d=2-206.
PDB; 6GWT; EM; 3.80 A; d=2-206.
PDB; 6GXM; EM; 3.80 A; d=2-206.
PDB; 6GXN; EM; 3.90 A; d=2-206.
PDB; 6GXO; EM; 3.90 A; d=2-206.
PDB; 6GXP; EM; 4.40 A; d=2-206.
PDB; 6H4N; EM; 3.00 A; d=2-206.
PDB; 6H58; EM; 7.90 A; d/dd=2-206.
PDBsum; 1EG0; -.
PDBsum; 1M5G; -.
PDBsum; 2YKR; -.
PDBsum; 3J9Y; -.
PDBsum; 3J9Z; -.
PDBsum; 3JA1; -.
PDBsum; 3JBU; -.
PDBsum; 3JBV; -.
PDBsum; 3JCD; -.
PDBsum; 3JCE; -.
PDBsum; 3JCJ; -.
PDBsum; 3JCN; -.
PDBsum; 4A2I; -.
PDBsum; 4ADV; -.
PDBsum; 4U1U; -.
PDBsum; 4U1V; -.
PDBsum; 4U20; -.
PDBsum; 4U24; -.
PDBsum; 4U25; -.
PDBsum; 4U26; -.
PDBsum; 4U27; -.
PDBsum; 4V47; -.
PDBsum; 4V48; -.
PDBsum; 4V4H; -.
PDBsum; 4V4Q; -.
PDBsum; 4V4V; -.
PDBsum; 4V4W; -.
PDBsum; 4V50; -.
PDBsum; 4V52; -.
PDBsum; 4V53; -.
PDBsum; 4V54; -.
PDBsum; 4V55; -.
PDBsum; 4V56; -.
PDBsum; 4V57; -.
PDBsum; 4V5B; -.
PDBsum; 4V5H; -.
PDBsum; 4V5Y; -.
PDBsum; 4V64; -.
PDBsum; 4V65; -.
PDBsum; 4V66; -.
PDBsum; 4V69; -.
PDBsum; 4V6C; -.
PDBsum; 4V6D; -.
PDBsum; 4V6E; -.
PDBsum; 4V6K; -.
PDBsum; 4V6L; -.
PDBsum; 4V6M; -.
PDBsum; 4V6N; -.
PDBsum; 4V6O; -.
PDBsum; 4V6P; -.
PDBsum; 4V6Q; -.
PDBsum; 4V6R; -.
PDBsum; 4V6S; -.
PDBsum; 4V6T; -.
PDBsum; 4V6V; -.
PDBsum; 4V6Y; -.
PDBsum; 4V6Z; -.
PDBsum; 4V70; -.
PDBsum; 4V71; -.
PDBsum; 4V72; -.
PDBsum; 4V73; -.
PDBsum; 4V74; -.
PDBsum; 4V75; -.
PDBsum; 4V76; -.
PDBsum; 4V77; -.
PDBsum; 4V78; -.
PDBsum; 4V79; -.
PDBsum; 4V7A; -.
PDBsum; 4V7B; -.
PDBsum; 4V7C; -.
PDBsum; 4V7D; -.
PDBsum; 4V7I; -.
PDBsum; 4V7S; -.
PDBsum; 4V7T; -.
PDBsum; 4V7U; -.
PDBsum; 4V7V; -.
PDBsum; 4V85; -.
PDBsum; 4V89; -.
PDBsum; 4V9C; -.
PDBsum; 4V9D; -.
PDBsum; 4V9O; -.
PDBsum; 4V9P; -.
PDBsum; 4WF1; -.
PDBsum; 4WOI; -.
PDBsum; 4WWW; -.
PDBsum; 4YBB; -.
PDBsum; 5AFI; -.
PDBsum; 5H5U; -.
PDBsum; 5IQR; -.
PDBsum; 5IT8; -.
PDBsum; 5J5B; -.
PDBsum; 5J7L; -.
PDBsum; 5J88; -.
PDBsum; 5J8A; -.
PDBsum; 5J91; -.
PDBsum; 5JC9; -.
PDBsum; 5JTE; -.
PDBsum; 5JU8; -.
PDBsum; 5KCR; -.
PDBsum; 5KCS; -.
PDBsum; 5KPS; -.
PDBsum; 5KPV; -.
PDBsum; 5KPW; -.
PDBsum; 5KPX; -.
PDBsum; 5L3P; -.
PDBsum; 5LZA; -.
PDBsum; 5LZB; -.
PDBsum; 5LZC; -.
PDBsum; 5LZD; -.
PDBsum; 5LZE; -.
PDBsum; 5LZF; -.
PDBsum; 5MDV; -.
PDBsum; 5MDW; -.
PDBsum; 5MDY; -.
PDBsum; 5MDZ; -.
PDBsum; 5ME0; -.
PDBsum; 5ME1; -.
PDBsum; 5MGP; -.
PDBsum; 5MY1; -.
PDBsum; 5NO2; -.
PDBsum; 5NO3; -.
PDBsum; 5NO4; -.
PDBsum; 5NP6; -.
PDBsum; 5NWY; -.
PDBsum; 5O2R; -.
PDBsum; 5U4I; -.
PDBsum; 5U4J; -.
PDBsum; 5U9F; -.
PDBsum; 5U9G; -.
PDBsum; 5UYK; -.
PDBsum; 5UYL; -.
PDBsum; 5UYM; -.
PDBsum; 5UYN; -.
PDBsum; 5UYP; -.
PDBsum; 5UYQ; -.
PDBsum; 5UZ4; -.
PDBsum; 5WDT; -.
PDBsum; 5WE4; -.
PDBsum; 5WE6; -.
PDBsum; 5WFK; -.
PDBsum; 6BU8; -.
PDBsum; 6C4I; -.
PDBsum; 6ENF; -.
PDBsum; 6ENJ; -.
PDBsum; 6ENU; -.
PDBsum; 6GWT; -.
PDBsum; 6GXM; -.
PDBsum; 6GXN; -.
PDBsum; 6GXO; -.
PDBsum; 6GXP; -.
PDBsum; 6H4N; -.
PDBsum; 6H58; -.
ProteinModelPortal; P0A7V8; -.
SMR; P0A7V8; -.
BioGrid; 852105; 1.
DIP; DIP-35794N; -.
IntAct; P0A7V8; 218.
MINT; P0A7V8; -.
STRING; 316385.ECDH10B_3471; -.
DrugBank; DB00453; Clomocycline.
DrugBank; DB00618; Demeclocycline.
DrugBank; DB00254; Doxycycline.
DrugBank; DB00256; Lymecycline.
DrugBank; DB01017; Minocycline.
DrugBank; DB00595; Oxytetracycline.
MoonProt; P0A7V8; -.
EPD; P0A7V8; -.
PaxDb; P0A7V8; -.
PRIDE; P0A7V8; -.
EnsemblBacteria; AAC76321; AAC76321; b3296.
EnsemblBacteria; BAE77995; BAE77995; BAE77995.
GeneID; 35807177; -.
GeneID; 947793; -.
KEGG; ecj:JW3258; -.
KEGG; eco:b3296; -.
PATRIC; fig|1411691.4.peg.3435; -.
EchoBASE; EB0896; -.
EcoGene; EG10903; rpsD.
eggNOG; ENOG4105G6W; Bacteria.
eggNOG; COG0522; LUCA.
HOGENOM; HOG000221003; -.
InParanoid; P0A7V8; -.
KO; K02986; -.
PhylomeDB; P0A7V8; -.
BioCyc; EcoCyc:EG10903-MONOMER; -.
BioCyc; MetaCyc:EG10903-MONOMER; -.
EvolutionaryTrace; P0A7V8; -.
PRO; PR:P0A7V8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:CAFA.
GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
GO; GO:0019843; F:rRNA binding; IDA:EcoliWiki.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0000900; F:translation repressor activity, mRNA regulatory element binding; IMP:EcoCyc.
GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
GO; GO:1990145; P:maintenance of translational fidelity; IMP:EcoCyc.
GO; GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
GO; GO:0031564; P:transcription antitermination; IDA:EcoCyc.
CDD; cd00165; S4; 1.
Gene3D; 3.10.290.10; -; 1.
HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
InterPro; IPR022801; Ribosomal_S4/S9.
InterPro; IPR001912; Ribosomal_S4/S9_N.
InterPro; IPR005709; Ribosomal_S4_bac-type.
InterPro; IPR018079; Ribosomal_S4_CS.
InterPro; IPR002942; S4_RNA-bd.
InterPro; IPR036986; S4_RNA-bd_sf.
PANTHER; PTHR11831; PTHR11831; 1.
PANTHER; PTHR11831:SF4; PTHR11831:SF4; 1.
Pfam; PF00163; Ribosomal_S4; 1.
Pfam; PF01479; S4; 1.
SMART; SM01390; Ribosomal_S4; 1.
SMART; SM00363; S4; 1.
TIGRFAMs; TIGR01017; rpsD_bact; 1.
PROSITE; PS00632; RIBOSOMAL_S4; 1.
PROSITE; PS50889; S4; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Reference proteome; Repressor;
Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
Transcription; Transcription regulation; Transcription termination;
Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1100394,
ECO:0000269|PubMed:4587210}.
CHAIN 2 206 30S ribosomal protein S4.
/FTId=PRO_0000132380.
DOMAIN 96 156 S4 RNA-binding.
VARIANT 51 51 Y -> D (in rpsD101; suppresses a
temperature-sensitive mutant of release
factor 1, R137P. Not a ram mutation).
VARIANT 170 206 Missing (in rpsD16; suppresses
streptomycin dependence in protein S12. A
ram mutation).
VARIANT 177 206 KMEGTFKRKPERSDLSADINEHLIVELYSK -> GRYV
(in rpsD12; suppresses streptomycin
dependence in protein S12. A ram
mutation).
VARIANT 179 206 EGTFKRKPERSDLSADINEHLIVELYSK -> ARYV (in
rpsD14; suppresses streptomycin
dependence in protein S12. A ram
mutation).
MUTAGEN 44 47 RKPR->AKPA: Decreases mRNA unwinding
ability of the ribosome.
{ECO:0000269|PubMed:15652481}.
CONFLICT 91 91 Missing (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 95 95 E -> Q (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 138 144 SPNDVVS -> DPNSVV (in Ref. 4; AA sequence
and 5; AA sequence). {ECO:0000305}.
CONFLICT 152 152 Q -> E (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 166 166 E -> Q (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
HELIX 9 15 {ECO:0000244|PDB:4U26}.
STRAND 20 22 {ECO:0000244|PDB:4V9O}.
STRAND 24 26 {ECO:0000244|PDB:4V9O}.
STRAND 28 32 {ECO:0000244|PDB:4U27}.
STRAND 34 36 {ECO:0000244|PDB:4U26}.
STRAND 38 41 {ECO:0000244|PDB:4U26}.
STRAND 42 44 {ECO:0000244|PDB:4V50}.
HELIX 50 65 {ECO:0000244|PDB:4U26}.
HELIX 69 81 {ECO:0000244|PDB:4U26}.
STRAND 82 84 {ECO:0000244|PDB:4U26}.
HELIX 86 95 {ECO:0000244|PDB:4U26}.
HELIX 98 104 {ECO:0000244|PDB:4U26}.
STRAND 107 110 {ECO:0000244|PDB:4U26}.
HELIX 111 119 {ECO:0000244|PDB:4U26}.
TURN 120 122 {ECO:0000244|PDB:4V6C}.
STRAND 124 129 {ECO:0000244|PDB:4U26}.
STRAND 132 134 {ECO:0000244|PDB:4V9C}.
STRAND 142 144 {ECO:0000244|PDB:4U26}.
TURN 147 151 {ECO:0000244|PDB:4U26}.
HELIX 153 164 {ECO:0000244|PDB:4U26}.
STRAND 169 172 {ECO:0000244|PDB:4U26}.
STRAND 175 177 {ECO:0000244|PDB:4U26}.
STRAND 179 182 {ECO:0000244|PDB:4U26}.
HELIX 188 190 {ECO:0000244|PDB:4U26}.
STRAND 193 195 {ECO:0000244|PDB:4V9C}.
HELIX 197 203 {ECO:0000244|PDB:4U26}.
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


Related products :

Catalog number Product name Quantity
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
29-214 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
29-215 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
29-216 RPL6 is a ribosomal protein that is a component of the 60S subunit. RPL6 belongs to the L6E family of ribosomal proteins. It is located in the cytoplasm. The protein can bind specifically to domain C 0.1 mg
26-118 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL39 is a 39S subunit protein. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes 0.05 mg
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
29-101 Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is 0.1 mg
29-221 RPL32 is a ribosomal protein that is a component of the 60S subunit. RPL32 belongs to the L32E family of ribosomal proteins. It is located in the cytoplasm. Although some studies have mapped this gene 0.1 mg
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
EIAAB35181 C15orf15,Homo sapiens,Human,My024,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,RPL24L,RSL24D1
EIAAB36079 40S ribosomal protein S2,40S ribosomal protein S4,Homo sapiens,Human,Protein LLRep3,RPS2,RPS4
18-783-75538 RABBIT ANTI RIBOSOMAL S6 KINASE 2 (C-TERMINAL) - RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; EC 2.7.11.1; S6K-alpha 2; 90 kDa ribosomal protein S6 kinase 2; p90-RSK 2; Ribosomal S6 kinase 3; RSK-3; pp90RSK3; 0.1 ml
EIAAB34981 60S ribosomal protein L22,EAP,EBER-associated protein,Epstein-Barr virus small RNA-associated protein,Heparin-binding protein HBp15,Homo sapiens,Human,RPL22
EIAAB33379 60S ribosomal protein L39 pseudogene 5,Homo sapiens,Human,Putative 60S ribosomal protein L39-like 5,RPL39P5
EIAAB35154 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Rat,Rattus norvegicus,Rplp0
EIAAB35158 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Homo sapiens,Human,RPLP0
EIAAB35156 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Mouse,Mus musculus,Rplp0
27-821 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
29-467 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
26-705 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
EIAAB35157 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Bos taurus,Bovine,RPLP0
EIAAB35108 60S ribosomal protein L1,60S ribosomal protein L4,Homo sapiens,Human,RPL1,RPL4
EIAAB35072 60S ribosomal protein L36a,60S ribosomal protein L44,Rat,Rattus norvegicus,Rpl36a,Rpl44


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur