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30S ribosomal protein S1 (Bacteriophage Q beta RNA-directed RNA polymerase subunit I) (Small ribosomal subunit protein bS1)

 RS1_ECOLI               Reviewed;         557 AA.
P0AG67; P02349; P77352;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
18-JUL-2018, entry version 116.
RecName: Full=30S ribosomal protein S1;
AltName: Full=Bacteriophage Q beta RNA-directed RNA polymerase subunit I {ECO:0000303|PubMed:816798};
AltName: Full=Small ribosomal subunit protein bS1 {ECO:0000303|PubMed:24524803};
Name=rpsA; Synonyms=ssyF; OrderedLocusNames=b0911, JW0894;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, AND SUBUNIT.
STRAIN=K12 / JS6.5, and MRE-600;
PubMed=7041110; DOI=10.1073/pnas.79.4.1008;
Schnier J., Kimura M., Foulaki K., Subramanian A.R., Isono K.,
Wittmann-Liebold B.;
"Primary structure of Escherichia coli ribosomal protein S1 and of its
gene rpsA.";
Proc. Natl. Acad. Sci. U.S.A. 79:1008-1011(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / JS6.5;
PubMed=6281725; DOI=10.1093/nar/10.6.1857;
Schnier J., Isono K.;
"The DNA sequence of the gene rpsA of Escherichia coli coding for
ribosomal protein S1.";
Nucleic Acids Res. 10:1857-1865(1982).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
PubMed=6384724; DOI=10.1007/BF00334105;
Pedersen S., Skouv J., Kajitani M., Ishihama A.;
"Transcriptional organization of the rpsA operon of Escherichia
coli.";
Mol. Gen. Genet. 196:135-140(1984).
[7]
PROTEIN SEQUENCE OF 1-6 AND 332-334, FUNCTION, SUBUNIT, AND DOMAIN.
STRAIN=MRE600;
PubMed=7003157; DOI=10.1016/0022-2836(80)90253-3;
Giorginis S., Subramanian A.R.;
"The major ribosome binding site of Escherichia coli ribosomal protein
S1 is located in its N-terminal segment.";
J. Mol. Biol. 141:393-408(1980).
[8]
PROTEIN SEQUENCE OF 118-128, AND IDENTIFICATION BY MASS SPECTROMETRY.
Bienvenut W.V., Barblan J., Quadroni M.;
Submitted (JAN-2004) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-557.
STRAIN=K12;
PubMed=3159903; DOI=10.1016/0022-2836(85)90206-2;
Flamm E., Weisberg R.A.;
"Primary structure of the hip gene of Escherichia coli and of its
product, the beta subunit of integration host factor.";
J. Mol. Biol. 183:117-128(1985).
[10]
PROTEIN SEQUENCE OF 1-11.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[11]
PROTEIN SEQUENCE OF 1-11.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[12]
FUNCTION, SUBUNIT, AND RNA-BINDING.
STRAIN=Q13;
PubMed=778845; DOI=10.1073/pnas.73.6.1824;
Bear D.G., Ng R., Van Derveer D., Johnson N.P., Thomas G.,
Schleich T., Noller H.F.;
"Alteration of polynucleotide secondary structure by ribosomal protein
S1.";
Proc. Natl. Acad. Sci. U.S.A. 73:1824-1828(1976).
[13]
FUNCTION IN QBETA VIRAL RNA REPLICATION, AND SUBUNIT.
PubMed=816798;
Carmichael G.G., Landers T.A., Weber K.;
"Immunochemical analysis of the functions of the subunits of phage
Qbeta ribonucleic acid replicase.";
J. Biol. Chem. 251:2744-2748(1976).
[14]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=MRE600;
PubMed=342903; DOI=10.1007/BF00455113;
Subramanian A.R., van Duin J.;
"Exchange of individual ribosomal proteins between ribosomes as
studied by heavy isotope-transfer experiments.";
Mol. Gen. Genet. 158:1-9(1977).
[15]
FUNCTION IN QBETA VIRAL RNA REPLICATION, SUBUNIT, AND DOMAIN.
PubMed=6358207;
Guerrier-Takada C., Subramanian A.R., Cole P.E.;
"The activity of discrete fragments of ribosomal protein S1 in Q beta
replicase function.";
J. Biol. Chem. 258:13649-13652(1983).
[16]
FUNCTION, INDUCTION, AND DOMAIN.
PubMed=2120211;
Skouv J., Schnier J., Rasmussen M.D., Subramanian A.R., Pedersen S.;
"Ribosomal protein S1 of Escherichia coli is the effector for the
regulation of its own synthesis.";
J. Biol. Chem. 265:17044-17049(1990).
[17]
FUNCTION, SUBUNIT, AND CROSS-LINKING TO MRNA.
PubMed=1712292;
Rinke-Appel J., Juenke N., Stade K., Brimacombe R.;
"The path of mRNA through the Escherichia coli ribosome; site-directed
cross-linking of mRNA analogues carrying a photo-reactive label at
various points 3' to the decoding site.";
EMBO J. 10:2195-2202(1991).
[18]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[19]
SUBUNIT, AND 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).
[20]
PHOSPHORYLATION, AND PROTEIN SEQUENCE OF 1-13.
PubMed=7783627; DOI=10.1111/j.1365-2958.1995.tb02270.x;
Freestone P., Grant S., Toth I., Norris V.;
"Identification of phosphoproteins in Escherichia coli.";
Mol. Microbiol. 15:573-580(1995).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9677288; DOI=10.1006/jmbi.1998.1909;
Sorensen M.A., Fricke J., Pedersen S.;
"Ribosomal protein S1 is required for translation of most, if not all,
natural mRNAs in Escherichia coli in vivo.";
J. Mol. Biol. 280:561-569(1998).
[22]
FUNCTION, AND TMRNA BINDING.
STRAIN=MRE600;
PubMed=11101533; DOI=10.1093/emboj/19.23.6612;
Wower I.K., Zwieb C.W., Guven S.A., Wower J.;
"Binding and cross-linking of tmRNA to ribosomal protein S1, on and
off the Escherichia coli ribosome.";
EMBO J. 19:6612-6621(2000).
[23]
FUNCTION, AND SUBUNIT.
PubMed=12068815; DOI=10.1046/j.1365-2958.2002.02971.x;
Moll I., Grill S., Gruendling A., Blaesi U.;
"Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEAD-box
helicase on translation of leaderless and canonical mRNAs in
Escherichia coli.";
Mol. Microbiol. 44:1387-1396(2002).
[24]
FUNCTION, DOMAIN, TMRNA BINDING, AND MRNA BINDING.
STRAIN=X90;
PubMed=15340139; DOI=10.1073/pnas.0405521101;
McGinness K.E., Sauer R.T.;
"Ribosomal protein S1 binds mRNA and tmRNA similarly but plays
distinct roles in translation of these molecules.";
Proc. Natl. Acad. Sci. U.S.A. 101:13454-13459(2004).
[25]
FUNCTION IN T4 VIRUS REGB ACTIVATION.
PubMed=17130171; DOI=10.1093/nar/gkl911;
Durand S., Richard G., Bisaglia M., Laalami S., Bontems F., Uzan M.;
"Activation of RegB endoribonuclease by S1 ribosomal protein requires
an 11 nt conserved sequence.";
Nucleic Acids Res. 34:6549-6560(2006).
[26]
LACK OF FUNCTION IN TRANS-TRANSLATION.
PubMed=17376482; DOI=10.1016/j.jmb.2007.02.068;
Qi H., Shimizu Y., Ueda T.;
"Ribosomal protein S1 is not essential for the trans-translation
machinery.";
J. Mol. Biol. 368:845-852(2007).
[27]
FUNCTION IN TRANS-TRANSLATION.
PubMed=17392345; DOI=10.1093/nar/gkm100;
Saguy M., Gillet R., Skorski P., Hermann-Le Denmat S., Felden B.;
"Ribosomal protein S1 influences trans-translation in vitro and in
vivo.";
Nucleic Acids Res. 35:2368-2376(2007).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229; LYS-279 AND LYS-363,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[29]
FUNCTION IN UNWINDING DSRNA, AND RNA-BINDING.
PubMed=22908248; DOI=10.1073/pnas.1208950109;
Qu X., Lancaster L., Noller H.F., Bustamante C., Tinoco I. Jr.;
"Ribosomal protein S1 unwinds double-stranded RNA in multiple steps.";
Proc. Natl. Acad. Sci. U.S.A. 109:14458-14463(2012).
[30]
FUNCTION IN QBETA VIRAL RNA REPLICATION, AND RNA-BINDING.
PubMed=23653193; DOI=10.1038/ncomms2807;
Vasilyev N.N., Kutlubaeva Z.S., Ugarov V.I., Chetverina H.V.,
Chetverin A.B.;
"Ribosomal protein S1 functions as a termination factor in RNA
synthesis by Qbeta phage replicase.";
Nat. Commun. 4:1781-1781(2013).
[31]
FUNCTION AS A RIBOSOME CHAPERONE, DOMAIN, AND MRNA-BINDING.
PubMed=24339747; DOI=10.1371/journal.pbio.1001731;
Duval M., Korepanov A., Fuchsbauer O., Fechter P., Haller A.,
Fabbretti A., Choulier L., Micura R., Klaholz B.P., Romby P.,
Springer M., Marzi S.;
"Escherichia coli ribosomal protein S1 unfolds structured mRNAs onto
the ribosome for active translation initiation.";
PLoS Biol. 11:E1001731-E1001731(2013).
[32]
REVIEW.
PubMed=22370051; DOI=10.1016/j.biochi.2012.02.010;
Hajnsdorf E., Boni I.V.;
"Multiple activities of RNA-binding proteins S1 and Hfq.";
Biochimie 94:1544-1553(2012).
[33]
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).
[34]
POSITION BY CRYO-ELECTRON MICROSCOPY, AND SUBUNIT.
PubMed=11593008; DOI=10.1073/pnas.211266898;
Sengupta J., Agrawal R.K., Frank J.;
"Visualization of protein S1 within the 30S ribosomal subunit and its
interaction with messenger RNA.";
Proc. Natl. Acad. Sci. U.S.A. 98:11991-11996(2001).
[35]
STRUCTURE BY NMR OF 267-361 AND OF 441-528, AND RNA-BINDING.
PubMed=19605565; DOI=10.1093/nar/gkp547;
Salah P., Bisaglia M., Aliprandi P., Uzan M., Sizun C., Bontems F.;
"Probing the relationship between Gram-negative and Gram-positive S1
proteins by sequence analysis.";
Nucleic Acids Res. 37:5578-5588(2009).
[36]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-273 IN QBETA VIRUS RNA
POLYMERASE, FUNCTION IN VIRAL RNA REPLICATION, SUBUNIT, DOMAIN,
RNA-BINDING, AND MUTAGENESIS OF TYR-205; PHE-208; HIS-219 AND ARG-254.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=25122749; DOI=10.1093/nar/gku745;
Takeshita D., Yamashita S., Tomita K.;
"Molecular insights into replication initiation by Qbeta replicase
using ribosomal protein S1.";
Nucleic Acids Res. 42:10809-10822(2014).
-!- FUNCTION: Required for translation of most natural mRNAs except
for leaderless mRNA (PubMed:9677288, PubMed:7003157,
PubMed:12068815, PubMed:17376482, PubMed:24339747). Binds mRNA
upstream of the Shine-Dalgarno (SD) sequence and helps it bind to
the 30S ribosomal subunit; acts as an RNA chaperone to unfold
structured mRNA on the ribosome but is not essential for mRNAs
with strong SDs and little 5'-UTR structure, thus it may help
fine-tune which mRNAs that are translated (PubMed:24339747).
Unwinds dsRNA by binding to transiently formed ssRNA regions;
binds about 10 nucleotides (PubMed:22908248). Has a preference for
polypyrimidine tracts (PubMed:778845). Negatively autoregulates
its own translation (PubMed:2120211).
{ECO:0000269|PubMed:12068815, ECO:0000269|PubMed:15340139,
ECO:0000269|PubMed:1712292, ECO:0000269|PubMed:17376482,
ECO:0000269|PubMed:2120211, ECO:0000269|PubMed:22908248,
ECO:0000269|PubMed:24339747, ECO:0000269|PubMed:7003157,
ECO:0000269|PubMed:778845, ECO:0000269|PubMed:9677288}.
-!- FUNCTION: It is not clear if it plays a role in trans-translation
(a process which rescues stalled ribosomes). Evidence for its
role; binds to tmRNA with very high affinity, is required for
binding of tmRNA to 30S subunit (PubMed:11101533,
PubMed:15340139). Thought to play a role only in translation of
the tmRNA in vitro (PubMed:17392345). Evidence against its role;
overexpression of whole protein or various S1 fragments inhibits
translation, they have no effect on trans-translation, and an in
vitro system with S1-less ribosomes performs trans-translation
(PubMed:15340139, PubMed:17376482). In trans-translation Ala-
aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA
gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a
short internal open reading frame (the tag peptide)) acts like a
tRNA, entering the A-site of the ribosome and displacing the
stalled mRNA (which is subsequently degraded). The ribosome then
switches to translate the ORF on the tmRNA, the nascent peptide is
terminated with the "tag peptide" encoded by the tmRNA and thus
targeted for degradation. {ECO:0000269|PubMed:11101533,
ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:17376482,
ECO:0000269|PubMed:17392345}.
-!- FUNCTION: In case of infection by bacteriophage Qbeta, part of the
viral RNA-dependent RNA polymerase complex; this subunit is
required for RNA replication initiation activity during synthesis
of (-) strand RNA from the (+) strand genomic RNA but not for (+)
strand synthesis from the (-) strand (PubMed:6358207,
PubMed:25122749). Binds an approximately 70 mucleotide RNA
internal to the viral replicase gene (the M-site)
(PubMed:25122749). Others have reported it is not involved in RNA
replication initiation but rather in termination of RNA synthesis
and is required for termination whether it is the (+) or (-)
strand that is being synthesized (PubMed:23653193).
{ECO:0000269|PubMed:23653193, ECO:0000269|PubMed:25122749,
ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:816798}.
-!- FUNCTION: In case of infection by bacteriophage T4, plays a
significant role in substrate choice by viral endoribonuclease
RegB. {ECO:0000269|PubMed:17130171}.
-!- SUBUNIT: Part of the 30S ribosomal subunit; the largest protein
subunit, it is loosely associated and rarely found in ribosomal
crystal structures (PubMed:7041110, PubMed:7003157, PubMed:778845,
PubMed:342903). Does not bind rRNA. Probably requires ribosomal
protein S2 to associate with the 30S subunit (PubMed:12068815).
Binds in the junction of the head, platform and main body of the
30S subunit; the N-terminus penetrates the 30S subunit while the
C-terminus faces ribosomal protein S2 (PubMed:11593008). Nascent
polypeptide chains cross-link this protein in situ
(PubMed:9716382). Can be cross-linked to mRNA in the ribosome
(PubMed:1712292). In case of infection by bacteriophage Qbeta,
part of the viral RNA-dependent RNA polymerase complex, the other
subunits are the viral replicase catalytic subunit (AC P14647),
host EF-Tu and EF-Ts (PubMed:816798, PubMed:6358207,
PubMed:25122749). {ECO:0000269|PubMed:11593008,
ECO:0000269|PubMed:12068815, ECO:0000269|PubMed:1712292,
ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:342903,
ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:7003157,
ECO:0000269|PubMed:7041110, ECO:0000269|PubMed:778845,
ECO:0000269|PubMed:816798, ECO:0000269|PubMed:9716382}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-546520, EBI-546520;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:342903}.
-!- INDUCTION: Represses its own translation via the N-terminus (at
protein level). {ECO:0000269|PubMed:2120211}.
-!- DOMAIN: The 6 S1 motif domains are not equivalent; the first 2 no
longer bind rRNA but instead are involved in protein-ribosome and
protein-protein interactions. Binds to the 30S ribosomal subunit
via its N-terminal fragment (190 residues, the first 2 S1 motifs)
and allows translation by S1-free ribosomes (PubMed:7003157,
PubMed:15340139). The same fragment represses its own translation
(PubMed:2120211). The first 3 S1 motifs do however bind to mRNA
pseudoknots in the 5'-UTR of at least 1 mRNA (rpsO); deletion of
S1 motifs 1-3 but not motifs 4-6 is not viable, although a
deletion of motifs 4-6 grows slowly and is cold-sensitive
(PubMed:24339747). In case of infection by bacteriophage Qbeta the
same N-terminal fragment is necessary and sufficient to form the
Qbeta virus RNA-dependent RNA polymerase, although in vitro (-)
strand RNA synthesis from the (+) strand genomic RNA also requires
the third S1 motif (residues 1-273) (PubMed:6358207,
PubMed:25122749). The third S1 motif is required to bind mRNA,
tmRNA and viral M-site RNA but requires cooperation with other S1
motifs (PubMed:15340139, PubMed:25122749).
{ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:2120211,
ECO:0000269|PubMed:24339747, ECO:0000269|PubMed:25122749,
ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:7003157}.
-!- PTM: Phosphorylated; probably on a serine.
{ECO:0000269|PubMed:7783627}.
-!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. Upon
depletion cell growth and total protein synthesis become linear.
{ECO:0000269|PubMed:9677288}.
-!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
{ECO:0000305}.
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EMBL; V00342; CAA23630.1; -; Genomic_DNA.
EMBL; V00352; CAA23644.1; -; Genomic_DNA.
EMBL; U00096; AAC73997.1; -; Genomic_DNA.
EMBL; AP009048; BAA35655.1; -; Genomic_DNA.
EMBL; X00785; CAA25361.1; -; Genomic_DNA.
EMBL; X04864; CAA28556.1; -; Genomic_DNA.
PIR; F64830; R3EC1.
RefSeq; NP_415431.1; NC_000913.3.
RefSeq; WP_000140327.1; NZ_LN832404.1.
PDB; 2BH8; X-ray; 1.90 A; A/B=364-398.
PDB; 2KHI; NMR; -; A=267-361.
PDB; 2KHJ; NMR; -; A=441-528.
PDB; 4Q7J; X-ray; 2.90 A; D/H=1-273.
PDB; 4R71; X-ray; 3.21 A; E/F=2-171.
PDB; 5XQ5; NMR; -; A=350-443.
PDB; 6BU8; EM; 3.50 A; Z=4-557.
PDBsum; 2BH8; -.
PDBsum; 2KHI; -.
PDBsum; 2KHJ; -.
PDBsum; 4Q7J; -.
PDBsum; 4R71; -.
PDBsum; 5XQ5; -.
PDBsum; 6BU8; -.
ProteinModelPortal; P0AG67; -.
SMR; P0AG67; -.
BioGrid; 4263060; 171.
BioGrid; 849910; 1.
DIP; DIP-35884N; -.
IntAct; P0AG67; 85.
MINT; P0AG67; -.
STRING; 316385.ECDH10B_0981; -.
CarbonylDB; P0AG67; -.
iPTMnet; P0AG67; -.
SWISS-2DPAGE; P0AG67; -.
EPD; P0AG67; -.
PaxDb; P0AG67; -.
PRIDE; P0AG67; -.
EnsemblBacteria; AAC73997; AAC73997; b0911.
EnsemblBacteria; BAA35655; BAA35655; BAA35655.
GeneID; 945536; -.
KEGG; ecj:JW0894; -.
KEGG; eco:b0911; -.
PATRIC; fig|1411691.4.peg.1365; -.
EchoBASE; EB0893; -.
EcoGene; EG10900; rpsA.
eggNOG; ENOG4105CAV; Bacteria.
eggNOG; COG0539; LUCA.
HOGENOM; HOG000044052; -.
InParanoid; P0AG67; -.
KO; K02945; -.
OMA; SLNEFRY; -.
PhylomeDB; P0AG67; -.
BioCyc; EcoCyc:EG10900-MONOMER; -.
BioCyc; MetaCyc:EG10900-MONOMER; -.
EvolutionaryTrace; P0AG67; -.
PRO; PR:P0AG67; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:CAFA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:EcoCyc.
GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
GO; GO:0006412; P:translation; IMP:EcoCyc.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR000110; Ribosomal_S1.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
Pfam; PF00575; S1; 6.
PIRSF; PIRSF002111; RpsA; 1.
SMART; SM00316; S1; 6.
SUPFAM; SSF50249; SSF50249; 6.
TIGRFAMs; TIGR00717; rpsA; 1.
PROSITE; PS50126; S1; 6.
1: Evidence at protein level;
3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding.
CHAIN 1 557 30S ribosomal protein S1.
/FTId=PRO_0000196033.
DOMAIN 21 87 S1 motif 1. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 105 171 S1 motif 2. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 192 260 S1 motif 3. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 277 347 S1 motif 4. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 364 434 S1 motif 5. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
DOMAIN 451 520 S1 motif 6. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
MOD_RES 229 229 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 363 363 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MUTAGEN 205 205 Y->A: Decreased binding of Q beta-derived
M-site RNA, 80% synthesis of (-) strand
RNA, in construct expressing residues 1-
273. {ECO:0000269|PubMed:25122749}.
MUTAGEN 208 208 F->A: Decreased binding of Q beta-derived
M-site RNA, 50% synthesis of (-) strand
RNA, in construct expressing residues 1-
273. {ECO:0000269|PubMed:25122749}.
MUTAGEN 219 219 H->A: Decreased binding of Q beta-derived
M-site RNA, 40% synthesis of (-) strand
RNA, in construct expressing residues 1-
273. {ECO:0000269|PubMed:25122749}.
MUTAGEN 254 254 R->A: Decreased binding of Q beta-derived
M-site RNA, 40% synthesis of (-) strand
RNA, in construct expressing residues 1-
273. {ECO:0000269|PubMed:25122749}.
CONFLICT 125 125 N -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 181 182 ER -> D (in Ref. 1; CAA23630 and 2;
CAA23644). {ECO:0000305}.
HELIX 4 18 {ECO:0000244|PDB:4Q7J}.
STRAND 21 31 {ECO:0000244|PDB:4Q7J}.
STRAND 36 39 {ECO:0000244|PDB:4Q7J}.
STRAND 41 44 {ECO:0000244|PDB:4Q7J}.
STRAND 46 48 {ECO:0000244|PDB:4Q7J}.
STRAND 53 56 {ECO:0000244|PDB:4Q7J}.
TURN 59 61 {ECO:0000244|PDB:4Q7J}.
STRAND 67 71 {ECO:0000244|PDB:4Q7J}.
HELIX 79 82 {ECO:0000244|PDB:4Q7J}.
HELIX 85 101 {ECO:0000244|PDB:4Q7J}.
TURN 102 105 {ECO:0000244|PDB:4Q7J}.
STRAND 107 115 {ECO:0000244|PDB:4Q7J}.
STRAND 117 124 {ECO:0000244|PDB:4Q7J}.
STRAND 127 133 {ECO:0000244|PDB:4Q7J}.
HELIX 143 145 {ECO:0000244|PDB:4Q7J}.
TURN 147 149 {ECO:0000244|PDB:4R71}.
STRAND 151 159 {ECO:0000244|PDB:4Q7J}.
STRAND 161 163 {ECO:0000244|PDB:4Q7J}.
STRAND 166 170 {ECO:0000244|PDB:4Q7J}.
HELIX 171 175 {ECO:0000244|PDB:4Q7J}.
STRAND 279 288 {ECO:0000244|PDB:2KHI}.
STRAND 291 295 {ECO:0000244|PDB:2KHI}.
STRAND 301 305 {ECO:0000244|PDB:2KHI}.
STRAND 308 310 {ECO:0000244|PDB:2KHI}.
TURN 319 321 {ECO:0000244|PDB:2KHI}.
STRAND 327 333 {ECO:0000244|PDB:2KHI}.
TURN 337 339 {ECO:0000244|PDB:2KHI}.
HELIX 441 444 {ECO:0000244|PDB:2KHJ}.
TURN 445 447 {ECO:0000244|PDB:2KHJ}.
STRAND 450 461 {ECO:0000244|PDB:2KHJ}.
STRAND 466 469 {ECO:0000244|PDB:2KHJ}.
STRAND 485 490 {ECO:0000244|PDB:2KHJ}.
HELIX 491 493 {ECO:0000244|PDB:2KHJ}.
STRAND 500 509 {ECO:0000244|PDB:2KHJ}.
TURN 510 513 {ECO:0000244|PDB:2KHJ}.
STRAND 514 518 {ECO:0000244|PDB:2KHJ}.
STRAND 521 524 {ECO:0000244|PDB:2KHJ}.
SEQUENCE 557 AA; 61158 MW; 0ABCDEB9E510C267 CRC64;
MTESFAQLFE ESLKEIETRP GSIVRGVVVA IDKDVVLVDA GLKSESAIPA EQFKNAQGEL
EIQVGDEVDV ALDAVEDGFG ETLLSREKAK RHEAWITLEK AYEDAETVTG VINGKVKGGF
TVELNGIRAF LPGSLVDVRP VRDTLHLEGK ELEFKVIKLD QKRNNVVVSR RAVIESENSA
ERDQLLENLQ EGMEVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE
ITVKVLKFDR ERTRVSLGLK QLGEDPWVAI AKRYPEGTKL TGRVTNLTDY GCFVEIEEGV
EGLVHVSEMD WTNKNIHPSK VVNVGDVVEV MVLDIDEERR RISLGLKQCK ANPWQQFAET
HNKGDRVEGK IKSITDFGIF IGLDGGIDGL VHLSDISWNV AGEEAVREYK KGDEIAAVVL
QVDAERERIS LGVKQLAEDP FNNWVALNKK GAIVTGKVTA VDAKGATVEL ADGVEGYLRA
SEASRDRVED ATLVLSVGDE VEAKFTGVDR KNRAISLSVR AKDEADEKDA IATVNKQEDA
NFSNNAMAEA FKAAKGE


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