RS1_ECOLI
ID RS1_ECOLI Reviewed; 557 AA.
AC P0AG67; P02349; P77352;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=30S ribosomal protein S1;
DE AltName: Full=Bacteriophage Q beta RNA-directed RNA polymerase subunit I {ECO:0000303|PubMed:816798};
DE AltName: Full=Small ribosomal subunit protein bS1 {ECO:0000303|PubMed:24524803};
GN Name=rpsA; Synonyms=ssyF; OrderedLocusNames=b0911, JW0894;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, AND SUBUNIT.
RC STRAIN=K12 / JS6.5, and MRE-600;
RX PubMed=7041110; DOI=10.1073/pnas.79.4.1008;
RA Schnier J., Kimura M., Foulaki K., Subramanian A.R., Isono K.,
RA Wittmann-Liebold B.;
RT "Primary structure of Escherichia coli ribosomal protein S1 and of its gene
RT rpsA.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1008-1011(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JS6.5;
RX PubMed=6281725; DOI=10.1093/nar/10.6.1857;
RA Schnier J., Isono K.;
RT "The DNA sequence of the gene rpsA of Escherichia coli coding for ribosomal
RT protein S1.";
RL Nucleic Acids Res. 10:1857-1865(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=6384724; DOI=10.1007/bf00334105;
RA Pedersen S., Skouv J., Kajitani M., Ishihama A.;
RT "Transcriptional organization of the rpsA operon of Escherichia coli.";
RL Mol. Gen. Genet. 196:135-140(1984).
RN [7]
RP PROTEIN SEQUENCE OF 1-6 AND 332-334, FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=MRE600;
RX PubMed=7003157; DOI=10.1016/0022-2836(80)90253-3;
RA Giorginis S., Subramanian A.R.;
RT "The major ribosome binding site of Escherichia coli ribosomal protein S1
RT is located in its N-terminal segment.";
RL J. Mol. Biol. 141:393-408(1980).
RN [8]
RP PROTEIN SEQUENCE OF 118-128, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Barblan J., Quadroni M.;
RL Submitted (JAN-2004) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-557.
RC STRAIN=K12;
RX PubMed=3159903; DOI=10.1016/0022-2836(85)90206-2;
RA Flamm E., Weisberg R.A.;
RT "Primary structure of the hip gene of Escherichia coli and of its product,
RT the beta subunit of integration host factor.";
RL J. Mol. Biol. 183:117-128(1985).
RN [10]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [11]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [12]
RP FUNCTION, SUBUNIT, AND RNA-BINDING.
RC STRAIN=Q13;
RX PubMed=778845; DOI=10.1073/pnas.73.6.1824;
RA Bear D.G., Ng R., Van Derveer D., Johnson N.P., Thomas G., Schleich T.,
RA Noller H.F.;
RT "Alteration of polynucleotide secondary structure by ribosomal protein
RT S1.";
RL Proc. Natl. Acad. Sci. U.S.A. 73:1824-1828(1976).
RN [13]
RP FUNCTION IN QBETA VIRAL RNA REPLICATION, AND SUBUNIT.
RX PubMed=816798; DOI=10.1016/s0021-9258(17)33551-2;
RA Carmichael G.G., Landers T.A., Weber K.;
RT "Immunochemical analysis of the functions of the subunits of phage Qbeta
RT ribonucleic acid replicase.";
RL J. Biol. Chem. 251:2744-2748(1976).
RN [14]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=MRE600;
RX PubMed=342903; DOI=10.1007/bf00455113;
RA Subramanian A.R., van Duin J.;
RT "Exchange of individual ribosomal proteins between ribosomes as studied by
RT heavy isotope-transfer experiments.";
RL Mol. Gen. Genet. 158:1-9(1977).
RN [15]
RP FUNCTION IN QBETA VIRAL RNA REPLICATION, SUBUNIT, AND DOMAIN.
RX PubMed=6358207; DOI=10.1016/s0021-9258(17)43965-2;
RA Guerrier-Takada C., Subramanian A.R., Cole P.E.;
RT "The activity of discrete fragments of ribosomal protein S1 in Q beta
RT replicase function.";
RL J. Biol. Chem. 258:13649-13652(1983).
RN [16]
RP FUNCTION, INDUCTION, AND DOMAIN.
RX PubMed=2120211; DOI=10.1016/s0021-9258(17)44866-6;
RA Skouv J., Schnier J., Rasmussen M.D., Subramanian A.R., Pedersen S.;
RT "Ribosomal protein S1 of Escherichia coli is the effector for the
RT regulation of its own synthesis.";
RL J. Biol. Chem. 265:17044-17049(1990).
RN [17]
RP FUNCTION, SUBUNIT, AND CROSS-LINKING TO MRNA.
RX PubMed=1712292; DOI=10.1002/j.1460-2075.1991.tb07755.x;
RA Rinke-Appel J., Juenke N., Stade K., Brimacombe R.;
RT "The path of mRNA through the Escherichia coli ribosome; site-directed
RT cross-linking of mRNA analogues carrying a photo-reactive label at various
RT points 3' to the decoding site.";
RL EMBO J. 10:2195-2202(1991).
RN [18]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [19]
RP SUBUNIT, AND 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 [20]
RP PHOSPHORYLATION, AND PROTEIN SEQUENCE OF 1-13.
RC STRAIN=E2348/69 / EPEC / MAR001;
RX PubMed=7783627; DOI=10.1111/j.1365-2958.1995.tb02270.x;
RA Freestone P., Grant S., Toth I., Norris V.;
RT "Identification of phosphoproteins in Escherichia coli.";
RL Mol. Microbiol. 15:573-580(1995).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9677288; DOI=10.1006/jmbi.1998.1909;
RA Sorensen M.A., Fricke J., Pedersen S.;
RT "Ribosomal protein S1 is required for translation of most, if not all,
RT natural mRNAs in Escherichia coli in vivo.";
RL J. Mol. Biol. 280:561-569(1998).
RN [22]
RP FUNCTION, AND TMRNA BINDING.
RC STRAIN=MRE600;
RX PubMed=11101533; DOI=10.1093/emboj/19.23.6612;
RA Wower I.K., Zwieb C.W., Guven S.A., Wower J.;
RT "Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the
RT Escherichia coli ribosome.";
RL EMBO J. 19:6612-6621(2000).
RN [23]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12068815; DOI=10.1046/j.1365-2958.2002.02971.x;
RA Moll I., Grill S., Gruendling A., Blaesi U.;
RT "Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEAD-box helicase
RT on translation of leaderless and canonical mRNAs in Escherichia coli.";
RL Mol. Microbiol. 44:1387-1396(2002).
RN [24]
RP FUNCTION, DOMAIN, TMRNA BINDING, AND MRNA BINDING.
RC STRAIN=X90;
RX PubMed=15340139; DOI=10.1073/pnas.0405521101;
RA McGinness K.E., Sauer R.T.;
RT "Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct
RT roles in translation of these molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13454-13459(2004).
RN [25]
RP FUNCTION IN T4 VIRUS REGB ACTIVATION.
RX PubMed=17130171; DOI=10.1093/nar/gkl911;
RA Durand S., Richard G., Bisaglia M., Laalami S., Bontems F., Uzan M.;
RT "Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11
RT nt conserved sequence.";
RL Nucleic Acids Res. 34:6549-6560(2006).
RN [26]
RP LACK OF FUNCTION IN TRANS-TRANSLATION.
RX PubMed=17376482; DOI=10.1016/j.jmb.2007.02.068;
RA Qi H., Shimizu Y., Ueda T.;
RT "Ribosomal protein S1 is not essential for the trans-translation
RT machinery.";
RL J. Mol. Biol. 368:845-852(2007).
RN [27]
RP FUNCTION IN TRANS-TRANSLATION.
RX PubMed=17392345; DOI=10.1093/nar/gkm100;
RA Saguy M., Gillet R., Skorski P., Hermann-Le Denmat S., Felden B.;
RT "Ribosomal protein S1 influences trans-translation in vitro and in vivo.";
RL Nucleic Acids Res. 35:2368-2376(2007).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229; LYS-279 AND LYS-363, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [29]
RP FUNCTION IN UNWINDING DSRNA, AND RNA-BINDING.
RX PubMed=22908248; DOI=10.1073/pnas.1208950109;
RA Qu X., Lancaster L., Noller H.F., Bustamante C., Tinoco I. Jr.;
RT "Ribosomal protein S1 unwinds double-stranded RNA in multiple steps.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14458-14463(2012).
RN [30]
RP FUNCTION IN QBETA VIRAL RNA REPLICATION, AND RNA-BINDING.
RX PubMed=23653193; DOI=10.1038/ncomms2807;
RA Vasilyev N.N., Kutlubaeva Z.S., Ugarov V.I., Chetverina H.V.,
RA Chetverin A.B.;
RT "Ribosomal protein S1 functions as a termination factor in RNA synthesis by
RT Qbeta phage replicase.";
RL Nat. Commun. 4:1781-1781(2013).
RN [31]
RP FUNCTION AS A RIBOSOME CHAPERONE, DOMAIN, AND MRNA-BINDING.
RX PubMed=24339747; DOI=10.1371/journal.pbio.1001731;
RA Duval M., Korepanov A., Fuchsbauer O., Fechter P., Haller A., Fabbretti A.,
RA Choulier L., Micura R., Klaholz B.P., Romby P., Springer M., Marzi S.;
RT "Escherichia coli ribosomal protein S1 unfolds structured mRNAs onto the
RT ribosome for active translation initiation.";
RL PLoS Biol. 11:E1001731-E1001731(2013).
RN [32]
RP REVIEW.
RX PubMed=22370051; DOI=10.1016/j.biochi.2012.02.010;
RA Hajnsdorf E., Boni I.V.;
RT "Multiple activities of RNA-binding proteins S1 and Hfq.";
RL Biochimie 94:1544-1553(2012).
RN [33]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [34]
RP POSITION BY CRYO-ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=11593008; DOI=10.1073/pnas.211266898;
RA Sengupta J., Agrawal R.K., Frank J.;
RT "Visualization of protein S1 within the 30S ribosomal subunit and its
RT interaction with messenger RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11991-11996(2001).
RN [35]
RP STRUCTURE BY NMR OF 267-361 AND OF 441-528, AND RNA-BINDING.
RX PubMed=19605565; DOI=10.1093/nar/gkp547;
RA Salah P., Bisaglia M., Aliprandi P., Uzan M., Sizun C., Bontems F.;
RT "Probing the relationship between Gram-negative and Gram-positive S1
RT proteins by sequence analysis.";
RL Nucleic Acids Res. 37:5578-5588(2009).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-273 IN QBETA VIRUS RNA
RP POLYMERASE, FUNCTION IN VIRAL RNA REPLICATION, SUBUNIT, DOMAIN,
RP RNA-BINDING, AND MUTAGENESIS OF TYR-205; PHE-208; HIS-219 AND ARG-254.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=25122749; DOI=10.1093/nar/gku745;
RA Takeshita D., Yamashita S., Tomita K.;
RT "Molecular insights into replication initiation by Qbeta replicase using
RT ribosomal protein S1.";
RL Nucleic Acids Res. 42:10809-10822(2014).
CC -!- FUNCTION: Required for translation of most natural mRNAs except for
CC leaderless mRNA (PubMed:9677288, PubMed:7003157, PubMed:12068815,
CC PubMed:17376482, PubMed:24339747). Binds mRNA upstream of the Shine-
CC Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit;
CC acts as an RNA chaperone to unfold structured mRNA on the ribosome but
CC is not essential for mRNAs with strong SDs and little 5'-UTR structure,
CC thus it may help fine-tune which mRNAs that are translated
CC (PubMed:24339747). Unwinds dsRNA by binding to transiently formed ssRNA
CC regions; binds about 10 nucleotides (PubMed:22908248). Has a preference
CC for polypyrimidine tracts (PubMed:778845). Negatively autoregulates its
CC own translation (PubMed:2120211). {ECO:0000269|PubMed:12068815,
CC ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:1712292,
CC ECO:0000269|PubMed:17376482, ECO:0000269|PubMed:2120211,
CC ECO:0000269|PubMed:22908248, ECO:0000269|PubMed:24339747,
CC ECO:0000269|PubMed:7003157, ECO:0000269|PubMed:778845,
CC ECO:0000269|PubMed:9677288}.
CC -!- FUNCTION: It is not clear if it plays a role in trans-translation (a
CC process which rescues stalled ribosomes). Evidence for its role; binds
CC to tmRNA with very high affinity, is required for binding of tmRNA to
CC 30S subunit (PubMed:11101533, PubMed:15340139). Thought to play a role
CC only in translation of the tmRNA in vitro (PubMed:17392345). Evidence
CC against its role; overexpression of whole protein or various S1
CC fragments inhibits translation, they have no effect on trans-
CC translation, and an in vitro system with S1-less ribosomes performs
CC trans-translation (PubMed:15340139, PubMed:17376482). In trans-
CC translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of
CC the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it
CC encodes a short internal open reading frame (the tag peptide)) acts
CC like a tRNA, entering the A-site of the ribosome and displacing the
CC stalled mRNA (which is subsequently degraded). The ribosome then
CC switches to translate the ORF on the tmRNA, the nascent peptide is
CC terminated with the 'tag peptide' encoded by the tmRNA and thus
CC targeted for degradation. {ECO:0000269|PubMed:11101533,
CC ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:17376482,
CC ECO:0000269|PubMed:17392345}.
CC -!- FUNCTION: In case of infection by bacteriophage Qbeta, part of the
CC viral RNA-dependent RNA polymerase complex; this subunit is required
CC for RNA replication initiation activity during synthesis of (-) strand
CC RNA from the (+) strand genomic RNA but not for (+) strand synthesis
CC from the (-) strand (PubMed:6358207, PubMed:25122749). Binds an
CC approximately 70 nucleotide RNA internal to the viral replicase gene
CC (the M-site) (PubMed:25122749). Others have reported it is not involved
CC in RNA replication initiation but rather in termination of RNA
CC synthesis and is required for termination whether it is the (+) or (-)
CC strand that is being synthesized (PubMed:23653193).
CC {ECO:0000269|PubMed:23653193, ECO:0000269|PubMed:25122749,
CC ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:816798}.
CC -!- FUNCTION: In case of infection by bacteriophage T4, plays a significant
CC role in substrate choice by viral endoribonuclease RegB.
CC {ECO:0000269|PubMed:17130171}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit; the largest protein
CC subunit, it is loosely associated and rarely found in ribosomal crystal
CC structures (PubMed:7041110, PubMed:7003157, PubMed:778845,
CC PubMed:342903). Does not bind rRNA. Probably requires ribosomal protein
CC S2 to associate with the 30S subunit (PubMed:12068815). Binds in the
CC junction of the head, platform and main body of the 30S subunit; the N-
CC terminus penetrates the 30S subunit while the C-terminus faces
CC ribosomal protein S2 (PubMed:11593008). Nascent polypeptide chains
CC cross-link this protein in situ (PubMed:9716382). Can be cross-linked
CC to mRNA in the ribosome (PubMed:1712292). In case of infection by
CC bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase
CC complex, the other subunits are the viral replicase catalytic subunit
CC (AC P14647), host EF-Tu and EF-Ts (PubMed:816798, PubMed:6358207,
CC PubMed:25122749). {ECO:0000269|PubMed:11593008,
CC ECO:0000269|PubMed:12068815, ECO:0000269|PubMed:1712292,
CC ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:342903,
CC ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:7003157,
CC ECO:0000269|PubMed:7041110, ECO:0000269|PubMed:778845,
CC ECO:0000269|PubMed:816798, ECO:0000269|PubMed:9716382}.
CC -!- INTERACTION:
CC P0AG67; P0AG67: rpsA; NbExp=2; IntAct=EBI-546520, EBI-546520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:342903}.
CC -!- INDUCTION: Represses its own translation via the N-terminus (at protein
CC level). {ECO:0000269|PubMed:2120211}.
CC -!- DOMAIN: The 6 S1 motif domains are not equivalent; the first 2 no
CC longer bind rRNA but instead are involved in protein-ribosome and
CC protein-protein interactions. Binds to the 30S ribosomal subunit via
CC its N-terminal fragment (190 residues, the first 2 S1 motifs) and
CC allows translation by S1-free ribosomes (PubMed:7003157,
CC PubMed:15340139). The same fragment represses its own translation
CC (PubMed:2120211). The first 3 S1 motifs do however bind to mRNA
CC pseudoknots in the 5'-UTR of at least 1 mRNA (rpsO); deletion of S1
CC motifs 1-3 but not motifs 4-6 is not viable, although a deletion of
CC motifs 4-6 grows slowly and is cold-sensitive (PubMed:24339747). In
CC case of infection by bacteriophage Qbeta the same N-terminal fragment
CC is necessary and sufficient to form the Qbeta virus RNA-dependent RNA
CC polymerase, although in vitro (-) strand RNA synthesis from the (+)
CC strand genomic RNA also requires the third S1 motif (residues 1-273)
CC (PubMed:6358207, PubMed:25122749). The third S1 motif is required to
CC bind mRNA, tmRNA and viral M-site RNA but requires cooperation with
CC other S1 motifs (PubMed:15340139, PubMed:25122749).
CC {ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:2120211,
CC ECO:0000269|PubMed:24339747, ECO:0000269|PubMed:25122749,
CC ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:7003157}.
CC -!- PTM: Phosphorylated; probably on a serine.
CC {ECO:0000269|PubMed:7783627}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. Upon depletion
CC cell growth and total protein synthesis become linear.
CC {ECO:0000269|PubMed:9677288}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; V00342; CAA23630.1; -; Genomic_DNA.
DR EMBL; V00352; CAA23644.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73997.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35655.1; -; Genomic_DNA.
DR EMBL; X00785; CAA25361.1; -; Genomic_DNA.
DR EMBL; X04864; CAA28556.1; -; Genomic_DNA.
DR PIR; F64830; R3EC1.
DR RefSeq; NP_415431.1; NC_000913.3.
DR RefSeq; WP_000140327.1; NZ_STEB01000006.1.
DR PDB; 2BH8; X-ray; 1.90 A; A/B=364-398.
DR PDB; 2KHI; NMR; -; A=267-361.
DR PDB; 2KHJ; NMR; -; A=441-528.
DR PDB; 4Q7J; X-ray; 2.90 A; D/H=1-273.
DR PDB; 4R71; X-ray; 3.21 A; E/F=2-171.
DR PDB; 5XQ5; NMR; -; A=350-443.
DR PDB; 6BU8; EM; 3.50 A; Z=4-557.
DR PDB; 6H4N; EM; 3.00 A; y=1-557.
DR PDB; 6H58; EM; 7.90 A; y/yy=1-557.
DR PDB; 6ZTJ; EM; 3.40 A; AY=1-557.
DR PDB; 7QGH; EM; 4.48 A; t=1-557.
DR PDBsum; 2BH8; -.
DR PDBsum; 2KHI; -.
DR PDBsum; 2KHJ; -.
DR PDBsum; 4Q7J; -.
DR PDBsum; 4R71; -.
DR PDBsum; 5XQ5; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6ZTJ; -.
DR PDBsum; 7QGH; -.
DR AlphaFoldDB; P0AG67; -.
DR BMRB; P0AG67; -.
DR SMR; P0AG67; -.
DR BioGRID; 4263060; 171.
DR BioGRID; 849910; 1.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR DIP; DIP-35884N; -.
DR IntAct; P0AG67; 87.
DR MINT; P0AG67; -.
DR STRING; 511145.b0911; -.
DR CarbonylDB; P0AG67; -.
DR iPTMnet; P0AG67; -.
DR SWISS-2DPAGE; P0AG67; -.
DR jPOST; P0AG67; -.
DR PaxDb; P0AG67; -.
DR PRIDE; P0AG67; -.
DR EnsemblBacteria; AAC73997; AAC73997; b0911.
DR EnsemblBacteria; BAA35655; BAA35655; BAA35655.
DR GeneID; 67414201; -.
DR GeneID; 945536; -.
DR KEGG; ecj:JW0894; -.
DR KEGG; eco:b0911; -.
DR PATRIC; fig|1411691.4.peg.1365; -.
DR EchoBASE; EB0893; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_6; -.
DR InParanoid; P0AG67; -.
DR OMA; SLNEFRY; -.
DR PhylomeDB; P0AG67; -.
DR BioCyc; EcoCyc:EG10900-MON; -.
DR BioCyc; MetaCyc:EG10900-MON; -.
DR EvolutionaryTrace; P0AG67; -.
DR PRO; PR:P0AG67; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:CAFA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:EcoCyc.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:EcoCyc.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEP:EcoCyc.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:EcoCyc.
DR GO; GO:0006412; P:translation; IMP:EcoCyc.
DR Gene3D; 2.40.50.140; -; 6.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR000110; Ribosomal_S1.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724:SF7; PTHR10724:SF7; 2.
DR Pfam; PF00575; S1; 6.
DR PIRSF; PIRSF002111; RpsA; 1.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 6.
DR SUPFAM; SSF50249; SSF50249; 6.
DR TIGRFAMs; TIGR00717; rpsA; 1.
DR PROSITE; PS50126; S1; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1..557
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196033"
FT DOMAIN 21..87
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 105..171
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 192..260
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 277..347
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 364..434
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 451..520
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 363
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 205
FT /note="Y->A: Decreased binding of Q beta-derived M-site
FT RNA, 80% synthesis of (-) strand RNA, in construct
FT expressing residues 1-273."
FT /evidence="ECO:0000269|PubMed:25122749"
FT MUTAGEN 208
FT /note="F->A: Decreased binding of Q beta-derived M-site
FT RNA, 50% synthesis of (-) strand RNA, in construct
FT expressing residues 1-273."
FT /evidence="ECO:0000269|PubMed:25122749"
FT MUTAGEN 219
FT /note="H->A: Decreased binding of Q beta-derived M-site
FT RNA, 40% synthesis of (-) strand RNA, in construct
FT expressing residues 1-273."
FT /evidence="ECO:0000269|PubMed:25122749"
FT MUTAGEN 254
FT /note="R->A: Decreased binding of Q beta-derived M-site
FT RNA, 40% synthesis of (-) strand RNA, in construct
FT expressing residues 1-273."
FT /evidence="ECO:0000269|PubMed:25122749"
FT CONFLICT 125
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="ER -> D (in Ref. 1; CAA23630 and 2; CAA23644)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 21..31
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4Q7J"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4Q7J"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:4Q7J"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:4Q7J"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:4Q7J"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4Q7J"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4R71"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4Q7J"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:2KHI"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:2KHI"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2KHI"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2KHI"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:2KHI"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:2KHI"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:2KHI"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:5XQ5"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:5XQ5"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:5XQ5"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5XQ5"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:5XQ5"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:5XQ5"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5XQ5"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:5XQ5"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:5XQ5"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:5XQ5"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:5XQ5"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:5XQ5"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:5XQ5"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:2KHJ"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:2KHJ"
FT STRAND 450..461
FT /evidence="ECO:0007829|PDB:2KHJ"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:2KHJ"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:2KHJ"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:2KHJ"
FT STRAND 500..509
FT /evidence="ECO:0007829|PDB:2KHJ"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:2KHJ"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:2KHJ"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:2KHJ"
SQ 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
