ID   RS1_ECOL6               Reviewed;         557 AA.
AC   P0AG68; P02349; P77352;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=30S ribosomal protein S1;
GN   Name=rpsA; OrderedLocusNames=c1049;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Required for translation of most natural mRNAs except for
CC       leaderless mRNA. Binds mRNA upstream of the Shine-Dalgarno (SD)
CC       sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA
CC       chaperone to unfold structured mRNA on the ribosome but is not
CC       essential for mRNAs with strong SDs and little 5'-UTR structure, thus
CC       it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by
CC       binding to transiently formed ssRNA regions; binds about 10
CC       nucleotides. Has a preference for polypyrimidine tracts. Negatively
CC       autoregulates its own translation. {ECO:0000250|UniProtKB:P0AG67}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Some nascent polypeptide
CC       chains are able to cross-link to this protein in situ. Can be cross-
CC       linked to mRNA in the ribosome (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated; probably on a serine. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE014075; AAN79519.1; -; Genomic_DNA.
DR   RefSeq; WP_000140327.1; NC_004431.1.
DR   AlphaFoldDB; P0AG68; -.
DR   BMRB; P0AG68; -.
DR   SMR; P0AG68; -.
DR   STRING; 199310.c1049; -.
DR   EnsemblBacteria; AAN79519; AAN79519; c1049.
DR   GeneID; 67414201; -.
DR   KEGG; ecc:c1049; -.
DR   eggNOG; COG0539; Bacteria.
DR   HOGENOM; CLU_015805_2_1_6; -.
DR   OMA; SLNEFRY; -.
DR   BioCyc; ECOL199310:C1049-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   3: Inferred from homology;
KW   Acetylation; Phosphoprotein; Repeat; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding.
FT   CHAIN           1..557
FT                   /note="30S ribosomal protein S1"
FT                   /id="PRO_0000196035"
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:0000250"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         363
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
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