RS1_ECO57
ID RS1_ECO57 Reviewed; 557 AA.
AC P0AG69; P02349; P77352;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=Z1257, ECs0994;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG55396.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34417.1; -; Genomic_DNA.
DR PIR; B90753; B90753.
DR PIR; H85616; H85616.
DR RefSeq; NP_309021.1; NC_002695.1.
DR RefSeq; WP_000140327.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AG69; -.
DR BMRB; P0AG69; -.
DR SMR; P0AG69; -.
DR STRING; 155864.EDL933_1174; -.
DR EnsemblBacteria; AAG55396; AAG55396; Z1257.
DR EnsemblBacteria; BAB34417; BAB34417; ECs_0994.
DR GeneID; 67414201; -.
DR GeneID; 917736; -.
DR KEGG; ece:Z1257; -.
DR KEGG; ecs:ECs_0994; -.
DR PATRIC; fig|386585.9.peg.1114; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_6; -.
DR OMA; SLNEFRY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1..557
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196034"
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
