ID   RS1_STAAS               Reviewed;         391 AA.
AC   Q6G987;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=30S ribosomal protein S1;
GN   Name=rpsA; OrderedLocusNames=SAS1417;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC       point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC       purine-rich sequence (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000305}.
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DR   EMBL; BX571857; CAG43194.1; -; Genomic_DNA.
DR   RefSeq; WP_000133954.1; NC_002953.3.
DR   AlphaFoldDB; Q6G987; -.
DR   SMR; Q6G987; -.
DR   KEGG; sas:SAS1417; -.
DR   HOGENOM; CLU_015805_4_5_9; -.
DR   OMA; WQQFART; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR10724:SF7; PTHR10724:SF7; 2.
DR   Pfam; PF00575; S1; 4.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 4.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   PROSITE; PS50126; S1; 4.
PE   3: Inferred from homology;
KW   Repeat; Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT   CHAIN           1..391
FT                   /note="30S ribosomal protein S1"
FT                   /id="PRO_0000196051"
FT   DOMAIN          16..90
FT                   /note="S1 motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          108..173
FT                   /note="S1 motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          194..262
FT                   /note="S1 motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          279..348
FT                   /note="S1 motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
SQ   SEQUENCE   391 AA;  43287 MW;  C7DD4497CC95FCC2 CRC64;
     MTEEFNESMI NDIKEGDKVT GEVQQVEDKQ VVVHINGGKF NGIIPISQLS THHIDSPSEV
     VKEGDEVEAY VTKVEFDEEN ETGAYILSRR QLETEKSYSY LQEKLDNNEI IEAKVTEVVK
     GGLVVDVGQR GFVPASLIST DFIEDFSVFD GQTIRIKVEE LDPENNRVIL SRKAVEQEEN
     DAKKDQLLQS LNEGDVIDGK VARLTQFGAF IDIGGVDGLV HVSELSHEHV QTPEEVVSIG
     QDVKVKIKSI DRDTERISLS IKDTLPTPFE NIKGQFHEND VIEGVVVRLA NFGAFVEIAP
     GVQGLVHISE IAHKHIGTPG EVLEPGQQVN VKILGIDEEN ERVSLSIKAT LPNEDVVESD
     PSTTKAYLEN EEEDNPTIGD MIGDKLKNLK L