RS1_STAAR
ID RS1_STAAR Reviewed; 391 AA.
AC Q6GGT5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=SAR1485;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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; BX571856; CAG40483.1; -; Genomic_DNA.
DR RefSeq; WP_000133953.1; NC_002952.2.
DR AlphaFoldDB; Q6GGT5; -.
DR SMR; Q6GGT5; -.
DR KEGG; sar:SAR1485; -.
DR HOGENOM; CLU_015805_4_5_9; -.
DR OMA; WQQFART; -.
DR OrthoDB; 1235756at2; -.
DR Proteomes; UP000000596; Chromosome.
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; 1.
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_0000196050"
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"
FT REGION 356..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43276 MW; 97DD4497D37FD153 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 DIEGVVVRLA NFGAFVEIAP
GVQGLVHISE IAHKHIGTPG EVLEPGQQVN VKILGIDEEN ERVSLSIKAT LPNEDVVESD
PSTTKAYLES EEEDNPTIGD MIGDKLKNLK L