RS1_STAS1
ID RS1_STAS1 Reviewed; 393 AA.
AC Q49XT0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=SSP1270;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008934; BAE18415.1; -; Genomic_DNA.
DR RefSeq; WP_002483245.1; NZ_MTGA01000038.1.
DR AlphaFoldDB; Q49XT0; -.
DR SMR; Q49XT0; -.
DR STRING; 342451.SSP1270; -.
DR DNASU; 3616900; -.
DR EnsemblBacteria; BAE18415; BAE18415; SSP1270.
DR KEGG; ssp:SSP1270; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_4_5_9; -.
DR OMA; WQQFART; -.
DR OrthoDB; 1235756at2; -.
DR Proteomes; UP000006371; 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 Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding.
FT CHAIN 1..393
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196055"
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"
FT COMPBIAS 356..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 42958 MW; EB32C48DF3FD32BA CRC64;
MTEEFNESMI NDIKEGDKVT GEVQEIEEKQ VIVAVNGAKF NGIIPISQLS THHIDNPSDA
VKVGDEIGAY VTKVEYDEEN ETGAYILSKR QLETEKSYEF LQEQLDNNQT IEAKVTEVVK
GGLVVDVGQR GFVPASLIST DFIEDFSDFE GQVLKLKVEE LDPANNRVIL SRKAVEALEN
AEKKDELLES LNEGDVIEGK VARLTNFGAF VDIGGVDGLV HVSELSHEHV KSPEDVVSIG
ETVNVKIKSV DKDSERISLS IKDTLPSPFE SIKGEFNEGD VIEGTVVRLA NFGAFVEIKP
GVQGLVHISE ISHSHIGSPS EALEPGQVVS VKVLGVDVEN ERISLSIKAT LPNENVIESD
SETTQSYLDN GSDDEDNPTL GDVFGDKLKD FKF
