RS1_BUCBP
ID RS1_BUCBP Reviewed; 566 AA.
AC Q89AJ3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=bbp_286;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAO27011.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016826; AAO27011.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011091412.1; NC_004545.1.
DR AlphaFoldDB; Q89AJ3; -.
DR SMR; Q89AJ3; -.
DR STRING; 224915.bbp_286; -.
DR PRIDE; Q89AJ3; -.
DR EnsemblBacteria; AAO27011; AAO27011; bbp_286.
DR GeneID; 56470827; -.
DR KEGG; bab:bbp_286; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_6; -.
DR OMA; SLNEFRY; -.
DR OrthoDB; 1235756at2; -.
DR Proteomes; UP000000601; 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; 5.
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 Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding.
FT CHAIN 1..566
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196029"
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..524
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
SQ SEQUENCE 566 AA; 63840 MW; 9C6D2202D1E4AE4E CRC64;
MTESFAQLFE ESLKNIKTRP GSIIQGTVVA ITKDTILVDA KLKSESKIPI DQFKNSQGEL
EVKVGDQIDV ALDAIEDGFG ETLLSREKAK RHEAWLTLEQ AYKDSKTVVG LINGKVKGGF
TVELEDIRAF LPGSLVDIRP VRETMHLEGK ELEFKVIKLD QKRNNVVVSR RAVIESEYNA
ERNLLLETLQ EGLIVSGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNIGDE
VKIKILKFDR EKIRVSLGLK QLSDDPWTKI SERYPEKTKI TGRVTNLTDY GCFVEIEEGV
EGLVHVSEMD WTNKNIHPSK MVQVNSVVKV MILDIDEERR RISLGLKQCK NNPWMEFSKK
YNKGSHVVGK IKSITDFGIF IGLEGSIDGL VHLSDISWNI SGEESVKKYK KGEEVLAVVL
QVDPDRERIS LGIKQLQEDP FAKYVSSHKK GSLVSGTIKK IDNNVIVVSL SEHIDGLIKF
LNISDEIMNV HDNKPWNKAK IGEIVEVKLN SIDKKERIIY LSILEKQELK ISNDIKKNNS
HKQEIDKDKN FSNAMTEAFK AAKNVD