ID   RS15_CLOBM              Reviewed;          87 AA.
AC   B1KWK2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN   Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=CLK_1789;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it helps nucleate assembly of the platform of the 30S
CC       subunit by binding and bridging several RNA helices of the 16S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC       the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the 50S
CC       subunit in the 70S ribosome, contacting the 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACA55644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000962; ACA55644.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003388351.1; NC_010520.1.
DR   AlphaFoldDB; B1KWK2; -.
DR   SMR; B1KWK2; -.
DR   EnsemblBacteria; ACA55644; ACA55644; CLK_1789.
DR   GeneID; 5186669; -.
DR   KEGG; cbl:CLK_1789; -.
DR   HOGENOM; CLU_148518_0_1_9; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR   HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR   InterPro; IPR000589; Ribosomal_S15.
DR   InterPro; IPR005290; Ribosomal_S15_bac-type.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   PANTHER; PTHR23321; PTHR23321; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; SSF47060; 1.
DR   TIGRFAMs; TIGR00952; S15_bact; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..87
FT                   /note="30S ribosomal protein S15"
FT                   /id="PRO_0000354187"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   87 AA;  10276 MW;  22995A25AF486614 CRC64;
     MDKAKKQELM AKHARHEGDT GSPEVQIALL TERINHLNSH LKEHKKDHHS RRGLLMMVGK
     RRGLLNYLMR EDIERYRAII KELGLRK