RS15_CLOBH
ID RS15_CLOBH Reviewed; 87 AA.
AC A5I4I8; A7G5N9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343};
GN OrderedLocusNames=CBO2414, CLC_2260;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
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=ABS37314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM412317; CAL83960.1; -; Genomic_DNA.
DR EMBL; CP000727; ABS37314.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003388351.1; NC_009698.1.
DR RefSeq; YP_001254909.1; NC_009495.1.
DR RefSeq; YP_001388104.1; NC_009698.1.
DR AlphaFoldDB; A5I4I8; -.
DR SMR; A5I4I8; -.
DR GeneID; 5186669; -.
DR KEGG; cbh:CLC_2260; -.
DR KEGG; cbo:CBO2414; -.
DR PATRIC; fig|413999.7.peg.2390; -.
DR HOGENOM; CLU_148518_0_1_9; -.
DR OMA; FKTHVKD; -.
DR PRO; PR:A5I4I8; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..87
FT /note="30S ribosomal protein S15"
FT /id="PRO_0000354185"
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
