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Database: UniProt
Entry: D9PS24_FINMA
LinkDB: D9PS24_FINMA
Original site: D9PS24_FINMA 
ID   D9PS24_FINMA            Unreviewed;        88 AA.
AC   D9PS24;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Small ribosomal subunit protein uS15 {ECO:0000256|HAMAP-Rule:MF_01343};
GN   Name=rpsO {ECO:0000256|HAMAP-Rule:MF_01343,
GN   ECO:0000313|EMBL:EFK93542.1};
GN   ORFNames=HMPREF9261_0525 {ECO:0000313|EMBL:EFK93542.1};
OS   Finegoldia magna ACS-171-V-Col3.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=768713 {ECO:0000313|EMBL:EFK93542.1, ECO:0000313|Proteomes:UP000003650};
RN   [1] {ECO:0000313|Proteomes:UP000003650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-171-V-Col3 {ECO:0000313|Proteomes:UP000003650};
RA   Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.;
RT   "Genome Sequence of Lactobacillus delbrueckii subsp. bulgaricus PB2003/044-
RT   T3-4.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC       the 50S subunit in the ribosome. {ECO:0000256|HAMAP-Rule:MF_01343}.
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:0000256|HAMAP-Rule:MF_01343, ECO:0000256|RuleBase:RU004524}.
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:0000256|HAMAP-Rule:MF_01343}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01343, ECO:0000256|RuleBase:RU003919}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFK93542.1}.
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DR   EMBL; AECM01000025; EFK93542.1; -; Genomic_DNA.
DR   RefSeq; WP_002838220.1; NZ_AECM01000025.1.
DR   AlphaFoldDB; D9PS24; -.
DR   SMR; D9PS24; -.
DR   GeneID; 60840164; -.
DR   Proteomes; UP000003650; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   Gene3D; 6.10.250.3130; -; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR   InterPro; IPR000589; Ribosomal_uS15.
DR   InterPro; IPR005290; Ribosomal_uS15_bac-type.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   NCBIfam; TIGR00952; S15_bact; 1.
DR   PANTHER; PTHR23321:SF26; 37S RIBOSOMAL PROTEIN S28, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23321; RIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01343};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01343};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01343,
KW   ECO:0000256|RuleBase:RU004524};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01343,
KW   ECO:0000256|RuleBase:RU004524}.
SQ   SEQUENCE   88 AA;  10731 MW;  4E42F27131BAC1C3 CRC64;
     MYNKEIKEEI IKEYQTKEGD TGSPEVQVAL LTYRINYLTE HLKSHKNDHH SRRGLFKMIG
     KRRNLLNYLS NKDIERYRDL IKRLNIRR
//
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