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Database: UniProt
Entry: A0A3P1S398_9FIRM
LinkDB: A0A3P1S398_9FIRM
Original site: A0A3P1S398_9FIRM 
ID   A0A3P1S398_9FIRM        Unreviewed;        88 AA.
AC   A0A3P1S398;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Small ribosomal subunit protein uS15 {ECO:0000256|HAMAP-Rule:MF_01343};
GN   Name=rpsO {ECO:0000256|HAMAP-Rule:MF_01343};
GN   ORFNames=EII25_06100 {ECO:0000313|EMBL:RRC91731.1};
OS   Erysipelotrichaceae bacterium OH741_COT-311.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=2491058 {ECO:0000313|EMBL:RRC91731.1, ECO:0000313|Proteomes:UP000270315};
RN   [1] {ECO:0000313|EMBL:RRC91731.1, ECO:0000313|Proteomes:UP000270315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH741_COT-311 {ECO:0000313|EMBL:RRC91731.1,
RC   ECO:0000313|Proteomes:UP000270315};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) 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}.
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:RRC91731.1}.
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DR   EMBL; RQZE01000009; RRC91731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1S398; -.
DR   OrthoDB; 9799262at2; -.
DR   Proteomes; UP000270315; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000270315};
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01343};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01343}.
SQ   SEQUENCE   88 AA;  10301 MW;  2C69C34CDF81B873 CRC64;
     MLTKAEKTAI INEYARGTND TGSVEVQVAV LTAQINRLTE HLKEHKKDYH STRGLMKMVG
     RRKNFLAYLR DKDINRYREL VQRLGLRK
//
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