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Database: UniProt
Entry: A0A1V0DB79_9BACT
LinkDB: A0A1V0DB79_9BACT
Original site: A0A1V0DB79_9BACT 
ID   A0A1V0DB79_9BACT        Unreviewed;        88 AA.
AC   A0A1V0DB79;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=AWN76_003340 {ECO:0000313|EMBL:ARA92301.1};
OS   Rhodothermaceae bacterium RA.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX   NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA92301.1, ECO:0000313|Proteomes:UP000055617};
RN   [1] {ECO:0000313|EMBL:ARA92301.1, ECO:0000313|Proteomes:UP000055617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA {ECO:0000313|EMBL:ARA92301.1,
RC   ECO:0000313|Proteomes:UP000055617};
RA   Liew K.J.;
RT   "Complete genome of the potential lignocellulosic biomass degrader
RT   Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT   Malaysia.";
RL   Submitted (MAR-2017) 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}.
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DR   EMBL; CP020382; ARA92301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0DB79; -.
DR   STRING; 1779382.AWN76_003340; -.
DR   KEGG; rbar:AWN76_003340; -.
DR   OrthoDB; 9799262at2; -.
DR   Proteomes; UP000055617; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000055617};
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;  10390 MW;  78A597D0E4650C5B CRC64;
     MITKEQKEAL VAQFGKHERD TGTPEVQIAI FSARINELTE HLKTHPKDHS TRRGLLKLVG
     KRRRLLNYVQ EQDVERYRTI IRELGIRK
//
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