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Database: UniProt
Entry: A0A0G0CEI5_9BACT
LinkDB: A0A0G0CEI5_9BACT
Original site: A0A0G0CEI5_9BACT 
ID   A0A0G0CEI5_9BACT        Unreviewed;       123 AA.
AC   A0A0G0CEI5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 28.
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=UR68_C0001G0096 {ECO:0000313|EMBL:KKP74496.1};
OS   Candidatus Roizmanbacteria bacterium GW2011_GWA2_35_19.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1618478 {ECO:0000313|EMBL:KKP74496.1, ECO:0000313|Proteomes:UP000034457};
RN   [1] {ECO:0000313|EMBL:KKP74496.1, ECO:0000313|Proteomes:UP000034457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKP74496.1}.
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DR   EMBL; LBQC01000001; KKP74496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0CEI5; -.
DR   STRING; 1618478.UR68_C0001G0096; -.
DR   PATRIC; fig|1618478.3.peg.102; -.
DR   Proteomes; UP000034457; 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   123 AA;  14067 MW;  749FB3A1631C6F62 CRC64;
     MKKTETKKKT VKKTSVKTVT KTPAVKKPVK SAPIDTTLLE DKDKIIEKFA QRKGDTGSPE
     VQIALLSHKI IKLSGHLGIN KKDNHSRRGL LKVIAKRRRI LNYLQKLDEK RYKTLIKELG
     LKR
//
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