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Database: UniProt
Entry: A0A0G3A8Z3_9ACTN
LinkDB: A0A0G3A8Z3_9ACTN
Original site: A0A0G3A8Z3_9ACTN 
ID   A0A0G3A8Z3_9ACTN        Unreviewed;        95 AA.
AC   A0A0G3A8Z3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, 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=ABB07_10235 {ECO:0000313|EMBL:AKJ10383.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ10383.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ10383.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(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}.
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DR   EMBL; CP011497; AKJ10383.1; -; Genomic_DNA.
DR   RefSeq; WP_030619140.1; NZ_CP011497.1.
DR   AlphaFoldDB; A0A0G3A8Z3; -.
DR   STRING; 665007.ABB07_10235; -.
DR   PATRIC; fig|665007.5.peg.2234; -.
DR   Proteomes; UP000035366; 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   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   95 AA;  10750 MW;  4441B1DADE34B923 CRC64;
     MSLDAATKKQ IIAEFGTKEG DTGSPEVQVA LLSRRISDLT EHLKTHKHDH HSRRGLLILV
     GQRRRLLQYL AKKDIQRFRT LVDRLGIRRG AAGAK
//
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