ID G4Q2Z5_ACIIR Unreviewed; 88 AA.
AC G4Q2Z5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AEQ22801.1};
GN OrderedLocusNames=Acin_1583 {ECO:0000313|EMBL:AEQ22801.1};
OS Acidaminococcus intestini (strain RyC-MR95).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ22801.1, ECO:0000313|Proteomes:UP000007093};
RN [1] {ECO:0000313|EMBL:AEQ22801.1, ECO:0000313|Proteomes:UP000007093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ22801.1,
RC ECO:0000313|Proteomes:UP000007093};
RX PubMed=22123762; DOI=10.1128/JB.06301-11;
RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA Latorre A.;
RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT negative bacterium from the phylum Firmicutes.";
RL J. Bacteriol. 193:7008-7009(2011).
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; CP003058; AEQ22801.1; -; Genomic_DNA.
DR AlphaFoldDB; G4Q2Z5; -.
DR STRING; 568816.Acin_1583; -.
DR KEGG; ain:Acin_1583; -.
DR PATRIC; fig|568816.4.peg.1536; -.
DR eggNOG; COG0184; Bacteria.
DR HOGENOM; CLU_148518_0_0_9; -.
DR InParanoid; G4Q2Z5; -.
DR Proteomes; UP000007093; 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:UP000007093};
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; 10418 MW; 5E1B803948D4CAF1 CRC64;
MLTPARKKEL IETYRINEAD TGSPEVQIAI LSERISYLTE HLKNNKKDHH SRRGLLKMVG
QRRGLLNYLM KKDIERYRSI VERLGLRK
//
