ID A0A221KFY8_VITFI Unreviewed; 107 AA.
AC A0A221KFY8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, 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=VITFI_CDS1945 {ECO:0000313|EMBL:ASM77723.1};
OS Vitreoscilla filiformis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Vitreoscilla.
OX NCBI_TaxID=63 {ECO:0000313|EMBL:ASM77723.1, ECO:0000313|Proteomes:UP000199729};
RN [1] {ECO:0000313|EMBL:ASM77723.1, ECO:0000313|Proteomes:UP000199729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15551 {ECO:0000313|EMBL:ASM77723.1,
RC ECO:0000313|Proteomes:UP000199729};
RA Contreras S., Sagory-Zalkind P., Blanquart H., Iltis A., Morand S.C.;
RT "Complete Genome Sequence of the cosmetic ferment Vitreoscilla filiformis
RT (ATCC15551).";
RL Submitted (JUL-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; CP022423; ASM77723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221KFY8; -.
DR KEGG; vff:VITFI_CDS1945; -.
DR Proteomes; UP000199729; 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:UP000199729};
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 107 AA; 12200 MW; ED3F0696EDCAA3D3 CRC64;
MRRSQQRGWR FQLYKEIAMS VADINKADIV AAHARGAADT GSPEVQVALL TARINELTPH
FKLHAKDHHG RRGLLKMVNQ RKRLLAYLKS TDADRYVALI KKLGLRK
//