ID F4KMD3_PORAD Unreviewed; 93 AA.
AC F4KMD3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Small ribosomal subunit protein uS15 {ECO:0000256|HAMAP-Rule:MF_01343};
GN Name=rpsO {ECO:0000256|HAMAP-Rule:MF_01343};
GN OrderedLocusNames=Poras_0298 {ECO:0000313|EMBL:AEE12252.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12252.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) 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; CP002689; AEE12252.1; -; Genomic_DNA.
DR RefSeq; WP_004331294.1; NC_015501.1.
DR AlphaFoldDB; F4KMD3; -.
DR STRING; 879243.Poras_0298; -.
DR KEGG; pah:Poras_0298; -.
DR eggNOG; COG0184; Bacteria.
DR HOGENOM; CLU_148518_0_1_10; -.
DR OrthoDB; 9799262at2; -.
DR Proteomes; UP000006545; 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:UP000006545};
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 93 AA; 10913 MW; A798B7706F10C33F CRC64;
MYLDSTKKQE IFAQYGASAQ DTGSVESQVA LFTYRIQHLT EHLKDNKKDF STSRSLKMLV
GKRRRLLDYL AKKDIERYRK LIADLGIRHT TKF
//
