ID L0ILA0_THETR Unreviewed; 100 AA.
AC L0ILA0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=Thethe_01369 {ECO:0000313|EMBL:AGB19011.1};
OS Thermoanaerobacterium thermosaccharolyticum M0795.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=698948 {ECO:0000313|EMBL:AGB19011.1, ECO:0000313|Proteomes:UP000010845};
RN [1] {ECO:0000313|EMBL:AGB19011.1, ECO:0000313|Proteomes:UP000010845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0795 {ECO:0000313|EMBL:AGB19011.1,
RC ECO:0000313|Proteomes:UP000010845};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Feinberg L., Folden J., Hogsett D.,
RA Shaw J., Woyke T.;
RT "Complete sequence of chromosome of Thermoanaerobacterium
RT thermosaccharolyticum M0795.";
RL Submitted (MAR-2012) 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; CP003066; AGB19011.1; -; Genomic_DNA.
DR AlphaFoldDB; L0ILA0; -.
DR KEGG; tto:Thethe_01369; -.
DR PATRIC; fig|698948.3.peg.1362; -.
DR HOGENOM; CLU_148518_0_0_9; -.
DR Proteomes; UP000010845; 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 100 AA; 11793 MW; A4BB9EEE46DEBAAC CRC64;
MLFGEFNSGG EIMLNKERKN EIIAQNRIHE KDTGSPEVQI ALLTERINSL NEHLKVHKKD
HHSRRGLLKM VGQRRGLLNY LMKKDMDRYR AIVEKLDLRK
//
