ID A0A0A2TQ44_9FIRM Unreviewed; 89 AA.
AC A0A0A2TQ44;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=JT05_03630 {ECO:0000313|EMBL:KGP76643.1};
OS Desulfosporosinus sp. Tol-M.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP76643.1, ECO:0000313|Proteomes:UP000030439};
RN [1] {ECO:0000313|EMBL:KGP76643.1, ECO:0000313|Proteomes:UP000030439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B., Dao A., Foght J.;
RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT probing of toluene- degrading methanogenic culture enriched from oil sands
RT tailing of Alberta, Canada.";
RL Submitted (OCT-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGP76643.1}.
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DR EMBL; JQID01000055; KGP76643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TQ44; -.
DR STRING; 1536651.JT05_03630; -.
DR Proteomes; UP000030439; Unassembled WGS sequence.
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:UP000030439};
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}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 89 AA; 10537 MW; D35A0A3E6B0F0438 CRC64;
MMMTPERKQE IIQKHARKEG DTGSPEVQIA LLTERIIYLT EHFKTHKKDH HSRRGLLKMV
GSRRALLTYL KNVDIERYRN LIAELGLRK
//
