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Database: UniProt
Entry: F4C5G4_SPHS2
LinkDB: F4C5G4_SPHS2
Original site: F4C5G4_SPHS2 
ID   F4C5G4_SPHS2            Unreviewed;        92 AA.
AC   F4C5G4;
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=Sph21_3076 {ECO:0000313|EMBL:ADZ79621.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ79621.1};
RN   [1] {ECO:0000313|EMBL:ADZ79621.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ79621.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-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; CP002584; ADZ79621.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4C5G4; -.
DR   STRING; 743722.Sph21_3076; -.
DR   KEGG; shg:Sph21_3076; -.
DR   PATRIC; fig|743722.3.peg.3285; -.
DR   eggNOG; COG0184; Bacteria.
DR   HOGENOM; CLU_148518_0_1_10; -.
DR   OrthoDB; 9799262at2; -.
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   92 AA;  10707 MW;  B78AF84255B920E2 CRC64;
     MYLSKEYKEG IFAEFAGNAK NTGSTEGQVA LFTKRIAHLT EHLKKNRKDF STQLALQKLV
     GKRRSLLSYL YKKDIERYRA IIKALELRDI IK
//
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