ID D5AK39_STRGZ Unreviewed; 130 AA.
AC D5AK39;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=SSGZ1_1748 {ECO:0000313|EMBL:ADE32204.1};
OS Streptococcus suis (strain GZ1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE32204.1, ECO:0000313|Proteomes:UP000002359};
RN [1] {ECO:0000313|EMBL:ADE32204.1, ECO:0000313|Proteomes:UP000002359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GZ1 {ECO:0000313|EMBL:ADE32204.1,
RC ECO:0000313|Proteomes:UP000002359};
RX PubMed=19016627; DOI=10.1086/594370;
RA Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., Zhou Z.,
RA Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT "Clinical, experimental, and genomic differences between intermediately
RT pathogenic, highly pathogenic, and epidemic Streptococcus suis.";
RL J. Infect. Dis. 199:97-107(2009).
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; CP000837; ADE32204.1; -; Genomic_DNA.
DR AlphaFoldDB; D5AK39; -.
DR KEGG; ssw:SSGZ1_1748; -.
DR PATRIC; fig|423211.3.peg.1720; -.
DR HOGENOM; CLU_148518_0_1_9; -.
DR Proteomes; UP000002359; 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 130 AA; 15386 MW; 2E4B78708804B3D6 CRC64;
MTKKTILDRI NEVQKDKSSF FLVTGRQPVT RIRLKNKGEH IMAISKEKKN EIMAQYARHE
GDTGSVEVQV AVLTWEINHL NDHIKQHKKD HATYRGLMKK IGRRRNLLAY LRRTDVNRYR
ELIHSLGLRR
//
