RS15_CAMJE
ID RS15_CAMJE Reviewed; 90 AA.
AC Q0PA13; P49392; Q9PP46;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=Cj0884;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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:0000255|HAMAP-Rule:MF_01343}.
CC -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
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:0000255|HAMAP-Rule:MF_01343}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000255|HAMAP-Rule:MF_01343}.
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DR EMBL; AL111168; CAL35006.1; -; Genomic_DNA.
DR PIR; E81361; E81361.
DR RefSeq; WP_002852579.1; NC_002163.1.
DR RefSeq; YP_002344284.1; NC_002163.1.
DR PDB; 4IYL; X-ray; 2.36 A; A=1-90.
DR PDBsum; 4IYL; -.
DR AlphaFoldDB; Q0PA13; -.
DR SMR; Q0PA13; -.
DR IntAct; Q0PA13; 20.
DR STRING; 192222.Cj0884; -.
DR PaxDb; Q0PA13; -.
DR PRIDE; Q0PA13; -.
DR EnsemblBacteria; CAL35006; CAL35006; Cj0884.
DR GeneID; 905176; -.
DR KEGG; cje:Cj0884; -.
DR PATRIC; fig|192222.6.peg.869; -.
DR eggNOG; COG0184; Bacteria.
DR HOGENOM; CLU_148518_0_0_7; -.
DR OMA; FKTHVKD; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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 HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR InterPro; IPR000589; Ribosomal_S15.
DR InterPro; IPR005290; Ribosomal_S15_bac-type.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR PANTHER; PTHR23321; PTHR23321; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR TIGRFAMs; TIGR00952; S15_bact; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..90
FT /note="30S ribosomal protein S15"
FT /id="PRO_0000115407"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:4IYL"
FT HELIX 25..51
FT /evidence="ECO:0007829|PDB:4IYL"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:4IYL"
FT HELIX 56..73
FT /evidence="ECO:0007829|PDB:4IYL"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:4IYL"
SQ SEQUENCE 90 AA; 10226 MW; 19A41B60BAB8180C CRC64;
MALDSAKKAE IVAKFAKKPG DTGSTEVQVA LLTARIAELT EHLKIYKKDF SSRLGLLKLV
GQRKRLLSYL KRKDYNSYSK LITELNLRDK