RS15_ACIB5
ID RS15_ACIB5 Reviewed; 89 AA.
AC B7I3U0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=AB57_0438;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001182; ACJ39862.1; -; Genomic_DNA.
DR RefSeq; WP_001229357.1; NC_011586.2.
DR PDB; 6V39; EM; 3.04 A; o=1-89.
DR PDB; 6V3A; EM; 2.82 A; o=1-89.
DR PDB; 6V3B; EM; 2.91 A; o=1-89.
DR PDB; 6V3E; EM; 4.40 A; o=1-89.
DR PDB; 7M4U; EM; 2.71 A; o=1-89.
DR PDB; 7M4W; EM; 2.55 A; o=1-89.
DR PDB; 7M4X; EM; 2.66 A; o=1-89.
DR PDB; 7M4Y; EM; 2.50 A; o=1-89.
DR PDB; 7M4Z; EM; 2.92 A; o=1-89.
DR PDB; 7RYF; EM; 2.65 A; o=1-89.
DR PDB; 7RYG; EM; 2.38 A; o=1-89.
DR PDB; 7RYH; EM; 2.43 A; o=1-89.
DR PDBsum; 6V39; -.
DR PDBsum; 6V3A; -.
DR PDBsum; 6V3B; -.
DR PDBsum; 6V3E; -.
DR PDBsum; 7M4U; -.
DR PDBsum; 7M4W; -.
DR PDBsum; 7M4X; -.
DR PDBsum; 7M4Y; -.
DR PDBsum; 7M4Z; -.
DR PDBsum; 7RYF; -.
DR PDBsum; 7RYG; -.
DR PDBsum; 7RYH; -.
DR AlphaFoldDB; B7I3U0; -.
DR SMR; B7I3U0; -.
DR IntAct; B7I3U0; 1.
DR GeneID; 60877359; -.
DR GeneID; 66398658; -.
DR KEGG; abn:AB57_0438; -.
DR HOGENOM; CLU_148518_0_0_6; -.
DR OMA; FKTHVKD; -.
DR Proteomes; UP000007094; 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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..89
FT /note="30S ribosomal protein S15"
FT /id="PRO_1000143059"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 25..45
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 50..73
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:7M4U"
SQ SEQUENCE 89 AA; 10125 MW; EBE7F1D1192DA19C CRC64;
MALTNADRAE IIAKFARAEN DTGSPEVQVA LLTAQINDLQ GHFKAHKHDH HSRRGLIRMV
NQRRKLLDYL NGKDHERYTA LIGALGLRR