ID   RL15_STAAR              Reviewed;         146 AA.
AC   Q6GEK2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341};
GN   Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; OrderedLocusNames=SAR2316;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01341}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01341}.
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DR   EMBL; BX571856; CAG41297.1; -; Genomic_DNA.
DR   RefSeq; WP_000766074.1; NC_002952.2.
DR   AlphaFoldDB; Q6GEK2; -.
DR   SMR; Q6GEK2; -.
DR   GeneID; 66840443; -.
DR   KEGG; sar:SAR2316; -.
DR   HOGENOM; CLU_055188_4_2_9; -.
DR   OMA; FKNINRV; -.
DR   OrthoDB; 1874945at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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   HAMAP; MF_01341; Ribosomal_L15; 1.
DR   InterPro; IPR036227; L18e/L15P_sf.
DR   InterPro; IPR030878; Ribosomal_L15.
DR   InterPro; IPR005749; Ribosomal_L15_bac-type.
DR   InterPro; IPR001196; Ribosomal_L15_CS.
DR   InterPro; IPR021131; Ribosomal_L18e/L15P.
DR   PANTHER; PTHR12934; PTHR12934; 1.
DR   Pfam; PF00828; Ribosomal_L27A; 1.
DR   SUPFAM; SSF52080; SSF52080; 1.
DR   TIGRFAMs; TIGR01071; rplO_bact; 1.
DR   PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..146
FT                   /note="50S ribosomal protein L15"
FT                   /id="PRO_0000104809"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   146 AA;  15597 MW;  6CB42B627B38F93E CRC64;
     MKLHELKPAE GSRKERNRVG RGVATGNGKT SGRGHKGQKA RSGGGVRPGF EGGQLPLFRR
     LPKRGFTNIN RKEYAIVNLD QLNKFEDGTE VTPALLVESG VVKNEKSGIK ILGNGSLDKK
     LTVKAHKFSA SAAEAIDAKG GAHEVI