RL15_ENTFA
ID RL15_ENTFA Reviewed; 146 AA.
AC Q839E5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341};
GN Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; OrderedLocusNames=EF_0226;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO80094.1; -; Genomic_DNA.
DR RefSeq; NP_814023.1; NC_004668.1.
DR RefSeq; WP_002356221.1; NZ_KE136524.1.
DR PDB; 6WU9; EM; 2.90 A; M=1-146.
DR PDB; 7P7R; EM; 2.90 A; O=1-146.
DR PDBsum; 6WU9; -.
DR PDBsum; 7P7R; -.
DR AlphaFoldDB; Q839E5; -.
DR SMR; Q839E5; -.
DR STRING; 226185.EF_0226; -.
DR EnsemblBacteria; AAO80094; AAO80094; EF_0226.
DR GeneID; 60892720; -.
DR KEGG; efa:EF0226; -.
DR PATRIC; fig|226185.45.peg.41; -.
DR eggNOG; COG0200; Bacteria.
DR HOGENOM; CLU_055188_4_2_9; -.
DR OMA; FKNINRV; -.
DR Proteomes; UP000001415; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..146
FT /note="50S ribosomal protein L15"
FT /id="PRO_0000104719"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6WU9"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6WU9"
SQ SEQUENCE 146 AA; 15574 MW; 7A795D2FBC417A04 CRC64;
MKLHELKPAE GSRQVRNRVG RGTSSGNGKT AGRGQKGQKA RSGGGVRLGF EGGQTPLFRR
LPKRGFTNIN RKDYAVVNLD TLNRFEDGTE VTPVVLKEAG IVKNEKAGIK VLADGELTKK
LTVKAAKFSK SAQEAIEAAG GSIEVI