RL18_ENTFA
ID RL18_ENTFA Reviewed; 118 AA.
AC Q839E8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337};
GN Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; OrderedLocusNames=EF_0223;
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: This is one of the proteins that binds and probably mediates
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. {ECO:0000255|HAMAP-
CC Rule:MF_01337}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
CC {ECO:0000255|HAMAP-Rule:MF_01337}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000255|HAMAP-Rule:MF_01337}.
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DR EMBL; AE016830; AAO80091.1; -; Genomic_DNA.
DR RefSeq; NP_814020.1; NC_004668.1.
DR RefSeq; WP_002356218.1; NZ_KE136524.1.
DR PDB; 6WU9; EM; 2.90 A; P=2-118.
DR PDB; 7P7R; EM; 2.90 A; R=1-118.
DR PDBsum; 6WU9; -.
DR PDBsum; 7P7R; -.
DR AlphaFoldDB; Q839E8; -.
DR SMR; Q839E8; -.
DR STRING; 226185.EF_0223; -.
DR PRIDE; Q839E8; -.
DR EnsemblBacteria; AAO80091; AAO80091; EF_0223.
DR GeneID; 60892717; -.
DR KEGG; efa:EF0223; -.
DR PATRIC; fig|226185.45.peg.44; -.
DR eggNOG; COG0256; Bacteria.
DR HOGENOM; CLU_098841_0_1_9; -.
DR OMA; NKQIYAQ; -.
DR Proteomes; UP000001415; 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 HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR InterPro; IPR005484; Ribosomal_L18.
DR InterPro; IPR004389; Ribosomal_L18_bac-type.
DR PANTHER; PTHR12899; PTHR12899; 1.
DR Pfam; PF00861; Ribosomal_L18p; 1.
DR TIGRFAMs; TIGR00060; L18_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..118
FT /note="50S ribosomal protein L18"
FT /id="PRO_0000131263"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:6WU9"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6WU9"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:6WU9"
SQ SEQUENCE 118 AA; 12913 MW; AB3DA8BA6930E64E CRC64;
MITKPDKNKT RQKRHRRVRN KISGTAECPR LNIFRSNKNI YAQVIDDVAG VTLASASALD
KEISGGTKTE TAAAVGKLVA ERAAEKGIKK VVFDRGGYLY HGRVQALAEA ARENGLEF
