ID   RL5_ENTFA               Reviewed;         179 AA.
AC   Q839F2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=EF_0218;
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 1 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. In the 70S ribosome it contacts
CC       protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC       this bridge is implicated in subunit movement. Contacts the P site
CC       tRNA; the 5S rRNA and some of its associated proteins might help
CC       stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01333}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA.
CC       Forms a bridge to the 30S subunit in the 70S ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
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; AE016830; AAO80087.1; -; Genomic_DNA.
DR   RefSeq; NP_814016.1; NC_004668.1.
DR   RefSeq; WP_002356213.1; NZ_KE136524.1.
DR   PDB; 6WU9; EM; 2.90 A; F=2-178.
DR   PDB; 7P7R; EM; 2.90 A; J=1-179.
DR   PDBsum; 6WU9; -.
DR   PDBsum; 7P7R; -.
DR   AlphaFoldDB; Q839F2; -.
DR   SMR; Q839F2; -.
DR   STRING; 226185.EF_0218; -.
DR   EnsemblBacteria; AAO80087; AAO80087; EF_0218.
DR   GeneID; 60892713; -.
DR   KEGG; efa:EF0218; -.
DR   PATRIC; fig|226185.45.peg.48; -.
DR   eggNOG; COG0094; Bacteria.
DR   HOGENOM; CLU_061015_2_1_9; -.
DR   OMA; ERMYAFL; -.
DR   Proteomes; UP000001415; Chromosome.
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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR020930; Ribosomal_L5_bac-type.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR020929; Ribosomal_L5_CS.
DR   InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_L5_N.
DR   PANTHER; PTHR11994; PTHR11994; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; SSF55282; 1.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..179
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000124928"
FT   HELIX           5..19
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   HELIX           93..105
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:6WU9"
FT   HELIX           163..171
FT                   /evidence="ECO:0007829|PDB:6WU9"
SQ   SEQUENCE   179 AA;  20093 MW;  90FA66C8D7D3A304 CRC64;
     MNRLKEKYIK EVTPSLVEKF NYSSVMQTPK VDKIVINMGV GDAVSNAKNL DKAVEELALI
     TGQKPLITKA KKSIAGFRLR EGMPIGAKVT LRGERMYEFL DKLVTVSLPR VRDFHGVSKK
     AFDGRGNYTL GIKEQLIFPE VDYDLVDKVR GMDIVIVTTA NTDEESRELL AQLGMPFQK