ID   RL5_AQUPY               Reviewed;         188 AA.
AC   Q9ZI40;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Synonyms=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333};
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX   PubMed=10795828; DOI=10.1007/s002399910040;
RA   Bocchetta M., Gribaldo S., Sanangelantoni A.M., Cammarano P.;
RT   "Phylogenetic depth of the bacterial genera Aquifex and Thermotoga inferred
RT   from analysis of ribosomal protein, elongation factor, and RNA polymerase
RT   subunit sequences.";
RL   J. Mol. Evol. 50:366-380(2000).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA   Veuthey A.-L.;
RL   Unpublished observations (MAR-2000).
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; AF040101; AAD08795.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZI40; -.
DR   SMR; Q9ZI40; -.
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   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..188
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000124886"
FT   CONFLICT        182..188
FT                   /note="GLPIRAM -> RTAHKGYVIKCLLSGGNYAEKG (in Ref. 1;
FT                   AAD08795)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21385 MW;  38AF4246E2FC93E1 CRC64;
     MSATETKYVP RLYKKYKEEV VPKLIQKFQY KNPMQVPRLV KIVVNMGVGE AVQDIKQLER
     AVEDLRAITG QQPMITRARK SKAGFKLRKG MPIGCKVTLR NHTMWDFLDK VISVALPRVK
     DFKGLNPRSF DGRGNYAFGI AEQIVFPEID YDKVDRIRGM DIIINTTAVS DQESLLATLT
     LGLPIRAM