ID   RL5_BUCAK               Reviewed;         179 AA.
AC   P46178;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333};
OS   Buchnera aphidicola subsp. Acyrthosiphon kondoi (Acyrthosiphon kondoi
OS   symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera; unclassified Buchnera (in: Bacteria).
OX   NCBI_TaxID=42474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Kurashiki;
RX   PubMed=7584036; DOI=10.1093/dnares/1.3.103;
RA   Abe R., Yamashita A., Isono K.;
RT   "Cloning and characterization of the ribosomal protein genes in the spc
RT   operon of a prokaryotic endosymbiont of the pea aphid, Acyrthosiphon
RT   kondoi.";
RL   DNA Res. 1:103-114(1994).
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}.
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DR   EMBL; D31786; BAA06587.1; -; Genomic_DNA.
DR   AlphaFoldDB; P46178; -.
DR   SMR; P46178; -.
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..179
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000124904"
SQ   SEQUENCE   179 AA;  20272 MW;  CFACC75A394203A4 CRC64;
     MAKLHDYYKD EVIKQLMSQF DYNSVMQVPR VEKITLNMGV GEAIADKKLL DNAAADLAAI
     SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF ERLISIAVPR IRDFRGLSAK
     SFDGRGNYSM GVREQIIFPE IDYDKVDRVR GLDITITTTA KSDDEGRALL AAFNFPFRK