ID   RL5_METMJ               Reviewed;         167 AA.
AC   A3CT10;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=Memar_0577;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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. May contact 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; contacts the 5S rRNA and
CC       probably tRNA. 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; CP000562; ABN56510.1; -; Genomic_DNA.
DR   RefSeq; WP_011843420.1; NC_009051.1.
DR   AlphaFoldDB; A3CT10; -.
DR   SMR; A3CT10; -.
DR   STRING; 368407.Memar_0577; -.
DR   PRIDE; A3CT10; -.
DR   EnsemblBacteria; ABN56510; ABN56510; Memar_0577.
DR   GeneID; 4846351; -.
DR   KEGG; mem:Memar_0577; -.
DR   eggNOG; arCOG04092; Archaea.
DR   HOGENOM; CLU_061015_3_0_2; -.
DR   OMA; ERMYAFL; -.
DR   OrthoDB; 97230at2157; -.
DR   Proteomes; UP000002146; 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_A; Ribosomal_L5_A; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR022804; Ribosomal_L5_arc.
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..167
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000365643"
SQ   SEQUENCE   167 AA;  18803 MW;  C678D9043F1EAF36 CRC64;
     MTAMKDIYID KVVVHMGVGE SGERLVKAED LVKQITGQKP VRTIAKRTQP AFGIRKGAPI
     GCKVTLRREN AEKFITTALD IIERRLAPSQ FDRTGNVSFG IEEHTDFPGM SYDPTIGIYG
     MDVNVVLEYK GARIARRSVE RRKLPADQKV NKEEAIAFMC ENYRVEV