RL5_METS3
ID RL5_METS3 Reviewed; 170 AA.
AC A5UL75;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=Msm_0748;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86953.1; -; Genomic_DNA.
DR RefSeq; WP_004033223.1; NC_009515.1.
DR AlphaFoldDB; A5UL75; -.
DR SMR; A5UL75; -.
DR STRING; 420247.Msm_0748; -.
DR EnsemblBacteria; ABQ86953; ABQ86953; Msm_0748.
DR GeneID; 5215720; -.
DR KEGG; msi:Msm_0748; -.
DR PATRIC; fig|420247.28.peg.745; -.
DR eggNOG; arCOG04092; Archaea.
DR HOGENOM; CLU_061015_3_0_2; -.
DR OMA; ERMYAFL; -.
DR Proteomes; UP000001992; 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; 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.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT CHAIN 1..170
FT /note="50S ribosomal protein L5"
FT /id="PRO_1000052773"
SQ SEQUENCE 170 AA; 19250 MW; 92B03325293EAD2C CRC64;
MNPMNEVQIS KATVSIGVGE AGEKLSRAIT LLEQMFDQTP VKTFSKVTNP EFGIRKRQPI
ACKLTLRGEK ADKAIEMVLE GINKNIKPTQ FDAQGNLSFG IKEHIDIPGM KYNPDIGIFG
MNVSVTFEKP GYRIAKRRIQ QKKVPAKHRI SKEETMKYME DNFNVNYVTE
