RL5_THEAQ
ID RL5_THEAQ Reviewed; 182 AA.
AC P24315;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 86.
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 Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EP 00276;
RX PubMed=2029902; DOI=10.1111/j.1432-1033.1991.tb15965.x;
RA Jahn O., Hartmann R.K., Erdmann V.A.;
RT "Analysis of the spc ribosomal protein operon of Thermus aquaticus.";
RL Eur. J. Biochem. 197:733-740(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EP 00276;
RX PubMed=1764514; DOI=10.1016/0300-9084(91)90046-4;
RA Jahn O., Hartmann R.K., Boeckh T., Erdmann V.A.;
RT "Comparative analysis of ribosomal protein L5 sequences from bacteria of
RT the genus Thermus.";
RL Biochimie 73:669-678(1991).
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; X56552; CAA39896.1; -; Genomic_DNA.
DR EMBL; S77828; AAB21094.1; -; Genomic_DNA.
DR AlphaFoldDB; P24315; -.
DR SMR; P24315; -.
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..182
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000125011"
SQ SEQUENCE 182 AA; 20830 MW; FBB4F5CED3B1601C CRC64;
MPLDVALKKK YYDEVRPELI RRFGYQNIWE VPRLEKVVIN QGLGEAKEDA RILEKASKEL
ALIAGQKPAI TRAKKSISNF KLRKGMPIGL RVTLRGDRMW IFLEKLLSVA LPRIRDFRGL
NPNSFDGRGN YNLGLKEQLI FPEITYDMVD VPRGMDIAVV TTAKTDEEAK ALLELLGFPF
RK
