RL5_SACEN
ID RL5_SACEN Reviewed; 187 AA.
AC A4FPL3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=SACE_6824;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(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. 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; AM420293; CAM05988.1; -; Genomic_DNA.
DR RefSeq; WP_009948643.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FPL3; -.
DR SMR; A4FPL3; -.
DR STRING; 405948.SACE_6824; -.
DR PRIDE; A4FPL3; -.
DR EnsemblBacteria; CAM05988; CAM05988; SACE_6824.
DR KEGG; sen:SACE_6824; -.
DR eggNOG; COG0094; Bacteria.
DR HOGENOM; CLU_061015_2_1_11; -.
DR OMA; ERMYAFL; -.
DR OrthoDB; 1456375at2; -.
DR Proteomes; UP000006728; 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_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; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..187
FT /note="50S ribosomal protein L5"
FT /id="PRO_1000052818"
SQ SEQUENCE 187 AA; 21281 MW; 1A5401745FE4BF95 CRC64;
MTTTEKIVPR LKTRYRDEIR QALNEEFHYS NAMQVPGVVK VVVNMGVGDA ARDSKLIEGA
VRDLATITGQ KPEIRKARKS IAQFKLREGM PIGARVTLRG DRMWEFIDRL VTIALPRIRD
FRGLSGKQFD GKGNYTFGLN EQSMFHEIDP DSIDRPRGMD ITVVTTANTD EEGRVLLRRL
GFPFKEN
