RL5_SULMW
ID RL5_SULMW Reviewed; 186 AA.
AC A8Z678;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=SMGWSS_232;
OS Sulcia muelleri (strain GWSS).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=444179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWSS;
RX PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA McCutcheon J.P., Moran N.A.;
RT "Parallel genomic evolution and metabolic interdependence in an ancient
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(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; CP000770; ABS30629.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Z678; -.
DR SMR; A8Z678; -.
DR STRING; 444179.SMGWSS_232; -.
DR EnsemblBacteria; ABS30629; ABS30629; SMGWSS_232.
DR KEGG; smg:SMGWSS_232; -.
DR HOGENOM; CLU_061015_2_1_10; -.
DR OMA; ERMYAFL; -.
DR Proteomes; UP000000781; 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..186
FT /note="50S ribosomal protein L5"
FT /id="PRO_1000142461"
SQ SEQUENCE 186 AA; 21515 MW; 5E094B22BDF4391D CRC64;
MNYCPRPKYL YKKKIINKLI EKFNYKSVMQ VPKLKKIVIN QGINVLIYDN KTINNAINNI
TAITGQKAIY CLSKRDESGF KLRKGTPISI KVTLRRDIMY EFLDRLINIA LPRVRDFVGV
NKNSFDGEGN YNLGISEQII FPEINTDSLK NNFGMNITFV TSSKKNKEAK YLLYLFGLPF
KTKKNV