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RL5_SYNC1
ID   RL5_SYNC1               Reviewed;         184 AA.
AC   Q3A6N5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=Pcar_0713;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000142; ABA87972.1; -; Genomic_DNA.
DR   RefSeq; WP_011340415.1; NC_007498.2.
DR   AlphaFoldDB; Q3A6N5; -.
DR   SMR; Q3A6N5; -.
DR   STRING; 338963.Pcar_0713; -.
DR   PRIDE; Q3A6N5; -.
DR   EnsemblBacteria; ABA87972; ABA87972; Pcar_0713.
DR   KEGG; pca:Pcar_0713; -.
DR   eggNOG; COG0094; Bacteria.
DR   HOGENOM; CLU_061015_2_1_7; -.
DR   OMA; ERMYAFL; -.
DR   OrthoDB; 1456375at2; -.
DR   Proteomes; UP000002534; 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; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..184
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000243036"
SQ   SEQUENCE   184 AA;  20605 MW;  C13887AD74A03456 CRC64;
     MGARLKEVYS TEIAPALVKR LQLKNVMEVP RVEKVVLNMG LGEAIQNIKV LESAVEELTR
     ICGQKPVVTK AKKSIAQFKL REGMPIGCMV TLRRDKAYEF LDRLINVALP RVRDFKGVSK
     KGFDGRGNYT LGIREQLIFP EIDLEKVDKV KGLNVTIVTT AKNDEEGYAL MEAIGMPFPK
     KAQD
 
 
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