RL5_CUTAK
ID RL5_CUTAK Reviewed; 210 AA.
AC Q6A6N8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=PPA1850;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT83575.1; -; Genomic_DNA.
DR RefSeq; WP_011183934.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A6N8; -.
DR SMR; Q6A6N8; -.
DR STRING; 267747.PPA1850; -.
DR PRIDE; Q6A6N8; -.
DR EnsemblBacteria; AAT83575; AAT83575; PPA1850.
DR KEGG; pac:PPA1850; -.
DR PATRIC; fig|267747.3.peg.1906; -.
DR eggNOG; COG0094; Bacteria.
DR HOGENOM; CLU_061015_2_1_11; -.
DR OMA; ERMYAFL; -.
DR Proteomes; UP000000603; 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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT CHAIN 1..210
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000243040"
FT REGION 188..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23843 MW; C41A5979CDA6EFD5 CRC64;
MSTDAIAHEM PRLKKQYREQ IRAAMQEEFG YRNPMLIPGL EKIVVNMGVG DAAHDSKVMD
GAIRDITAIT GQKPQVTKAR KSIAQFKLRE GQPIGCHVTL RGDRMWEFAD RLLTLALPRI
RDFRGLNSNQ FDGKGNYTFG LSEQVMFLEI DQDKIVRIRG MDITFVTTAQ TNEEGKALLK
HLGFPFKAKD DPKKAKTKRG PAYYAKKKKK