RL20_ENTFA
ID RL20_ENTFA Reviewed; 119 AA.
AC Q837C7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382};
GN Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; OrderedLocusNames=EF_0916;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the
CC in vitro assembly process of the 50S ribosomal subunit. It is not
CC involved in the protein synthesizing functions of that subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00382}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.
CC {ECO:0000255|HAMAP-Rule:MF_00382}.
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DR EMBL; AE016830; AAO80724.1; -; Genomic_DNA.
DR RefSeq; NP_814654.1; NC_004668.1.
DR RefSeq; WP_002355799.1; NZ_KE136527.1.
DR PDB; 6WU9; EM; 2.90 A; R=2-119.
DR PDB; 7P7R; EM; 2.90 A; T=1-119.
DR PDBsum; 6WU9; -.
DR PDBsum; 7P7R; -.
DR AlphaFoldDB; Q837C7; -.
DR SMR; Q837C7; -.
DR STRING; 226185.EF_0916; -.
DR EnsemblBacteria; AAO80724; AAO80724; EF_0916.
DR GeneID; 60893253; -.
DR KEGG; efa:EF0916; -.
DR PATRIC; fig|226185.45.peg.3124; -.
DR eggNOG; COG0292; Bacteria.
DR HOGENOM; CLU_123265_0_1_9; -.
DR OMA; GRRKNVW; -.
DR Proteomes; UP000001415; 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:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd07026; Ribosomal_L20; 1.
DR Gene3D; 1.10.1900.20; -; 1.
DR HAMAP; MF_00382; Ribosomal_L20; 1.
DR InterPro; IPR005813; Ribosomal_L20.
DR InterPro; IPR035566; Ribosomal_protein_L20_C.
DR PANTHER; PTHR10986; PTHR10986; 1.
DR Pfam; PF00453; Ribosomal_L20; 1.
DR PRINTS; PR00062; RIBOSOMALL20.
DR SUPFAM; SSF74731; SSF74731; 1.
DR TIGRFAMs; TIGR01032; rplT_bact; 1.
DR PROSITE; PS00937; RIBOSOMAL_L20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..119
FT /note="50S ribosomal protein L20"
FT /id="PRO_0000177159"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:6WU9"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 32..69
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:6WU9"
SQ SEQUENCE 119 AA; 13643 MW; 54B9E8EF359488B4 CRC64;
MARVKGGTVT RKRRKKVLKL AKGYYGSKHT LFKSAKEQVM NSYYYAFRDR RQKKRDFRKL
WIARINAAAR MNGLSYSKLM HGLKLAEIDI NRKMLADLAV NDAAAFTALA EQAKDALSK