RL19_ENTFA
ID RL19_ENTFA Reviewed; 115 AA.
AC Q833P5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=50S ribosomal protein L19 {ECO:0000255|HAMAP-Rule:MF_00402};
GN Name=rplS {ECO:0000255|HAMAP-Rule:MF_00402}; OrderedLocusNames=EF_1898;
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: This protein is located at the 30S-50S ribosomal subunit
CC interface and may play a role in the structure and function of the
CC aminoacyl-tRNA binding site. {ECO:0000255|HAMAP-Rule:MF_00402}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.
CC {ECO:0000255|HAMAP-Rule:MF_00402}.
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DR EMBL; AE016830; AAO81650.1; -; Genomic_DNA.
DR RefSeq; NP_815580.1; NC_004668.1.
DR RefSeq; WP_002357176.1; NZ_KE136528.1.
DR PDB; 6WU9; EM; 2.90 A; Q=2-115.
DR PDB; 7P7R; EM; 2.90 A; S=1-115.
DR PDBsum; 6WU9; -.
DR PDBsum; 7P7R; -.
DR AlphaFoldDB; Q833P5; -.
DR SMR; Q833P5; -.
DR STRING; 226185.EF_1898; -.
DR EnsemblBacteria; AAO81650; AAO81650; EF_1898.
DR GeneID; 66474860; -.
DR KEGG; efa:EF1898; -.
DR PATRIC; fig|226185.45.peg.1618; -.
DR eggNOG; COG0335; Bacteria.
DR HOGENOM; CLU_103507_2_1_9; -.
DR OMA; TITVYYE; -.
DR PRO; PR:Q833P5; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.790; -; 1.
DR HAMAP; MF_00402; Ribosomal_L19; 1.
DR InterPro; IPR038657; L19_sf.
DR InterPro; IPR001857; Ribosomal_L19.
DR InterPro; IPR018257; Ribosomal_L19_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR15680; PTHR15680; 1.
DR Pfam; PF01245; Ribosomal_L19; 1.
DR PIRSF; PIRSF002191; Ribosomal_L19; 1.
DR PRINTS; PR00061; RIBOSOMALL19.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01024; rplS_bact; 1.
DR PROSITE; PS01015; RIBOSOMAL_L19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..115
FT /note="50S ribosomal protein L19"
FT /id="PRO_0000163454"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6WU9"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6WU9"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:6WU9"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:6WU9"
SQ SEQUENCE 115 AA; 13217 MW; BCD531F6BC28B64D CRC64;
MNPLIQELTQ EQLRTDIPAF RPGDTVRVHA KVVEGTRERI QLFEGVVIKR RGAGISETYT
VRKVSNGVGV ERTFPLHTPR VAQIEVVRYG KVRRAKLYYL RALHGKAARI KEIRR
