ID D3HPL9_LEGLN Unreviewed; 119 AA.
AC D3HPL9;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000256|ARBA:ARBA00035197, ECO:0000256|HAMAP-Rule:MF_01337};
GN Name=rplR {ECO:0000256|HAMAP-Rule:MF_01337,
GN ECO:0000313|EMBL:CBJ10833.1};
GN OrderedLocusNames=LLO_0502 {ECO:0000313|EMBL:CBJ10833.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10833.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ10833.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10833.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- FUNCTION: This is one of the proteins that bind and probably mediate
CC the attachment of the 5S RNA into the large ribosomal subunit, where it
CC forms part of the central protuberance. {ECO:0000256|HAMAP-
CC Rule:MF_01337}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01337}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000256|ARBA:ARBA00007116, ECO:0000256|HAMAP-Rule:MF_01337}.
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DR EMBL; FN650140; CBJ10833.1; -; Genomic_DNA.
DR RefSeq; WP_003633064.1; NC_013861.1.
DR AlphaFoldDB; D3HPL9; -.
DR STRING; 661367.LLO_0502; -.
DR KEGG; llo:LLO_0502; -.
DR eggNOG; COG0256; Bacteria.
DR HOGENOM; CLU_098841_0_1_6; -.
DR OrthoDB; 9810939at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00432; Ribosomal_L18_L5e; 1.
DR Gene3D; 3.30.420.100; -; 1.
DR HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR InterPro; IPR005484; Ribosomal_uL18.
DR InterPro; IPR004389; Ribosomal_uL18_bac-type.
DR NCBIfam; TIGR00060; L18_bact; 1.
DR PANTHER; PTHR12899; 39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12899:SF3; 39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL; 1.
DR Pfam; PF00861; Ribosomal_L18p; 1.
DR SUPFAM; SSF53137; Translational machinery components; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01337};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01337};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01337};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01337}.
SQ SEQUENCE 119 AA; 13112 MW; 14A44BB07DD742C7 CRC64;
MNKQNSRIRR GLKAKALIRK SGRVRLVVHR SGLHIYSQIV RADELGDKVL VACSTNDKEI
RASLSGKCKV EQANLVGKLL GKRASEHGIT EVAFDRAGYK YHGRVKALAE GAREAGLDF
//
