ID A0A2R4T6J5_9ACTN Unreviewed; 127 AA.
AC A0A2R4T6J5;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ORFNames=SLUN_23930 {ECO:0000313|EMBL:AVZ74765.1};
OS Streptomyces lunaelactis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1535768 {ECO:0000313|EMBL:AVZ74765.1, ECO:0000313|Proteomes:UP000244201};
RN [1] {ECO:0000313|EMBL:AVZ74765.1, ECO:0000313|Proteomes:UP000244201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM109 {ECO:0000313|EMBL:AVZ74765.1,
RC ECO:0000313|Proteomes:UP000244201};
RA Naome A., Martinet L., Maciejewska M., Anderssen S., Adam D., Tenconi E.,
RA Deflandre B., Arguelles-Arias A., Calusinska M., Copieters W., Karim L.,
RA Hanikenne M., Baurain D., van Wezel G., Smargiasso N., de Pauw E.,
RA Delfosse P., Rigali S.;
RT "Complete genome sequence of Streptomyces lunaelactis MM109T, a Ferroverdin
RT A producer isolated from cave moonmilk deposits.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; CP026304; AVZ74765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4T6J5; -.
DR KEGG; slk:SLUN_23930; -.
DR OrthoDB; 9810939at2; -.
DR Proteomes; UP000244201; 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:UP000244201};
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 127 AA; 13462 MW; EAD9F0DBC3701C96 CRC64;
MAYGVKIAKG DAYKRAAIKR RHIRVRKHVS GTPVRPRLVV TRSNRNIVAQ VIDDIAGHTL
ASASTLDTSI RGGEGDKSAQ AKQVGALVAE RAKAAGVETV VFDRGGNRYA GRIAALADAA
REAGLKF
//