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Database: UniProt
Entry: A0A3S9NXI7_9BACT
LinkDB: A0A3S9NXI7_9BACT
Original site: A0A3S9NXI7_9BACT 
ID   A0A3S9NXI7_9BACT        Unreviewed;       117 AA.
AC   A0A3S9NXI7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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=EI427_00150 {ECO:0000313|EMBL:AZQ60671.1};
OS   Flammeovirga pectinis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ60671.1, ECO:0000313|Proteomes:UP000267268};
RN   [1] {ECO:0000313|EMBL:AZQ60671.1, ECO:0000313|Proteomes:UP000267268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L12M1 {ECO:0000313|EMBL:AZQ60671.1,
RC   ECO:0000313|Proteomes:UP000267268};
RA   Bae J.-W., Jeong Y.-S., Kang W.;
RT   "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT   scallop, Patinopecten yessoensis.";
RL   Submitted (DEC-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; CP034562; AZQ60671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9NXI7; -.
DR   KEGG; fll:EI427_00150; -.
DR   OrthoDB; 9810939at2; -.
DR   Proteomes; UP000267268; Chromosome 1.
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:UP000267268};
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   117 AA;  12748 MW;  62E83D8660032FB5 CRC64;
     MATKKDLRRL RIKRGIRKKV SGTPERPRLS VYKSNTAIYV QLIDDLNGRT VAAISSREIN
     AESKSTNIAL ASEVGKKVAE KATAAGISTV VFDRNGYLYH GKVKALAEGA REGGLKF
//
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