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Database: UniProt
Entry: A0A1E5CUU2_9VIBR
LinkDB: A0A1E5CUU2_9VIBR
Original site: A0A1E5CUU2_9VIBR 
ID   A0A1E5CUU2_9VIBR        Unreviewed;       117 AA.
AC   A0A1E5CUU2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=A130_06675 {ECO:0000313|EMBL:OEE73679.1};
OS   Vibrio genomosp. F6 str. FF-238.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE73679.1, ECO:0000313|Proteomes:UP000094165};
RN   [1] {ECO:0000313|EMBL:OEE73679.1, ECO:0000313|Proteomes:UP000094165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FF-238 {ECO:0000313|EMBL:OEE73679.1,
RC   ECO:0000313|Proteomes:UP000094165};
RX   PubMed=22955834; DOI=10.1126/science.1219385;
RA   Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA   Le Roux F., Mincer T., Polz M.F.;
RT   "Ecological populations of bacteria act as socially cohesive units of
RT   antibiotic production and resistance.";
RL   Science 337:1228-1231(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEE73679.1}.
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DR   EMBL; AJYW02000222; OEE73679.1; -; Genomic_DNA.
DR   RefSeq; WP_017051442.1; NZ_AJYW02000222.1.
DR   AlphaFoldDB; A0A1E5CUU2; -.
DR   Proteomes; UP000094165; Unassembled WGS sequence.
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:UP000094165};
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;  12625 MW;  2B0F96DEDF6AB964 CRC64;
     MDKKASRIRR ATRARRKIAE LGATRLVVHR TPRHVYAQVI ASNGSEVIAA ASTVEKAIRE
     QVKNTGNVDA AKAVGKAIAE RAIEKGISNV AFDRSGFQYH GRVAALADSA REAGLKF
//
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