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Database: UniProt
Entry: A0A0K2G9N2_NITMO
LinkDB: A0A0K2G9N2_NITMO
Original site: A0A0K2G9N2_NITMO 
ID   A0A0K2G9N2_NITMO        Unreviewed;       121 AA.
AC   A0A0K2G9N2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ALA57650.1};
GN   ORFNames=NITMOv2_1222 {ECO:0000313|EMBL:ALA57650.1};
OS   Nitrospira moscoviensis.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA57650.1, ECO:0000313|Proteomes:UP000069205};
RN   [1] {ECO:0000313|EMBL:ALA57650.1, ECO:0000313|Proteomes:UP000069205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA57650.1,
RC   ECO:0000313|Proteomes:UP000069205};
RX   PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA   Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA   Nielsen P.H., Wagner M., Daims H.;
RT   "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT   from the genus Nitrospira.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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; CP011801; ALA57650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K2G9N2; -.
DR   STRING; 42253.NITMOv2_1222; -.
DR   KEGG; nmv:NITMOv2_1222; -.
DR   PATRIC; fig|42253.5.peg.1203; -.
DR   OrthoDB; 9810939at2; -.
DR   Proteomes; UP000069205; 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:UP000069205};
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   121 AA;  13439 MW;  9F4CF2865AB6890B CRC64;
     MNTAEKERQL ERRRRRVRQR IMGTPERPRL NVFRSSAHIY AQIIDDIKGT TLAAASSLDK
     SLRTSLKSTS SIEGAKAVGK LLADRAKAAK ITAVVFDRGG RMYHGRIKAL AEASREGGLQ
     F
//
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