ID   RL18_HALMT              Reviewed;         184 AA.
AC   P50561; I3R7P0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337};
DE   AltName: Full=HmeL18;
GN   Name=rpl18 {ECO:0000255|HAMAP-Rule:MF_01337}; Synonyms=rplR;
GN   OrderedLocusNames=HFX_2569;
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX   PubMed=22843593; DOI=10.1128/jb.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-23.
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX   PubMed=8174557; DOI=10.1111/j.1432-1033.1994.tb18791.x;
RA   McDougall J., Wittmann-Liebold B.;
RT   "Comparative analysis of the protein components from 5S rRNA.protein
RT   complexes of halophilic archaebacteria.";
RL   Eur. J. Biochem. 221:779-785(1994).
CC   -!- FUNCTION: This is one of the proteins that binds and probably mediates
CC       the attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance. {ECO:0000255|HAMAP-
CC       Rule:MF_01337}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts the 5S and 23S
CC       rRNAs. {ECO:0000255|HAMAP-Rule:MF_01337}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01337}.
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DR   EMBL; CP001868; AFK20250.1; -; Genomic_DNA.
DR   PIR; F33084; F33084.
DR   RefSeq; WP_004060017.1; NZ_CP039139.1.
DR   AlphaFoldDB; P50561; -.
DR   SMR; P50561; -.
DR   STRING; 523841.HFX_2569; -.
DR   EnsemblBacteria; AFK20250; AFK20250; HFX_2569.
DR   GeneID; 40157538; -.
DR   KEGG; hme:HFX_2569; -.
DR   eggNOG; arCOG04088; Archaea.
DR   HOGENOM; CLU_056222_2_0_2; -.
DR   OMA; MAHGPRY; -.
DR   OrthoDB; 108717at2157; -.
DR   Proteomes; UP000006469; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR   InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR   PANTHER; PTHR23410; PTHR23410; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 2.
DR   PRINTS; PR00058; RIBOSOMALL5.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8174557"
FT   CHAIN           2..184
FT                   /note="50S ribosomal protein L18"
FT                   /id="PRO_0000131401"
SQ   SEQUENCE   184 AA;  20183 MW;  9608D14D7692CEB9 CRC64;
     MATGPRYKVP MRRRREVRTD YHQRLRLLKS GKPRLVARVS NKHVRAQLVT PGPQGDETHA
     AATSADLDEY GWEAPTGNLP SAYLTGYLAG IRALAAGVEE AVLDIGLNTA TPGNKVFAVQ
     EGAIDAGLEI PHNDAVLADW DRNRGVHIAE YAEQLDEPLY SGDFDATNLP EHFDEVLGNL
     QEDE