ID   RL18_MYCMM              Reviewed;         135 AA.
AC   B2HCT7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337};
GN   Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; OrderedLocusNames=MMAR_1051;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01337}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01337}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000854; ACC39509.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2HCT7; -.
DR   SMR; B2HCT7; -.
DR   STRING; 216594.MMAR_1051; -.
DR   EnsemblBacteria; ACC39509; ACC39509; MMAR_1051.
DR   KEGG; mmi:MMAR_1051; -.
DR   eggNOG; COG0256; Bacteria.
DR   HOGENOM; CLU_098841_0_1_11; -.
DR   OMA; NKQIYAQ; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   HAMAP; MF_01337_B; Ribosomal_L18_B; 1.
DR   InterPro; IPR005484; Ribosomal_L18.
DR   InterPro; IPR004389; Ribosomal_L18_bac-type.
DR   PANTHER; PTHR12899; PTHR12899; 1.
DR   Pfam; PF00861; Ribosomal_L18p; 1.
DR   TIGRFAMs; TIGR00060; L18_bact; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..135
FT                   /note="50S ribosomal protein L18"
FT                   /id="PRO_1000142692"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  14594 MW;  6A96CC1786B8F9F0 CRC64;
     MAQTQADTAA RKPVGQSVSA TRRVSRLRRH ARLRKRIAGT QQRPRLVVHR SARHIHVQLV
     NDANGTTVAA ASSIETDVRG LDGDKKARSV RVGQLIAERA KAAGIDTVVF DRGGYTYGGR
     IAALADAARE NGLKF