ID   RL24_METI4              Reviewed;         106 AA.
AC   B3E0J5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; OrderedLocusNames=Minf_0694;
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum.
OX   NCBI_TaxID=481448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4;
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC       the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01326}.
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DR   EMBL; CP000975; ACD82749.1; -; Genomic_DNA.
DR   RefSeq; WP_012463031.1; NC_010794.1.
DR   AlphaFoldDB; B3E0J5; -.
DR   SMR; B3E0J5; -.
DR   STRING; 481448.Minf_0694; -.
DR   EnsemblBacteria; ACD82749; ACD82749; Minf_0694.
DR   KEGG; min:Minf_0694; -.
DR   eggNOG; COG0198; Bacteria.
DR   HOGENOM; CLU_093315_2_2_0; -.
DR   OMA; EREFPIH; -.
DR   OrthoDB; 2040741at2; -.
DR   Proteomes; UP000009149; Chromosome.
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; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR041988; KOW_RPL26/RPL24.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR003256; Ribosomal_L24.
DR   InterPro; IPR005825; Ribosomal_L24/26_CS.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR12903; PTHR12903; 1.
DR   Pfam; PF17136; ribosomal_L24; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01079; rplX_bact; 1.
DR   PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..106
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_0000355694"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   106 AA;  11925 MW;  57F8DD67BA091787 CRC64;
     MNKRAKSKNR EPLRKSPVKR GDEVVVITGS ERGKRGKVLK VLRNTHKVIV EGIKMVKKAV
     RPSQDNPKGG IVEKEATIAI SNVMLASKWE KRQEKKKVAV EKKEQG