ID   RL24_HELAH              Reviewed;          73 AA.
AC   Q17ZC7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; OrderedLocusNames=Hac_0147;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ98999.1; -; Genomic_DNA.
DR   RefSeq; WP_000834236.1; NC_008229.1.
DR   AlphaFoldDB; Q17ZC7; -.
DR   SMR; Q17ZC7; -.
DR   STRING; 382638.Hac_0147; -.
DR   EnsemblBacteria; CAJ98999; CAJ98999; Hac_0147.
DR   KEGG; hac:Hac_0147; -.
DR   eggNOG; COG0198; Bacteria.
DR   HOGENOM; CLU_093315_3_0_7; -.
DR   OMA; EREFPIH; -.
DR   OrthoDB; 2040741at2; -.
DR   BioCyc; HACI382638:HAC_RS00635-MON; -.
DR   Proteomes; UP000000775; 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; PF00467; KOW; 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..73
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_1000142002"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   73 AA;  7938 MW;  E073541946550794 CRC64;
     MKSEIKKNDM VKVIAGDDKG KVAKVLAVLP KTSQVIVEGC KVVKKAIKPT DDNPKGGFIH
     KEKPMHISNV KKA