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Database: UniProt
Entry: A0A1D9FIT0_9CLOT
LinkDB: A0A1D9FIT0_9CLOT
Original site: A0A1D9FIT0_9CLOT 
ID   A0A1D9FIT0_9CLOT        Unreviewed;       103 AA.
AC   A0A1D9FIT0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Large ribosomal subunit protein uL24 {ECO:0000256|ARBA:ARBA00035206, ECO:0000256|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000256|HAMAP-Rule:MF_01326};
GN   ORFNames=BJL90_03765 {ECO:0000313|EMBL:AOY75094.1};
OS   Clostridium formicaceticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1497 {ECO:0000313|EMBL:AOY75094.1, ECO:0000313|Proteomes:UP000177894};
RN   [1] {ECO:0000313|EMBL:AOY75094.1, ECO:0000313|Proteomes:UP000177894}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27076 {ECO:0000313|EMBL:AOY75094.1,
RC   ECO:0000313|Proteomes:UP000177894};
RA   Bao T., Cheng C., Zhao J., Yang S.-T., Wang J., Wang M.;
RT   "Complete Genome Sequence of Acetogen Clostridium formicoaceticum ATCC
RT   27076.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01326}.
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:0000256|HAMAP-Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000256|ARBA:ARBA00010618, ECO:0000256|HAMAP-Rule:MF_01326}.
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DR   EMBL; CP017603; AOY75094.1; -; Genomic_DNA.
DR   RefSeq; WP_070964278.1; NZ_CP020559.1.
DR   AlphaFoldDB; A0A1D9FIT0; -.
DR   STRING; 1497.BJL90_03765; -.
DR   KEGG; cfm:BJL90_03765; -.
DR   OrthoDB; 9807419at2; -.
DR   Proteomes; UP000177894; Chromosome.
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; 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; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR003256; Ribosomal_uL24.
DR   InterPro; IPR041988; Ribosomal_uL24_KOW.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   NCBIfam; TIGR01079; rplX_bact; 1.
DR   PANTHER; PTHR12903:SF0; 39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF17136; ribosomal_L24; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW   ECO:0000313|EMBL:AOY75094.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT   DOMAIN          2..29
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
SQ   SEQUENCE   103 AA;  11438 MW;  2850B84DA464DE89 CRC64;
     MRIKKGDTVV VIAGKDKSKV GKVLQVLPKV NRVIVEGVNM VTKHQKPNPR TQQGGIIRHE
     APIHASNVMF FEKKANQGVR VGYKLLQNGE KVRISKKTGE VLD
//
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