RL24_BACSH
ID RL24_BACSH Reviewed; 103 AA.
AC E0TZF9; P12876;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=50S ribosomal protein L24;
GN Name=rplX; OrderedLocusNames=BSUW23_00645;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=1556555; DOI=10.1099/00221287-138-1-39;
RA Sharp P.M., Nolan N.C., Ni Cholmain N., Devine K.M.;
RT "DNA sequence variability at the rplX locus of Bacillus subtilis.";
RL J. Gen. Microbiol. 138:39-45(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(2011).
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:0000250}.
CC -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC tunnel on the outside of the subunit. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
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DR EMBL; M81749; AAB59024.1; -; Genomic_DNA.
DR EMBL; CP002183; ADM36187.1; -; Genomic_DNA.
DR PIR; S05993; R5BS2B.
DR RefSeq; WP_003156486.1; NC_014479.1.
DR AlphaFoldDB; E0TZF9; -.
DR SMR; E0TZF9; -.
DR EnsemblBacteria; ADM36187; ADM36187; BSUW23_00645.
DR GeneID; 64301965; -.
DR GeneID; 66327852; -.
DR KEGG; bss:BSUW23_00645; -.
DR HOGENOM; CLU_093315_2_0_9; -.
DR OMA; HVKPTQE; -.
DR Proteomes; UP000002233; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; 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 DNA-binding; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..103
FT /note="50S ribosomal protein L24"
FT /id="PRO_0000403663"
FT CONFLICT 12
FT /note="I -> T (in Ref. 1; AAB59024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11142 MW; BB635A9CBD673EF1 CRC64;
MHVKKGDKVM VISGKDKGKQ GTILAAFPKK DRVLVEGVNM VKKHSKPTQA NPQGGISNQE
APIHVSNVMP LDPKTGEVTR VGYKVEDGKK VRVAKKSGQV LDK