ID A0A0H4VB57_9SPHN Unreviewed; 106 AA.
AC A0A0H4VB57;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=CP97_07170 {ECO:0000313|EMBL:AKQ41852.1};
OS Aurantiacibacter atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ41852.1, ECO:0000313|Proteomes:UP000059113};
RN [1] {ECO:0000313|EMBL:AKQ41852.1, ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RX PubMed=26220886; DOI=10.1099/ijsem.0.000481;
RA Zhuang L., Liu Y., Wang L., Wang W., Shao Z.;
RT "Erythrobacter atlanticus sp. nov., a bacterium from ocean sediment able to
RT degrade polycyclic aromatic hydrocarbons.";
RL Int. J. Syst. Evol. Microbiol. 65:3714-3719(2015).
RN [2] {ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RA Zhuang L., Liu Y., Shao Z.;
RT "The complete genome sequence of Erythrobacter sp. s21-N3.";
RL Submitted (APR-2015) 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,
CC ECO:0000256|RuleBase:RU003477}.
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DR EMBL; CP011310; AKQ41852.1; -; Genomic_DNA.
DR RefSeq; WP_048885367.1; NZ_CP011310.1.
DR AlphaFoldDB; A0A0H4VB57; -.
DR STRING; 1648404.CP97_07170; -.
DR KEGG; ery:CP97_07170; -.
DR PATRIC; fig|1648404.4.peg.1492; -.
DR OrthoDB; 9807419at2; -.
DR Proteomes; UP000059113; 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; IPR005825; Ribosomal_uL24_CS.
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.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000059113};
KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326,
KW ECO:0000256|RuleBase:RU003477};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW ECO:0000256|RuleBase:RU003477};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT DOMAIN 5..32
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
SQ SEQUENCE 106 AA; 11184 MW; 4B4ABB3592A3F65F CRC64;
MAAAKIKKGD NVVVLSGKDK GQTGTVQQVM PKDGKVLVDG VNVMTRHRKP SQANPQGGID
RVPAPIALCK IALADPKDGK PTRVRFEEKG GKKVRVAVKS GETIDG
//
