RL23_MYCLB
ID RL23_MYCLB Reviewed; 100 AA.
AC B8ZSB7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=MLBr01861;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(2009).
CC -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of
CC the proteins that surrounds the polypeptide exit tunnel on the outside
CC of the ribosome. Forms the main docking site for trigger factor binding
CC to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC trigger factor when it is bound to the ribosome. {ECO:0000255|HAMAP-
CC Rule:MF_01369}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000255|HAMAP-Rule:MF_01369}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM211192; CAR71957.1; -; Genomic_DNA.
DR RefSeq; WP_010908584.1; NC_011896.1.
DR AlphaFoldDB; B8ZSB7; -.
DR SMR; B8ZSB7; -.
DR EnsemblBacteria; CAR71957; CAR71957; MLBr01861.
DR KEGG; mlb:MLBr01861; -.
DR HOGENOM; CLU_037562_3_2_11; -.
DR OMA; FEVDHRA; -.
DR OrthoDB; 1978865at2; -.
DR Proteomes; UP000006900; 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 Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..100
FT /note="50S ribosomal protein L23"
FT /id="PRO_1000184096"
SQ SEQUENCE 100 AA; 10939 MW; 1A9254F7D639D1AF CRC64;
MATIADSRDI ILAPVISEKS YGLLDDNVYT FVVHPDSNKT QIKIAIEKIF SVKVASVNTS
NRKGKCKRTR TGFGRRKNTK RAIVTLAPGS KSIDLFGTPA