RL23_FRATN
ID RL23_FRATN Reviewed; 99 AA.
AC A0Q4I5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=FTN_0241;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
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}.
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DR EMBL; CP000439; ABK89150.1; -; Genomic_DNA.
DR RefSeq; WP_003027200.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q4I5; -.
DR SMR; A0Q4I5; -.
DR EnsemblBacteria; ABK89150; ABK89150; FTN_0241.
DR KEGG; ftn:FTN_0241; -.
DR OMA; FEVDHRA; -.
DR OrthoDB; 1978865at2; -.
DR BioCyc; FTUL401614:G1G75-252-MON; -.
DR Proteomes; UP000000762; 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..99
FT /note="50S ribosomal protein L23"
FT /id="PRO_1000068079"
SQ SEQUENCE 99 AA; 11136 MW; 5A456B109D0B4713 CRC64;
MSSQEKLLKT VIRPHVSDKT YGLSDANSTI VFEVARFANK QDVKNAVEKL FEVKVESVNI
LNVKGKARRF GRVEGRTKAW KKAYVKLAEG HDINFVGAE