ID   RL23_STRS7              Reviewed;          98 AA.
AC   C0MCB2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-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=SZO_00520;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(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}.
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DR   EMBL; FM204884; CAW97648.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MCB2; -.
DR   SMR; C0MCB2; -.
DR   EnsemblBacteria; CAW97648; CAW97648; SZO_00520.
DR   KEGG; seq:SZO_00520; -.
DR   eggNOG; COG0089; Bacteria.
DR   HOGENOM; CLU_037562_3_2_9; -.
DR   OMA; FEVDHRA; -.
DR   Proteomes; UP000001368; 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..98
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_1000215045"
SQ   SEQUENCE   98 AA;  10840 MW;  C4CAD53046C1CCE9 CRC64;
     MNLYDVIKKP VITEKSMYAL EEGKYTFEVD TRAHKLLIKQ AVEAAFDGVK VASVNTVNVK
     PKAKRVGRYT GFTSKTKKAI ITLTADSKAI ELFAAEAE