ID   RL23_CLOAB              Reviewed;          98 AA.
AC   Q97EI0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=CA_C3131;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81070.1; -; Genomic_DNA.
DR   PIR; C97285; C97285.
DR   RefSeq; NP_349730.1; NC_003030.1.
DR   RefSeq; WP_010966410.1; NC_003030.1.
DR   AlphaFoldDB; Q97EI0; -.
DR   SMR; Q97EI0; -.
DR   STRING; 272562.CA_C3131; -.
DR   EnsemblBacteria; AAK81070; AAK81070; CA_C3131.
DR   GeneID; 44999618; -.
DR   KEGG; cac:CA_C3131; -.
DR   PATRIC; fig|272562.8.peg.3314; -.
DR   eggNOG; COG0089; Bacteria.
DR   HOGENOM; CLU_037562_3_2_9; -.
DR   OMA; FEVDHRA; -.
DR   OrthoDB; 1978865at2; -.
DR   Proteomes; UP000000814; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..98
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_1000068062"
SQ   SEQUENCE   98 AA;  11140 MW;  78FC40553A408123 CRC64;
     MYTNSHDIIR KPVITEKSMA EMADKKYTFI VDPHANKVQI KKAIEEVFGV KVEKVNTSNI
     LGKTKRVGVH VGKRADYKKA IVKLTEDSKA IEFFEGMQ