ID   RL23_GEOSE              Reviewed;          95 AA.
AC   P04454; O82994;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4018095; DOI=10.1111/j.1432-1033.1985.tb09049.x;
RA   Kimura M., Kimura J., Ashman K.;
RT   "The complete primary structure of ribosomal proteins L1, L14, L15, L23,
RT   L24 and L29 from Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 150:491-497(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kimura M.;
RT   "Nucleotide sequence of the genes encoding the ribosomal proteins L23 and
RT   L2 from the Bacillus stearothermophilus ribosome.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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: Contacts protein L29, and trigger factor when it is bound to
CC       the ribosome (By similarity). Part of the 50S ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR   EMBL; AB015722; BAA31209.1; -; Genomic_DNA.
DR   PIR; A02815; R5BS23.
DR   AlphaFoldDB; P04454; -.
DR   SMR; P04454; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..95
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_0000129397"
FT   CONFLICT        52
FT                   /note="E -> A (in Ref. 2; BAA31209)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="K -> R (in Ref. 2; BAA31209)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   95 AA;  11083 MW;  FF24F65D770EFF7F CRC64;
     MKDPRDIIKR PIITENTMNL IGQKKYTFEV DVKANKTEVK DAVEKIFGVK VEKVNIMNYK
     GKFKRVGRYS GYTNRRKKAI VTLTPDSKEI ELFEV