ID   RL23_MESH2              Reviewed;         167 AA.
AC   Q601L3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=50S ribosomal protein L23;
GN   Name=rplW; OrderedLocusNames=mhp189;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC       trigger factor when it is bound to the ribosome (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000305}.
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DR   EMBL; AE017332; AAV27446.1; -; Genomic_DNA.
DR   RefSeq; WP_011206026.1; NC_006360.1.
DR   AlphaFoldDB; Q601L3; -.
DR   SMR; Q601L3; -.
DR   STRING; 295358.mhp189; -.
DR   EnsemblBacteria; AAV27446; AAV27446; mhp189.
DR   KEGG; mhy:mhp189; -.
DR   eggNOG; COG0089; Bacteria.
DR   HOGENOM; CLU_037562_1_0_14; -.
DR   OMA; GRFHGFT; -.
DR   PhylomeDB; Q601L3; -.
DR   Proteomes; UP000006822; 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; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..167
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_0000272775"
FT   REGION          1..97
FT                   /note="50S ribosomal protein L23"
FT   REGION          91..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..167
FT                   /note="Unknown"
FT   REGION          137..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   167 AA;  19040 MW;  A4866B8BC5725A1A CRC64;
     MNVNEIIKGP ILTEKSYQLM SSGVYSFKVS PKTNRSETKK AVEYIFNVKV EKVNIFTVPK
     KEKKLGKSKG FTTKYKKALV KLMPGYTINL FEDESPQDQK DSETVSENTE EKAKIAKKKA
     ELEAKNKEIA EKLAKKQAEL AKKESETNEN QEKKIENQTE NQENSAK