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RL23_TRIEI
ID   RL23_TRIEI              Reviewed;         101 AA.
AC   Q110A9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, 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};
GN   Synonyms=rpl23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=Tery_3010;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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: 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; CP000393; ABG52165.1; -; Genomic_DNA.
DR   RefSeq; WP_011612520.1; NC_008312.1.
DR   AlphaFoldDB; Q110A9; -.
DR   SMR; Q110A9; -.
DR   STRING; 203124.Tery_3010; -.
DR   EnsemblBacteria; ABG52165; ABG52165; Tery_3010.
DR   KEGG; ter:Tery_3010; -.
DR   eggNOG; COG0089; Bacteria.
DR   HOGENOM; CLU_037562_3_2_3; -.
DR   OMA; FEVDHRA; -.
DR   OrthoDB; 1978865at2; -.
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..101
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_0000272867"
SQ   SEQUENCE   101 AA;  11811 MW;  4A93789085FF7405 CRC64;
     MKLDSRDLVD IIKNPVVTEK ATRLMELNQY TFDVDPRATK PMIKQVIEQI FEVKVIGINT
     LNLPRKKRRV GKYIGFKPRY KRAIVTLEDG EPIRKVLFPD L
 
 
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