ID T2G299_ECOLX Unreviewed; 100 AA. AC T2G299; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 26-NOV-2014, entry version 11. DE RecName: Full=50S ribosomal protein L23 {ECO:0000256|HAMAP-Rule:MF_01369, ECO:0000256|RuleBase:RU003935}; GN Name=rplW {ECO:0000256|HAMAP-Rule:MF_01369, GN ECO:0000313|EMBL:AGW10403.1}; GN ORFNames=LY180_17090 {ECO:0000313|EMBL:AGW10403.1}; OS Escherichia coli LY180. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1335916 {ECO:0000313|EMBL:AGW10403.1, ECO:0000313|Proteomes:UP000016700}; RN [1] {ECO:0000313|EMBL:AGW10403.1, ECO:0000313|Proteomes:UP000016700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LY180 {ECO:0000313|EMBL:AGW10403.1}; RX PubMed=25063650; DOI=10.1128/AEM.01913-14; RA Geddes R.D., Wang X., Yomano L.P., Miller E.N., Zheng H., RA Shanmugam K.T., Ingram L.O.; RT "Polyamine Transporters and Polyamines Increase Furfural Tolerance RT during Xylose Fermentation with Ethanologenic Escherichia coli Strain RT LY180."; RL Appl. Environ. Microbiol. 80:5955-5964(2014). CC -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. CC One of the proteins that surrounds the polypeptide exit tunnel on CC the outside of the ribosome. Forms the main docking site for CC trigger factor binding to the ribosome. {ECO:0000256|HAMAP- CC Rule:MF_01369}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, CC and trigger factor when it is bound to the ribosome. CC {ECO:0000256|HAMAP-Rule:MF_01369}. CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family. CC {ECO:0000256|HAMAP-Rule:MF_01369, ECO:0000256|RuleBase:RU003934}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP006584; AGW10403.1; -; Genomic_DNA. DR RefSeq; YP_008566472.1; NC_022364.1. DR ProteinModelPortal; T2G299; -. DR SMR; T2G299; 7-98. DR EnsemblBacteria; AGW10403; AGW10403; LY180_17090. DR GeneID; 16981088; -. DR KEGG; ecol:LY180_17090; -. DR KO; K02892; -. DR OMA; FGRRSDW; -. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR InterPro; IPR001014; Ribosomal_L23/L25_CS. DR InterPro; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016700}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01369, KW ECO:0000256|RuleBase:RU003934}; KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01369, KW ECO:0000256|RuleBase:RU003934}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01369, KW ECO:0000256|RuleBase:RU003935}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01369, KW ECO:0000256|RuleBase:RU003935}. SQ SEQUENCE 100 AA; 11199 MW; 30CD1D77CC7CF9EB CRC64; MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE //