AC MF_01367; DC Protein; auto c? or or TR HAMAP; MF_01367; -; 1; level=0 XX Names: Ribosomal_uL14 XX case and not ID RL14 DE RecName: Full=Large ribosomal subunit protein uL14; GN Name=rplN; else case ID RL14 DE RecName: Full=Large ribosomal subunit protein uL14; GN Name=rplN; Synonyms=rpl14; else case ID RL14 DE RecName: Full=Large ribosomal subunit protein uL14; GN Name=rpl14; else case ID RK14 DE RecName: Full=Large ribosomal subunit protein uL14c; GN Name=rpl14; end case XX case CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in CC the 70S ribosome. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and CC together make contacts with the 16S rRNA in bridges B5 and B8. else case CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in CC the 70S ribosome. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L24e, part of which may contact the 16S rRNA in 2 CC intersubunit bridges. else case CC -!- FUNCTION: Binds to 23S rRNA. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family. XX DR PROSITE; PS00049; RIBOSOMAL_L14; 1; trigger=no DR Pfam; PF00238; Ribosomal_L14; 1; trigger=no DR NCBIfam; TIGR01067; RplN_bact; 1; trigger=no DR NCBIfam; TIGR03673; rpl14p_arch; 1; trigger=no XX KW Ribonucleoprotein KW Ribosomal protein KW RNA-binding KW rRNA-binding XX GO GO:0019843; F:rRNA binding GO GO:0006412; P:translation case GO GO:0009507; C:chloroplast end case XX Size: 119-182; Related: None; Template: Q9RXJ2; P0ADY3; Q5SHP8; P22450; Scope: Bacteria Archaea Plastid Fusion: Nter: None Cter: None Duplicate: in BARBK, LEPBL Plasmid: None Comments: In E.coli interaction of L14 with ribosomal silencing factor RsfS has been shown block formation of bridge B8, preventing association of 2 ribosomal subunits and thus causes ribosomal silencing. The same interaction is suspected to have the same effect in human mitochondrial ribosomes and maybe maize chloroplasts as well. It has not yet been propagated to all ribosomal proteins while waiting further experimental confirmation. XX # Revision 1.22 2023/09/22 //