AC MF_01318; DC Protein; auto c? or TR HAMAP; MF_01318_B; -; 1; level=0 c? TR HAMAP; MF_01318_A; -; 1; level=0 XX Names: Ribosomal_uL1 XX case and not ID RL1 DE RecName: Full=Large ribosomal subunit protein uL1; GN Name=rplA; else case ID RL1 DE RecName: Full=Large ribosomal subunit protein uL1; GN Name=rplA; Synonyms=rpl1; else case ID RL1 DE RecName: Full=Large ribosomal subunit protein uL1; GN Name=rpl1; else case ID RK1 DE RecName: Full=Large ribosomal subunit protein uL1c; GN Name=rpl1; end case XX case CC -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in CC the ribosome, and is involved in E site tRNA release. CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it CC controls the translation of the L11 operon by binding to its mRNA. else case CC -!- FUNCTION: Binds directly to 23S rRNA. Probably involved in E site tRNA CC release. CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it CC controls the translation of its operon by binding to its mRNA. end case CC -!- SUBUNIT: Part of the 50S ribosomal subunit. case CC -!- FUNCTION: Binds directly to 23S rRNA. Might be involved in E site tRNA CC release. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family. XX DR Pfam; PF00687; Ribosomal_L1; 1; trigger=no DR NCBIfam; TIGR01169; RplA_bact; 1; trigger=no DR PROSITE; PS01199; RIBOSOMAL_L1; 1; trigger=no XX KW Ribonucleoprotein KW Ribosomal protein KW RNA-binding KW rRNA-binding case not KW Repressor KW Translation regulation KW tRNA-binding end case XX GO GO:0019843; F:rRNA binding GO GO:0006412; P:translation case GO GO:0009507; C:chloroplast end case XX FT None XX Size: 209-253; Related: None; Template: P0A7L0; Q5SLP7; P27150; P54050; O52704; P35024; Scope: Bacteria Archaea Plastid Fusion: Nter: None Cter: Duplicate: in CERS1 Plasmid: None Comments: C-terminal fusion in MALP2, quite atypical in NEOSM. Some of the Rickettsiales are about 15 residues shorter at the N-terminus. L1 proteins from thermophilic organisms have an approximately 10-fold higher affinity for their binding sites on both 23S rRNA and mRNA than do their mesophilic counterparts, maybe helping to explain the ribosome's greater stability in thermophiles. See: PubMed=9746351; Kohrer C., Mayer C., Neumair O., Grobner P., Piendl W.; "Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA."; Eur. J. Biochem. 256:97-105(1998). XX # Revision 1.35 2023/09/22 //