Accession	MF_01318
Dates	22-JUL-2003 (Created) 30-JUN-2008 (Last updated, Version 23)

Data class

Protein

Predictors

HAMAP; MF_01318_B; [distribution of match scores in UniProtKB];[seed alignment for MF_01318_B]

Predictors

HAMAP; MF_01318_A; [distribution of match scores in UniProtKB];[seed alignment for MF_01318_A]

Identifier

RL1

Protein name

RecName: Full=50S ribosomal protein L1;

Gene name

rplA

Identifier

RL1

Protein name

RecName: Full=50S ribosomal protein L1;

Gene name

rplA, rpl1

Identifier

RL1

Protein name

RecName: Full=50S ribosomal protein L1P;

Gene name

rpl1p

Identifier

RK1

Protein name

RecName: Full=50S ribosomal protein L1, chloroplastic;

Gene name

rpl1

FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity).

FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).

FUNCTION: Binds directly to 23S rRNA. Probably involved in E site tRNA release (By similarity).

FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity).

SUBUNIT: Part of the 50S ribosomal subunit (By similarity).

FUNCTION: Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential).

SUBCELLULAR LOCATION: Plastid, chloroplast.

SIMILARITY: Belongs to the ribosomal protein L1P family.

Pfam	PF00687; Ribosomal_L1; 1;
TIGRFAMs	TIGR01169; rplA_bact; 1;
PROSITE	PS01199; RIBOSOMAL_L1; 1;

Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding.

Repressor, Translation regulation, tRNA-binding.

GO:0019843; Molecular function: rRNA binding.
GO:0006412; Biological process: translation.

GO:0009507; Cellular component: chloroplast.

Size range:	209-253 amino acids
Related UniRules:	None
Template:	P0A7L0 (RL1_ECOLI); Q5SLP7 (RL1_THET8); P27150 (RL1_THETH); P54050 (RL1_METJA); O52704 (RL1_METTL); P35024 (RL1_SULAC): [Recover all]
Scope:	Bacteria Archaea Plastid
Fusion:	Nter: None; Cter: <Unknown>
Duplicate:	in RHOS1
Plasmid encoded:	None
Comments:	C-terminal fusion in MYCPE, quite atypical in NANEQ and 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).