Accession	MF_01320
Dates	2-FEB-2004 (Created) 25-SEP-2008 (Last updated, Version 20)

Data class

Protein

Predictors

HAMAP; MF_01320_B; [distribution of match scores in UniProtKB];[seed alignment for MF_01320_B]

Predictors

HAMAP; MF_01320_A; [distribution of match scores in UniProtKB];[seed alignment for MF_01320_A]

Identifier

RL2

Protein name

RecName: Full=50S ribosomal protein L2;

Gene name

rplB

Identifier

RL2

Protein name

RecName: Full=50S ribosomal protein L2;

Gene name

rplB, rpl2

Identifier

RL2

Protein name

RecName: Full=50S ribosomal protein L2P;

Gene name

rpl2p

Identifier

RK2

Protein name

RecName: Full=50S ribosomal protein L2, chloroplastic;

Gene name

rpl2

FUNCTION: One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (By similarity).

SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome (By similarity).

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

SUBCELLULAR LOCATION: Plastid, chloroplast.

SIMILARITY: Belongs to the ribosomal protein L2P family.

Pfam	PF00181; Ribosomal_L2; 1; PF03947; Ribosomal_L2_C; 1;
TIGRFAMs	TIGR01171; rplB_bact; 1;
PROSITE	PS00467; RIBOSOMAL_L2; 1;

Acetylation.

Ribonucleoprotein, Ribosomal protein.

RNA-binding, rRNA-binding.

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

GO:0009507; Cellular component: chloroplast.

From: RL2_ECOLI (P60422)
Key		From		To		Description		Condition		FTGroup
MOD_RES		242		242		N6-acetyllysine (By similarity)		K

Size range:	233-304 amino acids
Related UniRules:	None
Template:	Q9RXJ9 (RL2_DEIRA); P20276 (RL2_HALMA); P60422 (RL2_ECOLI): [Recover all]
Scope:	Bacteria Archaea Plastid
Fusion:	Nter: None; Cter: None
Duplicate:	in BARBK, LEPBL
Plasmid encoded:	None
Comments:	The initiation codon is created by RNA editing in barley and maize, and is suggested to be created by editing in wheat. The same start codon exists in rice (ACG), so we suggest it too is edited.