UniProt functional annotation for P07012



	UniProt functional annotation for P07012

UniProt code: P07012.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:17932046, ECO:0000269|PubMed:22857598, ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875, ECO:0000305|PubMed:22857598}.

Subunit: Interacts with the ribosome (PubMed:22857598, PubMed:22922063, PubMed:25355516, PubMed:12511960, PubMed:12511961). Recruited to stalled ribosomes by ArfA, in the presence of truncated mRNA, ArfA influences RF2 conformation so RF2 can hydrolyze the peptidyl-tRNA bond (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). {ECO:0000269|PubMed:12511960, ECO:0000269|PubMed:12511961, ECO:0000269|PubMed:22857598, ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875}.

Subcellular location: Cytoplasm. Note=Recruited to the 70S ribosome by ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516, PubMed:27934701). {ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27934701}.

Ptm: Methylated by PrmC. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced. {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124, ECO:0000269|PubMed:17932046}.

Miscellaneous: The gene for this protein contains a UGA in-frame termination codon after Leu-25; a naturally occurring frameshift enables complete translation of RF-2. This provides a mechanism for the protein to regulate its own production. {ECO:0000269|PubMed:22857598}.

Similarity: Belongs to the prokaryotic/mitochondrial release factor family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). {ECO:0000269\|PubMed:11118225, ECO:0000269\|PubMed:17932046, ECO:0000269\|PubMed:22857598, ECO:0000269\|PubMed:22922063, ECO:0000269\|PubMed:25355516, ECO:0000269\|PubMed:27906160, ECO:0000269\|PubMed:27906161, ECO:0000269\|PubMed:27934701, ECO:0000269\|PubMed:28077875, ECO:0000305\|PubMed:22857598}.


Subunit:		Interacts with the ribosome (PubMed:22857598, PubMed:22922063, PubMed:25355516, PubMed:12511960, PubMed:12511961). Recruited to stalled ribosomes by ArfA, in the presence of truncated mRNA, ArfA influences RF2 conformation so RF2 can hydrolyze the peptidyl-tRNA bond (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). {ECO:0000269\|PubMed:12511960, ECO:0000269\|PubMed:12511961, ECO:0000269\|PubMed:22857598, ECO:0000269\|PubMed:22922063, ECO:0000269\|PubMed:25355516, ECO:0000269\|PubMed:27906160, ECO:0000269\|PubMed:27906161, ECO:0000269\|PubMed:27934701, ECO:0000269\|PubMed:28077875}.
Subcellular location:		Cytoplasm. Note=Recruited to the 70S ribosome by ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516, PubMed:27934701). {ECO:0000269\|PubMed:22922063, ECO:0000269\|PubMed:25355516, ECO:0000269\|PubMed:27934701}.
Ptm:		Methylated by PrmC. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced. {ECO:0000269\|PubMed:11118225, ECO:0000269\|PubMed:11805295, ECO:0000269\|PubMed:11847124, ECO:0000269\|PubMed:17932046}.
Miscellaneous:		The gene for this protein contains a UGA in-frame termination codon after Leu-25; a naturally occurring frameshift enables complete translation of RF-2. This provides a mechanism for the protein to regulate its own production. {ECO:0000269\|PubMed:22857598}.
Similarity:		Belongs to the prokaryotic/mitochondrial release factor family. {ECO:0000305}.