PrfA
- Description: peptide chain release factor 1
| Gene name | prfA |
| Synonyms | |
| Essential | yes PubMed |
| Product | peptide chain release factor 1 |
| Function | translation |
| MW, pI | 40 kDa, 4.824 |
| Gene length, protein length | 1068 bp, 356 aa |
| Immediate neighbours | ywkE, ywkD |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU37010
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: binds to the ribosome through specific recognition of messenger RNA stop codons and triggers hydrolysis of the bond between the nascent polypeptide and the transfer RNA at the peptidyl-tRNA site, thereby releasing the newly synthesized protein. PrfA is highly specific for a U in the first stop-codon position and recognizes UAA and UAG
- Protein family: prokaryotic/mitochondrial release factor family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P45872
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Johan Sund, Martin Andér, Johan Aqvist
Principles of stop-codon reading on the ribosome.
Nature: 2010, 465(7300);947-50
[PubMed:20512119]
[WorldCat.org]
[DOI]
(I p)
Daniel J Rigden, Peter Setlow, Barbara Setlow, Irina Bagyan, Richard A Stein, Mark J Jedrzejas
PrfA protein of Bacillus species: prediction and demonstration of endonuclease activity on DNA.
Protein Sci: 2002, 11(10);2370-81
[PubMed:12237459]
[WorldCat.org]
[DOI]
(P p)
