PrkA proteins are bacterial and archaeal serine kinases approximately 630 residues in length. This entry represents the N-terminal AAA domain [ (PUBMED:8626065) ].
Family alignment:
There are 4714 AAA_PrkA domains in 4714 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing AAA_PrkA domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with AAA_PrkA domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing AAA_PrkA domain in the selected taxonomic class.
Cloning and characterization of the Bacillus subtilis prkA gene encoding a novel serine protein kinase.
Gene. 1996; 168: 55-60
Display abstract
We have cloned and sequenced a 3574-bp Bacillus subtilis (Bs) DNA fragment located between the nrdA and citB genes at about 169 degrees on the chromosome. An Escherichia coli strain, LBG1605, carrying a mutated ptsH gene (encoding HPr (His-containing protein) of the bacterial phosphotransferase system (PTS)) and complemented for PTS activity with the ptsH of Staphylococcus carnosus, exhibited reduced mannitol fermentation activity when transformed with a plasmid bearing this 3574-bp Bs fragment. This fragment contained an incomplete and two complete open reading frames (ORFs). The product of the first complete ORF, a protein composed of 235 amino acids (aa) (25038 Da), was found to be responsible for the observed reduced mannitol fermentation. The 3' part of this 705-bp second ORF and the 428-bp incomplete first ORF encode aa sequences exhibiting almost 40% sequence identify. However, the function of these two proteins remains unknown. The third ORF, the 1893-bp prkA gene, encodes a protein (PrkA) of 72889 Da. PrkA possesses the A-motif of nucleotide-binding proteins and exhibits distant homology to eukaryotic protein kinases. Several of the essential aa in the loops known to form the active site of cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase appeared to be conserved in PrkA. After expression of prkA and purification of PrkA, we could demonstrate that PrkA can indeed phosphorylate a Bs 60-kDa protein at a Ser residue.
Links (links to other resources describing this domain)
