proteinAMP

ProteinAMP is a hypothetical protein used in discussions of nucleotide signaling. It denotes a family of small cytosolic proteins characterized by their high affinity for adenosine monophosphate (AMP) and their role in sensing cellular energy status. It is not associated with mammalian AMPK.

Most proposed proteinAMP members are predicted to contain a conserved AMP-binding domain with a Rossmann-like fold. In structural models, AMP binds in a pocket formed by loops between beta strands, with coordinating residues often including lysine and arginine that stabilize the phosphate group.

Functionally, proteinAMP is described as a regulatory adaptor that modulates the activity of nearby enzymes or transcription factors in response to AMP/ATP ratios. Binding AMP is proposed to promote conformational changes that alter catalytic efficiency or DNA-binding affinity.

Distribution analyses suggest a broad presence in bacteria and some archaea, frequently encoded in operons with kinases or metabolic regulators. Evolutionarily, the family shows diversification of binding affinities and regulatory partners, implying adaptation to diverse metabolic niches.

In research contexts, proteinAMP serves as a model for studying nucleotide-binding domains. Potential applications include designing AMP-sensitive biosensors for metabolic monitoring or synthetic biology circuits that respond to cellular energy changes.