Joined: May 2002
IIRC the ATPase doesn't synthesize the entirety of ATP, it just adds or removes energized phosphates -- Adenosine Triphophsate toe Diphosphate and back.
But none of what you wrote (or linked to) contradicts what I said above. There is no evidence of a pre-PPi synthase, and no evidence that the ATP synthesis molecular machine can be reduced to one component. The synthesis of ATP is a lot more than just inorganic phosphate.
Rather like what the remarkably simple, 1-component (dimer) PPase does with phosphates:
Hmm, might not be working, look here:
...and both are coupled to H+ gradients, and use the same basic fold, what a coincidence! It just looks like all of that rotating complexity may be useful and efficiency-increasing add-on rather than an absolutely necessary part of primitive cellular energetics.
You are entitled to your prediction. Regarding TTSS, I am holding out for:
Since the synthesis of diphosphate can be reduced to one subunit, I would say that it is simpler than ATP synthesis, but I wonder if a prediction not unlike the TTSS can be formed, in that it came after or evolved from ATP synthase rather than to it.
1) TTSS with nonvirulence, nonflagellar functions, and
2) Basal homologs of the TTSS.
These are predictions that only further data can resolve, however. In general, you'll forgive me for sticking with Baltscheffsky until some IDist (1) acknowledges his existence and (2) explains how they don't greatly weaken the ID argument based on the F1F0 ATPase.