Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (PubMed:19876400, PubMed:21264299). Can also use dATP, with lower efficiency, but cannot use GTP, dGTP or CTP (PubMed:19876400). 3'-dephospho-CoA + ATP = ADP + CoA + H(+) Inhibited by CTP (PubMed:19876400, PubMed:21731728). CTP strongly binds the enzyme at a site overlapping that of the leading substrate, dephosphocoenzyme A. Binding of CTP probably prevents interaction with dephosphocoenzyme A and oligomeric transformation to the active form, which limits the catalytic efficiency of the enzyme (PubMed:21731728). kcat is 1.76 min(-1). Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. Forms monomers and homotrimers. The monomer is the active form and the trimeric form is inactive. Shift from inactive homotrimer to active monomer is induced in the presence of dephosphocoenzyme A. A dynamic equilibrium between the trimeric and monomeric forms regulates the effective concentration of active enzyme. The C-terminal UPF0157 domain is involved in the proper folding of the full length enzyme. Was identified as a high-confidence drug target. In the N-terminal section; belongs to the CoaE family. In the C-terminal section; belongs to the UPF0157 (GrpB) family.