Iron-sulfur (FeeS) clusters are considered one of the most ancient and versatile inorganic cofactors present in the three domains of life. FeeS clusters can act as redox sensors or catalysts and are found to be used by a large number of functional and structurally diverse proteins. Here, we cover current knowledge of the SUF multiprotein machinery that synthesizes and inserts FeeS clusters into proteins. Specific focus is put on the ABC ATPase SufC, which contributes to building FeeS clusters, and appeared early on during evolution.