Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease (PubMed:23279021, PubMed:29581261). Binds one molecule of StP/metal. Binds StP/Co(2+) and StP/Ni(2+) tighter than StP/Zn(2+) (PubMed:29581261). Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro (PubMed:23279021). Nickel/cobalt import is reduced in the presence of zinc. The complex is composed of two ATP-binding proteins (CntD and CntF), two transmembrane proteins (CntB and CntC) and a solute-binding protein (CntA). Repressed by zinc. StP/metal binding triggers a notable interdomain conformational change. Deletion of the cntABCDF genes decreases nickel and cobalt intracellular levels and decreases virulence (PubMed:23279021). Insertion mutant shows attenuated growth in several infection models (PubMed:9791183). Belongs to the bacterial solute-binding protein 5 family.