Multi-solute ABC transporter that mediates uptake of unrelated hydrophilic compounds (PubMed:32296172). Can transport vitamin B12 and related corrinoids, and antimicrobial peptides such as bleomycin (PubMed:18996991, PubMed:32296172, PubMed:23407640). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:32296172). Contributes to maintenance of chronic infections (PubMed:18996991). The presence of cobalamin does not affect the ATPase activity. Homodimer. Contains a large occluded hydrophilic cavity that spans the entire thickness of the membrane and extends into the intracellular part of the protein. It consists of two connected chambers. The larger chamber is located in the transmembrane domain, and the smaller chamber is formed by the part of the protein that connects the NBDs and transmembrane domains. Disruption results in bleomycin resistance and alters the outcome of a chronic infection within the host, but does not alter sensitivity to other membrane-disrupting agents and resistance to clinically important antituberculosis drugs (PubMed:18996991). Deletion eliminates the ability of the bacterium to transport vitamin B12 and related corrinoids (PubMed:23407640). Belongs to the ABC transporter superfamily.