ABC transporter (ABC transporter) was first discovered in bacteria. It is a transport ATPase (transport ATPase) on the bacterial plasma membrane. It belongs to a large and diverse protein family. The ABC transporter contains at least two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). In some bacterial transport proteins, these regions are located on different polypeptides. Most ABC transporters act as dimers and consist of four domains, two ABC modules, and two TMDs. ABC transporters usually consist of multiple subunits, one or two of which are transmembrane proteins. One or two are membrane-associated AAA ATPase. The function of the intact inner membrane protein is to transport the substrate across the membrane and to recognize the substrate (64, 65). ABC transporter dimerizes by binding ATP. ATP is hydrolyzed and depolymerized. The substrate-bound to it is transferred to the other side of the membrane through conformational changes. The ATPase subunit uses the energy of adenosine triphosphate (ATP) binding and hydrolysis to provide the energy required for substrate transport across the membrane to absorb or export the substrate.