Protein Domain : Cation efflux system protein CusB, domain 1 IPR043602

Type	Domain
Description	CusB can be divided into four different domains. The first three domains of the protein are mostly β-strands. However, the fourth domain forms an all α-helical domain, which is folded into a three-helix bundle secondary structure [ ]. This entry represents the first beta-domain (domain 1) of cation efflux system protein CusB from E. coli. It is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385) [ ]. CusB is part of the copper-transporting efflux system CusCFBA []. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids []. HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm []. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore [].
Short Name	CusB_dom_1