v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes [ ]. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex []. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme []. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins []. HflKC can modulate the activity of FtsH []. HflC is considered to be a protease inhibitor and is a member of inhibitor family I87 in the MEROPS database. HHflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection []. |
| Short Name | HflC |