v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | GspM is part of the inner membrane component of the type II secretion system (T2SS). It consists of a short cytosolic N-terminal domain, a transmembrane domain, and a C-terminal periplasmic domain. The precise function of this protein is unknown [ ]. However, though in Vibrio cholerae, the EpsM protein interacts with the EpsL protein, and also forms homodimers [].The periplasmic domain forms a sandwich consisting of two α-helices and a four-stranded antiparallel β-sheet [ ]. The overall fold is a circular permutation of the ferredoxin fold. In the dimer, a deep cleft with a polar rim and a hydrophobic bottom made by conserved residues is located between the monomers. This cleft contains an extra electron density suggesting that this region might serve as a binding site of an unknown ligand or part of a protein partner. |
| Short Name | T2SS_M_periplasmic_sf |