Six-bladed beta-propeller, TolB-like
IPR011042
Definition
This superfamily represents a six-bladed β-propeller domain consisting of six 4-stranded β-sheet motifs. This domain can be found in TolB proteins (C-terminal), in soluble quinoprotein glucose dehydrogenase, in calcium-dependent phosphotriesterases, in the low density lipoprotein (LDL) receptor YWTD domain, in nidogen, and in serine/threonine-protein kinase (PknD) NHL repeat domain. TolB is a periplasmic protein from Escherichia coli that is part of the Tol-dependent translocation system involving group A and E colicins that is used to penetrate and kill cells [[cite:PMID:10545334], [cite:PMID:10673426]]. TolB has two domains, an α-helical N-terminal domain that shares structural similarity with the C-terminal domain of transfer RNA ligases, and a β-propeller C-terminal domain that shares structural similarity with numerous members of the prolyl oligopeptidase family and, to a lesser extent, to class B metallo-beta-lactamases (although its does not necessarily occur at the C-terminal in these proteins) PMID:10545334. The C-terminal domain of TolB may mediate protein-protein interactions with colicins.
38 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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