Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS. Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids. Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. ATP + H2O = ADP + H(+) + phosphate Protein modification; protein ubiquitination. Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'. The RING-type zinc finger domain is required for the ubiquitin-protein ligase activity. The RZ-type (RNF213-ZNFX1) zinc-finger is required for the ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS). No visible phenotype (PubMed:21799892, PubMed:26530008). No vascular phenotype (PubMed:21799892, PubMed:26530008). Belongs to the AAA ATPase family.