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The mitochondrial chaperone (Wagener et al., 2011). Some proteins require completion of folding before translocation across a membrane into another cellular compartment, but the permeability barrier of the membrane should not be compromised. Kater et al. 2020 presented the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding and incorporation of a 2Fe-2S cluster before translocation and subsequent integration into the bc1 complex (TC# 3.D.3). Bcs1 assembles into an exclusively heptameric homo-oligomer, with each protomer consisting of an amphipathic transmembrane helix, a middle domain and an ATPase domain. Together they form two aqueous vestibules, the first being accessible from the mitochondrial matrix and the second positioned in the inner membrane, with both separated by the seal-forming middle domain. On the basis of this unique architecture, Kater et al. 2020 proposed an airlock-like translocation mechanism for folded Rip1.

Fungi, Ascomycota
Bcs1 of Saccharomyces cerevisiae (P32839)

The mycorrhiza-induced mitochondrial AAA-ATPase, Bsc1

Fungi, Basidiomycota
Bsc1 of Laccaria bicolor (B0DYA3)

AAA-ATPase of 514 aas and one or two N-terminal TMSs, AATP1 or ASD. 

Viridiplantae, Streptophyta
ATPase, ASD, of Arabidopsis thaliana

AAA-ATPase of 475 aas and 1 or 2 N-terminal TMSs.

Viridiplantae, Streptophyta
ATPase of Arabidopsis thaliana (Mouse-ear cress)

AAA-ATPase, Bcs1 or Bcs1L of 419 aas and 2 or 3 TMSs. Bcs1 is a chaperone necessary for the assembly of mitochondrial respiratory chain complex III. It plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex 1 (Tamai et al. 2008).

Metazoa, Chordata
Bcs1 of Homo sapiens