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3.D.3.5.4
The three component QcrABC cytochrome bc1 (bcc) complex.  The bc1 complex catalyzes the oxidation of menaquinol and the reduction of a cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. QcrA is an iron-sulfur (2Fe-2S) protein of 353 aas and 3 central TMSs; QcrB is a cytochrom b protein that contains two quinone binding sites, one for oxidations, and one for reduction of 545 aas and 9 TMSs, while  QcrC is a membrane-bound diheme c-type cytochrome with 269 aas and 2 TMSs, one N-terminal, and one C-terminal.  QcrABC forms a complex with CtaCDEF (TC# 3.D.4.4.5), a cytochrome aa3 oxidase complex (Falke et al. 2018). This supercomplex is required for spore-specific nitrate reductase 1 activity (Falke et al. 2019).

Accession Number:Q9X807
Protein Name:Cytochrome bc1 complex Rieske iron-sulfur subunit
Length:353
Molecular Weight:38574.00
Species:Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [100226]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate

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FASTA formatted sequence
1:	MSSQDIPEEN LPAEQDRPHG AAARPADETN PFADPGLPPH EPRVQDVDER AAKRSERTVA 
61:	LLFTLSMLAT IAFIAAFVAI DVDKSVYIFP LGHISALNFA LGMTLGVALF AIGAGAVHWA 
121:	RTLMSDEEVA DERHPIEASP EVRAKVHADF KQGAKESVIG RRKLIRNTML GALTLVPLSG 
181:	VVLLRDLGPL PGTKLRHTLW SKGKLLVNMN TNEPLRPSDV AVGSLTFAMP EGLEEHDEDF 
241:	QNEIAKAALM IIRLEPDSIK DKRELEWSHE GIVAYSKICT HVGCPISLYE QQTHHALCPC 
301:	HQSTFDLADG ARVIFGPAGH ALPQLRIGVN DEGYLEALGD FEEPVGPAYW ERG