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: | Q9X806 |
Protein Name: | Cytochrome bc1 complex cytochrome b subunit |
Length: | 545 |
Molecular Weight: | 60886.00 |
Species: | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [100226] |
Number of TMSs: | 8 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
hydron |
---|
1: MSTAANEPSR SRGKAPAGER VADWADGRLG IYSLAKANMR KIFPDHWSFM LGEVCLYSFI
61: IIILTGVYLT LFFHPSMAEV EYHGSYVPLQ GQMMSEAYAS TLDISFDVRG GLLIRQIHHW
121: AALIFLAGMF VHMMRVFFTG AFRKPREVNW LFGFLLLVLG MFTGFTGYSL PDDLLSGTGI
181: RFMEGAILSV PIVGTYISFF LFGGEFPGHD FVSRFYSIHI LLLPGIMLGL LVGHLILVFY
241: HKHTQFAGPG KTNKNVVGMP LLPVYTAKAG GFFFLVFGVI SVVSAIATIN PIWAIGPYRP
301: DQVSTGAQPD WYMGFSEGLI RVMPGWEINA WGHTLVLGVF VPLLIFPLVL AAIAVYPFIE
361: SWVTGDKREH HILDRPRNAP TRTAFGVAWL TVYFVLLIGG GNDLWATHFH LSINAITWFV
421: RIAFFVGPVV AFIATKRICL GLQRRDKDKV LHGRESGIIK RLPHGEFIEV HEPLSQEQLH
481: TLTAHEQYQP AEIGPTVDEN GVERKVSGTQ KLRAKLSESY YGEESQIPKP TVEEYKEITS
541: GHGHH