ID   QCRA_STRLI              Reviewed;         170 AA.
AC   Q9ZFB7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytochrome bc1 complex Rieske iron-sulfur subunit;
DE   AltName: Full=Cytochrome bc1 reductase complex subunit QcrA;
DE   AltName: Full=Rieske iron-sulfur protein;
DE   AltName: Full=Ubiquinol--cytochrome c reductase iron-sulfur subunit;
DE   Flags: Fragment;
GN   Name=qcrA;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TK21;
RA   Parro V., Mellado R.P.;
RT   "Cytochrome b of Streptomyces lividans.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Iron-sulfur subunit of the cytochrome bc1 complex, an
CC       essential component of the respiratory electron transport chain
CC       required for ATP synthesis. The bc1 complex catalyzes the oxidation of
CC       menaquinol and the reduction of cytochrome c in the respiratory chain.
CC       The bc1 complex operates through a Q-cycle mechanism that couples
CC       electron transfer to generation of the proton gradient that drives ATP
CC       synthesis. {ECO:0000250|UniProtKB:P9WH23}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- SUBUNIT: The cytochrome bc1 complex is composed of a cytochrome b
CC       (QcrB), the Rieske iron-sulfur protein (QcrA) and a diheme cytochrome c
CC       (QcrC) subunit. {ECO:0000250|UniProtKB:P9WH23}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; AF107888; AAD04932.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZFB7; -.
DR   SMR; Q9ZFB7; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   PANTHER; PTHR10134; PTHR10134; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Cell membrane; Disulfide bond; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Respiratory chain;
KW   Transmembrane; Transport.
FT   CHAIN           <1..170
FT                   /note="Cytochrome bc1 complex Rieske iron-sulfur subunit"
FT                   /id="PRO_0000127793"
FT   DOMAIN          63..153
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         98
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         115
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         118
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   DISULFID        101..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   NON_TER         1
SQ   SEQUENCE   170 AA;  18940 MW;  84C6D18F10222DC6 CRC64;
     WRDLGPLPGT KLRHTLWSKG KLLVNMNTNE PLRPSDVAVG SLTFAMPEGL EEHDEDFQNE
     IAKAALMIIR LEPDSIKDKR ELEWSHEGIV AYSKICTHVG CPISLYEQQT HHALCPCHQS
     TFDLADGARV IFGPAGHALP QLRIGVNDEG YLEALGDFEE PVGPAYWERG