QCRA_MYCTO
ID QCRA_MYCTO Reviewed; 429 AA.
AC P9WH22; L0TBK9; Q10387;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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;
GN Name=qcrA; OrderedLocusNames=MT2251;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46537.1; -; Genomic_DNA.
DR PIR; D70784; D70784.
DR RefSeq; WP_003411396.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WH22; -.
DR SMR; P9WH22; -.
DR EnsemblBacteria; AAK46537; AAK46537; MT2251.
DR KEGG; mtc:MT2251; -.
DR PATRIC; fig|83331.31.peg.2426; -.
DR HOGENOM; CLU_050668_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
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; IPR045603; QcrA_N.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF19297; QcrA_N; 1.
DR Pfam; PF00355; Rieske; 1.
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; Transmembrane helix; Transport.
FT CHAIN 1..429
FT /note="Cytochrome bc1 complex Rieske iron-sulfur subunit"
FT /id="PRO_0000428262"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 316..410
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 355
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 372
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 375
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 358..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 429 AA; 46923 MW; C22C87EC283FE0EE CRC64;
MSRADDDAVG VPPTCGGRSD EEERRIVPGP NPQDGAKDGA KATAVPREPD EAALAAMSNQ
ELLALGGKLD GVRIAYKEPR WPVEGTKAEK RAERSVAVWL LLGGVFGLAL LLIFLFWPWE
FKAADGESDF IYSLTTPLYG LTFGLSILSI AIGAVLYQKR FIPEEISIQE RHDGASREID
RKTVVANLTD AFEGSTIRRR KLIGLSFGVG MGAFGLGTLV AFAGGLIKNP WKPVVPTAEG
KKAVLWTSGW TPRYQGETIY LARATGTEDG PPFIKMRPED MDAGGMETVF PWRESDGDGT
TVESHHKLQE IAMGIRNPVM LIRIKPSDLG RVVKRKGQES FNFGEFFAFT KVCSHLGCPS
SLYEQQSYRI LCPCHQSQFD ALHFAKPIFG PAARALAQLP ITIDTDGYLV ANGDFVEPVG
PAFWERTTT
