QCRA_CORGL
ID QCRA_CORGL Reviewed; 408 AA.
AC Q79VE8; Q9AEL6; Q9F482;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cytochrome bc1 complex Rieske iron-sulfur subunit;
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrA;
DE AltName: Full=Menaquinol--cytochrome c reductase iron-sulfur subunit;
DE AltName: Full=Rieske iron-sulfur protein;
GN Name=qcrA; OrderedLocusNames=Cgl2190, cg2404;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11382224; DOI=10.1007/s002030100262;
RA Niebisch A., Bott M.;
RT "Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium
RT glutamicum respiratory chain containing an unusual diheme cytochrome c1.";
RL Arch. Microbiol. 175:282-294(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=11115640; DOI=10.1016/s0005-2728(00)00205-x;
RA Sone N., Nagata K., Kojima H., Tajima J., Kodera Y., Kanamaru T.,
RA Noguchi S., Sakamoto J.;
RT "A novel hydrophobic diheme c-type cytochrome. Purification from
RT Corynebacterium glutamicum and analysis of the QcrCBA operon encoding three
RT subunit proteins of a putative cytochrome reductase complex.";
RL Biochim. Biophys. Acta 1503:279-290(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP FUNCTION, SUBUNIT, AND DETECTION IN A SUPERCOMPLEX WITH CYTOCHROME C
RP OXIDASE (CYTOCHROME AA3).
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12446663; DOI=10.1074/jbc.m210499200;
RA Niebisch A., Bott M.;
RT "Purification of a cytochrome bc1-aa3 supercomplex with quinol oxidase
RT activity from Corynebacterium glutamicum. Identification of a fourth
RT subunity of cytochrome aa3 oxidase and mutational analysis of diheme
RT cytochrome c1.";
RL J. Biol. Chem. 278:4339-4346(2003).
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:0000305, ECO:0000305|PubMed:11382224,
CC ECO:0000305|PubMed:12446663}.
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. The bc1 complex forms a supercomplex with cytochrome c
CC oxidase (cytochrome aa3). {ECO:0000269|PubMed:12446663}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking qcrCAB show strongly impaired
CC growth in glucose minimal medium, which indicates that the bc1-aa3
CC pathway is the main route of respiration under these conditions.
CC {ECO:0000269|PubMed:11382224}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAB99583.1; -; Genomic_DNA.
DR EMBL; AB047851; BAB13772.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20531.1; -; Genomic_DNA.
DR EMBL; AJ306418; CAC33827.1; -; Genomic_DNA.
DR RefSeq; NP_601394.1; NC_003450.3.
DR RefSeq; WP_011014946.1; NC_006958.1.
DR PDB; 7Q21; EM; 3.00 A; A/a=1-408.
DR PDBsum; 7Q21; -.
DR AlphaFoldDB; Q79VE8; -.
DR SMR; Q79VE8; -.
DR STRING; 196627.cg2404; -.
DR KEGG; cgb:cg2404; -.
DR KEGG; cgl:Cgl2190; -.
DR PATRIC; fig|196627.13.peg.2127; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_050668_0_0_11; -.
DR OMA; LGCPTSL; -.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cell membrane; Disulfide bond; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..408
FT /note="Cytochrome bc1 complex Rieske iron-sulfur subunit"
FT /id="PRO_0000127790"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 293..390
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 333
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000305|PubMed:11382224"
FT BINDING 335
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000305|PubMed:11382224"
FT BINDING 352
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000305|PubMed:11382224"
FT BINDING 355
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000305|PubMed:11382224"
FT DISULFID 338..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT ECO:0000305|PubMed:11382224"
FT CONFLICT 44
FT /note="A -> P (in Ref. 2; BAB13772)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="A -> S (in Ref. 2; BAB13772)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> K (in Ref. 2; BAB13772)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="V -> I (in Ref. 2; BAB13772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 45184 MW; 4E60F7D35EFD4907 CRC64;
MSNNNDKQYT TQELNAMSNE DLARLGTELD DVTIAYRKER FPIANDPAEK RAARAVTFWL
VLGIIGGLGF LATYIFWPWE YKAHGDEGLL AYTLYTPMLG ITSGLCILSL GFAVVLYVKK
FIPEEIAVQR RHDGPSEEVD RRTIVALLND SWQTSTLGRR KLIMGLAGGG AVLAGLTIIA
PMGGMIKNPW NPKEGPMDVQ GDGTLWTSGW TLVENDVKVY LGRDTAAIAE SHTDATGEHW
STTGVSRLVR MRPEDLAAAS METVFPLPAE MVNDGAEYDP AKDVYEHQMH SVHGPRNAVM
LIRLRTADAE KVIEREGQES FHYGDYYAYS KICTHIGCPT SLYEAQTNRI LCPCHQSQFD
ALHYGKPVFG PAARALPQLP ITVDEEGYLI AAGNFIEPLG PAFWERKS
