QCRB_CORGL
ID QCRB_CORGL Reviewed; 539 AA.
AC Q79VE9; Q9AEL5; Q9F481;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytochrome bc1 complex cytochrome b subunit {ECO:0000303|PubMed:11382224};
DE EC=7.1.1.8 {ECO:0000305};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrB;
DE AltName: Full=Menaquinol--cytochrome c reductase cytochrome b subunit;
GN Name=qcrB; OrderedLocusNames=Cgl2189, cg2403;
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, CATALYTIC ACTIVITY, SUBUNIT, AND DETECTION IN A SUPERCOMPLEX WITH
RP CYTOCHROME C 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: Cytochrome b 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000305|PubMed:12446663};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P00163};
CC Note=Binds 2 heme groups non-covalently per subunit.
CC {ECO:0000250|UniProtKB:P00163};
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 cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00968}.
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DR EMBL; AJ306418; CAC33828.1; -; Genomic_DNA.
DR EMBL; AB047851; BAB13773.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99582.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20530.1; -; Genomic_DNA.
DR RefSeq; NP_601393.1; NC_003450.3.
DR RefSeq; WP_003856609.1; NC_006958.1.
DR PDB; 7Q21; EM; 3.00 A; B/b=1-539.
DR PDBsum; 7Q21; -.
DR AlphaFoldDB; Q79VE9; -.
DR SMR; Q79VE9; -.
DR STRING; 196627.cg2403; -.
DR GeneID; 58308867; -.
DR KEGG; cgb:cg2403; -.
DR KEGG; cgl:Cgl2189; -.
DR PATRIC; fig|196627.13.peg.2126; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_2_0_11; -.
DR OMA; WNYGPYD; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF13631; Cytochrom_B_N_2; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Respiratory chain; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..539
FT /note="Cytochrome bc1 complex cytochrome b subunit"
FT /id="PRO_0000061924"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968,
FT ECO:0000305|PubMed:11382224"
FT BINDING 117
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968,
FT ECO:0000305|PubMed:11382224"
FT BINDING 204
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968,
FT ECO:0000305|PubMed:11382224"
FT BINDING 219
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968,
FT ECO:0000305|PubMed:11382224"
FT CONFLICT 242
FT /note="I -> V (in Ref. 2; BAB13773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 59809 MW; 6CC31CBBAAE6B647 CRC64;
MSLATVGNNL DSRYTMASGI RRQINKVFPT HWSFMLGEIA LYSFIVLLLT GVYLTLFFDP
SITKVIYDGG YLPLNGVEMS RAYATALDIS FEVRGGLFIR QMHHWAALLF VVSMLVHMLR
IFFTGAFRRP REANWIIGVV LIILGMAEGF MGYSLPDDLL SGVGLRIMSA IIVGLPIIGT
WMHWLIFGGD FPSDLMLDRF YIAHVLIIPA ILLGLIAAHL ALVWYQKHTQ FPGAGRTENN
VIGIRIMPLF AVKAVAFGLI VFGFLALLAG VTTINAIWNL GPYNPSQVSA GSQPDVYMLW
TDGAARVMPA WELYLGNYTI PAVFWVAVML GILVVLLVTY PFIERKFTGD DAHHNLLQRP
RDVPVRTSLG VMALVFYILL TVSGGNDVYA MQFHVSLNAM TWIGRIGLIV GPAIAYFITY
RLCIGLQRSD REVLEHGIET GIIKQMPNGA FIEVHQPLGP VDDHGHPIPL PYAGAAVPKQ
MNQLGYAEVE TRGGFFGPDP EDIRAKAKEI EHANHIEEAN TLRALNEANI ERDKNEGKN
