QCRC_CORGL
ID QCRC_CORGL Reviewed; 283 AA.
AC Q8NNK5; Q6M3P2; Q93HZ3; Q9AEL7; Q9F483;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytochrome bc1 complex cytochrome c subunit {ECO:0000303|PubMed:11382224};
DE Short=Cytochrome c1 {ECO:0000303|PubMed:11382224};
DE EC=7.1.1.8 {ECO:0000269|PubMed:11115640};
DE AltName: Full=Cytochrome bc1 reductase complex subunit Qcrc;
DE AltName: Full=Menaquinol--cytochrome c reductase cytochrome c subunit;
GN Name=qcrC; OrderedLocusNames=Cgl2191, cg2405;
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, DISRUPTION PHENOTYPE, COVALENT
RP HEME BINDING, AND SUBCELLULAR LOCATION.
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], PROTEIN SEQUENCE OF 110-125 AND 152-175,
RP AND DETECTION OF TWO HEME C GROUPS.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-235.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11577165; DOI=10.1099/00221287-147-10-2865;
RA Sakamoto J., Shibata T., Mine T., Miyahara R., Torigoe T., Noguchi S.,
RA Matsushita K., Sone N.;
RT "Cytochrome c oxidase contains an extra charged amino acid cluster in a new
RT type of respiratory chain in the amino acid-producing Gram-positive
RT bacterium Corynebacterium glutamicum.";
RL Microbiology 147:2865-2871(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DETECTION IN A SUPERCOMPLEX WITH
RP CYTOCHROME C OXIDASE (CYTOCHROME AA3), AND MUTAGENESIS OF HEME-BINDING
RP SITES.
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 c1 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:0000269|PubMed:12446663};
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:0000269|PubMed:11382224};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:11115640, ECO:0000305|PubMed:11382224}.
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 -!- MISCELLANEOUS: No stable monoheme protein can accumulate if the
CC incorporation of the other heme group is blocked; assembly of both the
CC cytochrome bc1 complex and the cytochrome bc1-aa3 supercomplex depends
CC on heme assembly. {ECO:0000269|PubMed:12446663}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB99584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAF20532.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ306418; CAC33826.1; -; Genomic_DNA.
DR EMBL; AB047851; BAB13771.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99584.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927154; CAF20532.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB052749; BAB64409.1; -; Genomic_DNA.
DR RefSeq; NP_601395.2; NC_003450.3.
DR PDB; 7Q21; EM; 3.00 A; C/c=1-283.
DR PDBsum; 7Q21; -.
DR AlphaFoldDB; Q8NNK5; -.
DR SMR; Q8NNK5; -.
DR STRING; 196627.cg2405; -.
DR KEGG; cgb:cg2405; -.
DR KEGG; cgl:Cgl2191; -.
DR PATRIC; fig|196627.13.peg.2128; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_086567_0_0_11; -.
DR OMA; LFRTNCA; -.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009152; bc1_cytC-su.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000007; Ubiq_cycred_cyc; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Reference proteome; Repeat;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..283
FT /note="Cytochrome bc1 complex cytochrome c subunit"
FT /id="PRO_0000108447"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 54..134
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 164..242
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:11382224"
FT BINDING 70
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:11382224"
FT BINDING 71
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:11382224"
FT BINDING 177
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:11382224"
FT BINDING 180
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:11382224"
FT BINDING 181
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:11382224"
FT MUTAGEN 67..70
FT /note="CITC->SITS: Complete lack of c-type cytochromes."
FT /evidence="ECO:0000269|PubMed:12446663"
FT MUTAGEN 177..180
FT /note="CASC->SASS: Complete lack of c-type cytochromes."
FT /evidence="ECO:0000269|PubMed:12446663"
SQ SEQUENCE 283 AA; 29867 MW; 0EBBB1C335861CAE CRC64;
MAKPSAKKVK NRRKVRRTVA GALALTIGLS GAGILATAIT PDAQVATAQR DDQALISEGK
DLYDVACITC HGVNLQGVED RGPSLVGVGE GAVYFQVHSG RMPILRNEAQ AERKAPRYTE
AQTLAIAAYV AANGGGPGLV YNEDGTLAME ELRGENYDGQ ITSADVARGG DLFRLNCASC
HNFTGRGGAL SSGKYAPNLD AANEQEIYQA MLTGPQNMPK FSDRQLSADE KKDIIAFIKS
TKETPSPGGY SLGSLGPVAE GLFMWVFGIL VLVAAAMWIG SRS
