QCRC_COREF
ID QCRC_COREF Reviewed; 296 AA.
AC Q8FNR0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome bc1 complex cytochrome c subunit;
DE EC=7.1.1.8 {ECO:0000250|UniProtKB:Q8NNK5};
DE AltName: Full=Cytochrome bc1 reductase complex subunit Qcrc;
DE AltName: Full=Menaquinol--cytochrome c reductase cytochrome c subunit;
GN Name=qcrC; OrderedLocusNames=CE2084;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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:0000250|UniProtKB:Q8NNK5}.
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:0000250|UniProtKB:Q8NNK5};
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:0000250|UniProtKB:Q8NNK5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000250|UniProtKB:Q8NNK5}.
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DR EMBL; BA000035; BAC18894.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FNR0; -.
DR SMR; Q8FNR0; -.
DR STRING; 196164.23493926; -.
DR PRIDE; Q8FNR0; -.
DR EnsemblBacteria; BAC18894; BAC18894; BAC18894.
DR KEGG; cef:CE2084; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_086567_0_0_11; -.
DR OMA; LFRTNCA; -.
DR Proteomes; UP000001409; 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 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Repeat; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..296
FT /note="Cytochrome bc1 complex cytochrome c subunit"
FT /id="PRO_0000108446"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 67..147
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 177..255
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 84
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 190
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 193
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 194
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:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 296 AA; 31261 MW; FC3038B069212C33 CRC64;
MMETNPQTSE GAGKAQSSAK KVKNRRKLRR TVAGAMALTI GLSGAGILAT AITPDAQIAT
AQRDDQALIA EGKDLYDVAC ITCHGMNLQG VQDRGPSLIG VGEGAVYFQV HSGRMPMQRN
EAQASRKTPR YTEAQTLAIA AYVAANGGGP GLVYNEDGTL AMEELRGSNF DGQIDPLDVS
RGGDLFRLNC ASCHNFTGRG GALSSGKYAP VLDPANEQEI YQAMLTGPQN MPKFSDRQLS
ADEKKDIIAF IKSTKETPSP GGYSLGGLGP VSEGLFMWGI GIMVLIAAAM WIGSRS
