QCRC_GEOTD
ID QCRC_GEOTD Reviewed; 250 AA.
AC Q45659;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Menaquinol-cytochrome c reductase cytochrome b/c subunit;
GN Name=qcrC;
OS Geobacillus thermodenitrificans.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=33940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1041;
RX PubMed=8647852; DOI=10.1074/jbc.271.21.12457;
RA Sone N., Tsuchiya N., Inoue M., Noguchi S.;
RT "Bacillus stearothermophilus qcr operon encoding Rieske FeS protein,
RT cytochrome b6, and a novel-type cytochrome c1 of quinol-cytochrome c
RT reductase.";
RL J. Biol. Chem. 271:12457-12462(1996).
CC -!- FUNCTION: Component of the menaquinol-cytochrome c reductase complex.
CC -!- SUBUNIT: The main subunits of the menaquinone:cytochrome c complex are:
CC cytochrome b, the Rieske protein and a cytochrome b/c subunit.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967}.
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DR EMBL; D83789; BAA12118.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45659; -.
DR STRING; 33940.GTHT12_01702; -.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR012049; MenaQ_cyt_c_Rdtase_cyt_b/c-su.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF036636; QcrC; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..250
FT /note="Menaquinol-cytochrome c reductase cytochrome b/c
FT subunit"
FT /id="PRO_0000061921"
FT TRANSMEM 46..62
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00967"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00967"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00967"
FT DOMAIN 178..250
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 229..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 195
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 196
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 250 AA; 27343 MW; E6D57CF486430306 CRC64;
MHRGKGMKFV GDSRIPAVRK PNIPKDYSEY PGKTEVFWPN FLLKEWLVGS VFLVGFLCLT
VAHPSPLERI ADPTDTTYIP LPDWYFLFLY QLLKYSYASG PYTVIGAIVM PGLAFGALLL
APFLDRGPER RPWKRPVATG MMLLTLAAIV YLTWESVVTH DWEKAAEQGK IRAEVEIDTN
AEGYKIAQAN TCTSCHGENL SGGAGPSLVG TGLTAEEIAK IAKEGQGSMP GGIFKGTDEE
LQKMANSSPA
