QCRB_GEOTD
ID QCRB_GEOTD Reviewed; 224 AA.
AC Q45658;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Menaquinol-cytochrome c reductase cytochrome b subunit;
GN Name=qcrB;
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups per subunit. One heme group is bound
CC covalently by a single cysteine link, the other one non-covalently.
CC {ECO:0000250};
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:PRU00968}.
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DR EMBL; D83789; BAA12117.1; -; Genomic_DNA.
DR RefSeq; WP_008879599.1; NZ_PIZS01000087.1.
DR AlphaFoldDB; Q45658; -.
DR SMR; Q45658; -.
DR STRING; 33940.GTHT12_01703; -.
DR OMA; WATQTGM; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00284; Cytochrome_b_N; 1.
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; PF00033; Cytochrome_B; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="Menaquinol-cytochrome c reductase cytochrome b
FT subunit"
FT /id="PRO_0000061919"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 43
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 94
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 BINDING 108
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 BINDING 196
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 BINDING 211
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"
SQ SEQUENCE 224 AA; 25411 MW; AD05E81F4E7F0518 CRC64;
MLNKLYDWVD ERLDITPLWR DIADHEVPEH VNPAHHFSAF VYCFGGLTFF VTVIQILSGM
FLTMYYVPDI KNAWESVYYL QNEVAFGQIV RGMHHWGASL VIVMMFLHTL RVFFQGAYKK
PREMNWIVGV LIFMVMMGLG FTGYLLPWDM KALFATKVGL QIAEAVPLIG PAIKTLLAGD
PEIVGAQTLA RFFAIHVFFL PAALLGLMAA HFLMIRRQGI SGPL
