QCRB_COREF
ID QCRB_COREF Reviewed; 541 AA.
AC Q8FNR2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cytochrome bc1 complex cytochrome b subunit;
DE EC=7.1.1.8 {ECO:0000250|UniProtKB:Q79VE9};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrB;
DE AltName: Full=Menaquinol--cytochrome c reductase cytochrome b subunit;
GN Name=qcrB; OrderedLocusNames=CE2082;
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 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:0000250|UniProtKB:Q79VE9}.
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:Q79VE9};
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 protein iron-sulfur (QcrA) and a diheme cytochrome c
CC (QcrC) subunit. {ECO:0000250|UniProtKB:Q79VE9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00968}.
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DR EMBL; BA000035; BAC18892.1; -; Genomic_DNA.
DR RefSeq; WP_011075748.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FNR2; -.
DR SMR; Q8FNR2; -.
DR STRING; 196164.23493924; -.
DR EnsemblBacteria; BAC18892; BAC18892; BAC18892.
DR KEGG; cef:CE2082; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_2_0_11; -.
DR OMA; WNYGPYD; -.
DR OrthoDB; 262439at2; -.
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: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 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="Cytochrome bc1 complex cytochrome b subunit"
FT /id="PRO_0000061923"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 105
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 119
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 206
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 221
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"
SQ SEQUENCE 541 AA; 60048 MW; B8193CC87F214189 CRC64;
MSNKLATVGN NLDSRYTMAG GIRRQINKVF PTHWSFLLGE IALYSFIILI LTGVYLTLFF
DPSITKVIYD GAYLPLNGVE MSRAYMTALD ISFEVRGGLF VRQMHHWAAL MFVVSMMVHM
MRIFFTGAFR RPREANWVIG VVLLILGIAE GFMGYSLPDD LLSGVGLRIM SAIIVGLPII
GTWMHWMIFG GDFPSDIMLD RFYIAHVLII PGIILGLIAA HLALVWYQKH TQFPGAGRTE
NNVIGIRIMP VFAVKSVAFG AITLGFLSLL AGVTTINAIW NLGPYNPSQV SAGSQPDIYM
LWTDGAARVM PAWELYFGNY TVPAVFWVAI MLGILVVLLI AYPWIEKKLT GDDAHHNLLQ
RPRDVPVRTS LGVMALIFYI LLTISGGNDI WAYQFDVSLN AMTWIGRIGL IVFPAIGYFV
TYRLCIGLQR SDREVLEHGI ETGVIKQMPN GAFIEVHQPL GPVDEHGHPI PLPYSGAKVP
KQLNELGFAE VESRGGFFGP DPESVATKAN EIAHANHLEE VATLAAIQEE NRKRDQAEGR
I
