QCRB_MYCLE
ID QCRB_MYCLE Reviewed; 551 AA.
AC P15878;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cytochrome bc1 complex cytochrome b subunit;
DE EC=7.1.1.8 {ECO:0000250|UniProtKB:P9WP37};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrB;
DE AltName: Full=Ubiquinol--cytochrome c reductase cytochrome b subunit;
GN Name=qcrB; Synonyms=mla12A; OrderedLocusNames=ML0879;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-551.
RX PubMed=2181404; DOI=10.1093/nar/18.5.1294;
RA Hartskeerl R.A., Stabel L.F.E.M., Hermans C.R., Klatser P.R., Thole J.E.R.;
RT "Nucleotide and deduced amino acid sequence of a Mycobacterium leprae 12K
RT protein.";
RL Nucleic Acids Res. 18:1294-1294(1990).
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 ubiquinol 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. The cytochrome b subunit contains two ubiquinol reactive
CC sites: the oxidation (QP) site and the reduction (QN) site.
CC {ECO:0000250|UniProtKB:P9WP37}.
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:P9WP37};
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 iron-sulfur protein (QcrA) and a diheme cytochrome c
CC (QcrC) subunit. {ECO:0000250|UniProtKB:P9WP37}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35710.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL583920; CAC31260.1; -; Genomic_DNA.
DR EMBL; X51328; CAA35710.1; ALT_FRAME; Genomic_DNA.
DR PIR; A87019; A87019.
DR PIR; S08427; S08427.
DR RefSeq; NP_301665.1; NC_002677.1.
DR RefSeq; WP_010907989.1; NC_002677.1.
DR AlphaFoldDB; P15878; -.
DR SMR; P15878; -.
DR STRING; 272631.ML0879; -.
DR EnsemblBacteria; CAC31260; CAC31260; CAC31260.
DR KEGG; mle:ML0879; -.
DR PATRIC; fig|272631.5.peg.1610; -.
DR Leproma; ML0879; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_2_0_11; -.
DR OMA; WNYGPYD; -.
DR Proteomes; UP000000806; 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..551
FT /note="Cytochrome bc1 complex cytochrome b subunit"
FT /id="PRO_0000061926"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT REGION 532..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
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 127
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 215
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 230
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 551 AA; 61546 MW; 65BDC841D1DD3239 CRC64;
MSPKSVPDIG DVLARQAEDI DTRYHPSAAL RRQLNKVFPT HWSFLLGEIA LYSFIVLLLT
GVYLTLFFDP SMTDVTYNGV YQPLRGVEMS RAYQSTLDIS FEVRGGLFVR QIHHWAALMF
TAAIMVHLAR IFFTGAFRRP RETNWVIGSL LLILAMFEGY FGYSMPDDLL SGIGLRAALS
SITLGIPVIG TWLHWALFGG DFPGTILIPR LYALHILLIP GVILALIGLH LALVWFQKHT
QFPGPGRTEY NVVGVRVMPV FAFKSGAFFA AIVGVLGLMG GFLQINPIWN LGPYKPSQVS
AGSQPDFYMM WTEGLARIWP AWEFYFWHHT IPAPVWVAVI MALVFVLLIT YPFLEKRFTG
DYAHHNLLQR PRDVPVRTSI GAMAITFYMV LTLAAMNDII ALKFHISLNA TTWIGRIGMV
ILPLLVYFIT YRWCIGLQRS DRAVLEHGIE TGIIKRLPHG AYIELHQPLG PVDDHGHPIP
LEYQGTAVPK RMNKLGSAGS PSSGSFLFAD PVSEDAALRE ATHVAEQRAL TALREHQDSI
ASSPNGERGK H
