QCRC_MYCTU
ID QCRC_MYCTU Reviewed; 280 AA.
AC P9WP35; L0TBS3; P63887; Q10386;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cytochrome bc1 complex cytochrome c subunit;
DE EC=7.1.1.8 {ECO:0000305};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrC;
DE AltName: Full=Ubiquinol--cytochrome c reductase cytochrome c subunit;
GN Name=qcrC; OrderedLocusNames=Rv2194; ORFNames=MTCY190.05;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000305}.
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; Evidence={ECO:0000305};
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:0000305}.
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}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000303|PubMed:19099550}.
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DR EMBL; AL123456; CCP44971.1; -; Genomic_DNA.
DR PIR; C70784; C70784.
DR RefSeq; NP_216710.1; NC_000962.3.
DR RefSeq; WP_003411392.1; NZ_NVQJ01000008.1.
DR PDB; 7E1V; EM; 2.68 A; C/O=2-280.
DR PDB; 7E1W; EM; 2.67 A; C/O=2-280.
DR PDB; 7E1X; EM; 2.93 A; C/O=2-280.
DR PDBsum; 7E1V; -.
DR PDBsum; 7E1W; -.
DR PDBsum; 7E1X; -.
DR AlphaFoldDB; P9WP35; -.
DR SMR; P9WP35; -.
DR STRING; 83332.Rv2194; -.
DR PaxDb; P9WP35; -.
DR PRIDE; P9WP35; -.
DR DNASU; 888737; -.
DR GeneID; 45426170; -.
DR GeneID; 888737; -.
DR KEGG; mtu:Rv2194; -.
DR PATRIC; fig|83332.111.peg.2441; -.
DR TubercuList; Rv2194; -.
DR eggNOG; COG2010; Bacteria.
DR OMA; LFRTNCA; -.
DR PhylomeDB; P9WP35; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Repeat; Respiratory chain; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..280
FT /note="Cytochrome bc1 complex cytochrome c subunit"
FT /id="PRO_0000108450"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 60..140
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 161..239
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 73
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 76
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 77
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 174
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 177
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 178
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"
FT TURN 63..68
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7E1V"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7E1V"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:7E1W"
SQ SEQUENCE 280 AA; 29138 MW; 7A058AE7E12EF713 CRC64;
MTKLGFTRSG GSKSGRTRRR LRRRLSGGVL LLIALTIAGG LAAVLTPTPQ VAVADESSSA
LLRTGKQLFD TSCVSCHGAN LQGVPDHGPS LIGVGEAAVY FQVSTGRMPA MRGEAQAPRK
DPIFDEAQID AIGAYVQANG GGPTVVRNPD GSIATQSLRG NDLGRGGDLF RLNCASCHNF
TGKGGALSSG KYAPDLAPAN EQQILTAMLT GPQNMPKFSN RQLSFEAKKD IIAYVKVATE
ARQPGGYLLG GFGPAPEGMA MWIIGMVAAI GLALWIGARS
