QCRA_MYCTU
ID QCRA_MYCTU Reviewed; 429 AA.
AC P9WH23; L0TBK9; Q10387;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Cytochrome bc1 complex Rieske iron-sulfur subunit;
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrA;
DE AltName: Full=Rieske iron-sulfur protein;
DE AltName: Full=Ubiquinol--cytochrome c reductase iron-sulfur subunit;
GN Name=qcrA; OrderedLocusNames=Rv2195; ORFNames=MTCY190.06;
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: Iron-sulfur 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:0000305}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000303|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44972.1; -; Genomic_DNA.
DR PIR; D70784; D70784.
DR RefSeq; NP_216711.1; NC_000962.3.
DR RefSeq; WP_003411396.1; NZ_NVQJ01000008.1.
DR PDB; 7E1V; EM; 2.68 A; A/M=1-429.
DR PDB; 7E1W; EM; 2.67 A; A/M=1-429.
DR PDB; 7E1X; EM; 2.93 A; A/M=1-429.
DR PDBsum; 7E1V; -.
DR PDBsum; 7E1W; -.
DR PDBsum; 7E1X; -.
DR AlphaFoldDB; P9WH23; -.
DR SMR; P9WH23; -.
DR STRING; 83332.Rv2195; -.
DR PaxDb; P9WH23; -.
DR DNASU; 888420; -.
DR GeneID; 888420; -.
DR KEGG; mtu:Rv2195; -.
DR PATRIC; fig|83332.111.peg.2442; -.
DR TubercuList; Rv2195; -.
DR eggNOG; COG0723; Bacteria.
DR OMA; LGCPTSL; -.
DR PhylomeDB; P9WH23; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR045603; QcrA_N.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF19297; QcrA_N; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cell membrane; Disulfide bond; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..429
FT /note="Cytochrome bc1 complex Rieske iron-sulfur subunit"
FT /id="PRO_0000127792"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 316..410
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 355
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 372
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 375
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 358..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 87..116
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 135..160
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 201..222
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:7E1W"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7E1V"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:7E1V"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:7E1W"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:7E1W"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:7E1W"
SQ SEQUENCE 429 AA; 46923 MW; C22C87EC283FE0EE CRC64;
MSRADDDAVG VPPTCGGRSD EEERRIVPGP NPQDGAKDGA KATAVPREPD EAALAAMSNQ
ELLALGGKLD GVRIAYKEPR WPVEGTKAEK RAERSVAVWL LLGGVFGLAL LLIFLFWPWE
FKAADGESDF IYSLTTPLYG LTFGLSILSI AIGAVLYQKR FIPEEISIQE RHDGASREID
RKTVVANLTD AFEGSTIRRR KLIGLSFGVG MGAFGLGTLV AFAGGLIKNP WKPVVPTAEG
KKAVLWTSGW TPRYQGETIY LARATGTEDG PPFIKMRPED MDAGGMETVF PWRESDGDGT
TVESHHKLQE IAMGIRNPVM LIRIKPSDLG RVVKRKGQES FNFGEFFAFT KVCSHLGCPS
SLYEQQSYRI LCPCHQSQFD ALHFAKPIFG PAARALAQLP ITIDTDGYLV ANGDFVEPVG
PAFWERTTT
