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QCRC_MYCBO
ID   QCRC_MYCBO              Reviewed;         280 AA.
AC   P63888; A0A1R3Y186; Q10386; X2BKD0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cytochrome bc1 complex cytochrome c subunit;
DE            EC=7.1.1.8 {ECO:0000250|UniProtKB:P9WP35};
DE   AltName: Full=Cytochrome bc1 reductase complex subunit QcrC;
DE   AltName: Full=Ubiquinol--cytochrome c reductase cytochrome c subunit;
GN   Name=qcrC; OrderedLocusNames=BQ2027_MB2217;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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:0000250|UniProtKB:P9WP35}.
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:P9WP35};
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:P9WP35}.
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}.
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DR   EMBL; LT708304; SIU00825.1; -; Genomic_DNA.
DR   RefSeq; NP_855866.1; NC_002945.3.
DR   RefSeq; WP_003411392.1; NC_002945.4.
DR   AlphaFoldDB; P63888; -.
DR   SMR; P63888; -.
DR   EnsemblBacteria; SIU00825; SIU00825; BQ2027_MB2217.
DR   GeneID; 45426170; -.
DR   PATRIC; fig|233413.5.peg.2433; -.
DR   OMA; LFRTNCA; -.
DR   Proteomes; UP000001419; 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: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   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Repeat; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..280
FT                   /note="Cytochrome bc1 complex cytochrome c subunit"
FT                   /id="PRO_0000108448"
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"
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
 
 
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