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QCRB_MYCTO
ID   QCRB_MYCTO              Reviewed;         549 AA.
AC   P9WP36; L0TAG7; P63885; Q10388;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
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; OrderedLocusNames=MT2252;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
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DR   EMBL; AE000516; AAK46538.1; -; Genomic_DNA.
DR   PIR; E70784; E70784.
DR   RefSeq; WP_003899212.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP36; -.
DR   SMR; P9WP36; -.
DR   EnsemblBacteria; AAK46538; AAK46538; MT2252.
DR   GeneID; 45426172; -.
DR   KEGG; mtc:MT2252; -.
DR   PATRIC; fig|83331.31.peg.2427; -.
DR   HOGENOM; CLU_031114_2_0_11; -.
DR   Proteomes; UP000001020; 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   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..549
FT                   /note="Cytochrome bc1 complex cytochrome b subunit"
FT                   /id="PRO_0000427020"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         114
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         128
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         216
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         231
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   549 AA;  61014 MW;  0E75E0BCAA46B3A7 CRC64;
     MSPKLSPPNI GEVLARQAED IDTRYHPSAA LRRQLNKVFP THWSFLLGEI ALYSFVVLLI
     TGVYLTLFFD PSMVDVTYNG VYQPLRGVEM SRAYQSALDI SFEVRGGLFV RQIHHWAALM
     FAAAIMVHLA RIFFTGAFRR PRETNWVIGS LLLILAMFEG YFGYSLPDDL LSGLGLRAAL
     SSITLGMPVI GTWLHWALFG GDFPGTILIP RLYALHILLL PGIILALIGL HLALVWFQKH
     TQFPGPGRTE HNVVGVRVMP VFAFKSGAFF AAIVGVLGLM GGLLQINPIW NLGPYKPSQV
     SAGSQPDFYM MWTEGLARIW PPWEFYFWHH TIPAPVWVAV IMGLVFVLLP AYPFLEKRFT
     GDYAHHNLLQ RPRDVPVRTA IGAMAIAFYM VLTLAAMNDI IALKFHISLN ATTWIGRIGM
     VILPPFVYFI TYRWCIGLQR SDRSVLEHGV ETGIIKRLPH GAYIELHQPL GPVDEHGHPI
     PLQYQGAPLP KRMNKLGSAG SPGSGSFLFA DSAAEDAALR EAGHAAEQRA LAALREHQDS
     IMGSPDGEH
 
 
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