QOX1_BACSH
ID QOX1_BACSH Reviewed; 649 AA.
AC E0TW66;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Quinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Oxidase aa(3)-600 subunit 1;
DE AltName: Full=Quinol oxidase aa3-600, subunit qoxB;
DE AltName: Full=Quinol oxidase polypeptide I;
GN Name=qoxB; OrderedLocusNames=BSUW23_18870;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(2011).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=7575098; DOI=10.1007/bf00272132;
RA Lemma E., Simon J., Schagger H., Kroger A.;
RT "Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of
RT Bacillus subtilis.";
RL Arch. Microbiol. 163:432-438(1995).
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. Major component for energy conversion during
CC vegetative growth.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:132124;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds a copper B center.;
CC -!- COFACTOR:
CC Name=ferriheme a; Xref=ChEBI:CHEBI:60532;
CC -!- COFACTOR:
CC Note=Heme A3.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; CP002183; ADM39808.1; -; Genomic_DNA.
DR RefSeq; WP_003222173.1; NC_014479.1.
DR AlphaFoldDB; E0TW66; -.
DR SMR; E0TW66; -.
DR EnsemblBacteria; ADM39808; ADM39808; BSUW23_18870.
DR GeneID; 64305590; -.
DR KEGG; bss:BSUW23_18870; -.
DR HOGENOM; CLU_011899_7_1_9; -.
DR OMA; WAMMSIG; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002233; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014233; QoxB.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02882; QoxB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport;
KW Ion transport; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="Quinol oxidase subunit 1"
FT /id="PRO_0000402829"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 102
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 329
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 415
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 417
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 280..284
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 649 AA; 73821 MW; FD9C8F04AC8E2D88 CRC64;
MKFKWDEFFV TGDPLILGAQ VSIALSTIAI IFVLTYFKKW KWLWSEWITT VDHKKLGIMY
IISAVIMLFR GGVDGLMMRA QLALPNNSFL DSNHYNEIFT THGTIMIIFM AMPFLIGLIN
VVVPLQIGAR DVAFPYLNNL SFWTFFVGAM LFNISFVIGG SPNAGWTSYM PLASNDMSPG
PGENYYLLGL QIAGIGTLMT GINFMVTILK MRTKGMTLMR MPMFTWTTLI TMVIIVFAFP
VLTVALALLS FDRLFGAHFF TLEAGGMPML WANLFWIWGH PEVYIVILPA FGIFSEIISS
FARKQLFGYT AMVGSIIAIS VLSFLVWTHH FFTMGNSASV NSFFSITTMA ISIPTGVKIF
NWLFTMYKGR ISFTTPMLWA LAFIPNFVIG GVTGVMLAMA AADYQYHNTY FLVSHFHYVL
IAGTVFACFA GFIFWYPKMF GHKLNERIGK WFFWIFMIGF NICFFPQYFL GLQGMPRRIY
TYGPNDGWTT LNFISTVGAF MMGVGFLILC YNIYYSFRYS TREISGDSWG VGRSLDWATS
SAIPPHYNFA VLPEVKSKDA FHHMKEEKTE LYPESKFKKI HMPSNSGRPF FMSVAFGIAG
FGLVFEWYWM GVVGLIGVLL CMVLRSFEYD NGYYISVDEI KETERKISE
