ID A0A101XR14_9BACL Unreviewed; 113 AA.
AC A0A101XR14;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Quinol oxidase subunit 4 {ECO:0000256|RuleBase:RU367153};
DE EC=1.10.3.- {ECO:0000256|RuleBase:RU367153};
GN ORFNames=ATW55_02435 {ECO:0000313|EMBL:KUO95957.1};
OS Ferroacidibacillus organovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Ferroacidibacillus.
OX NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO95957.1, ECO:0000313|Proteomes:UP000053557};
RN [1] {ECO:0000313|EMBL:KUO95957.1, ECO:0000313|Proteomes:UP000053557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITV001 {ECO:0000313|EMBL:KUO95957.1,
RC ECO:0000313|Proteomes:UP000053557};
RA Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L., Pylro V.,
RA Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J., Orellana S.C.,
RA Oliveira G.;
RT "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated from
RT a chalcopyrite acid mine drainage site in Brazil.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. {ECO:0000256|RuleBase:RU367153}.
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; Evidence={ECO:0000256|ARBA:ARBA00000725,
CC ECO:0000256|RuleBase:RU367153};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU367153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU367153}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase bacterial subunit 4
CC family. {ECO:0000256|ARBA:ARBA00008079, ECO:0000256|RuleBase:RU367153}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO95957.1}.
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DR EMBL; LPVJ01000030; KUO95957.1; -; Genomic_DNA.
DR RefSeq; WP_067715269.1; NZ_LPVJ01000030.1.
DR AlphaFoldDB; A0A101XR14; -.
DR OrthoDB; 2375888at2; -.
DR Proteomes; UP000053557; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:UniProtKB-UniRule.
DR InterPro; IPR005171; Cyt_c_oxidase_su4_prok.
DR InterPro; IPR014250; QoxD.
DR NCBIfam; TIGR02901; QoxD; 1.
DR PANTHER; PTHR36835; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 4; 1.
DR PANTHER; PTHR36835:SF1; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 4; 1.
DR Pfam; PF03626; COX4_pro; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367153};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367153};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367153};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367153};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367153}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
SQ SEQUENCE 113 AA; 12301 MW; 6A02A95CE1C7E291 CRC64;
MDTSHHDGHE HTAVSTHREG FPWKDIIGLV LSLALTFASL HIVLTHALPL GELITAIVVL
AVFQLFVQLF LFMHLTEKTG TRSNIGALAF GLFVAFTIVA GSIWIMAFNS TAS
//
