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Database: UniProt
Entry: F3M2A4_9BACL
LinkDB: F3M2A4_9BACL
Original site: F3M2A4_9BACL 
ID   F3M2A4_9BACL            Unreviewed;        95 AA.
AC   F3M2A4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Quinol oxidase subunit 4 {ECO:0000256|RuleBase:RU367153};
DE            EC=1.10.3.- {ECO:0000256|RuleBase:RU367153};
GN   Name=qoxD {ECO:0000313|EMBL:EGG38447.1};
GN   ORFNames=HMPREF9412_0618 {ECO:0000313|EMBL:EGG38447.1};
OS   Paenibacillus sp. HGF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG38447.1, ECO:0000313|Proteomes:UP000004272};
RN   [1] {ECO:0000313|EMBL:EGG38447.1, ECO:0000313|Proteomes:UP000004272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF5 {ECO:0000313|EMBL:EGG38447.1,
RC   ECO:0000313|Proteomes:UP000004272};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) 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:EGG38447.1}.
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DR   EMBL; AEXS01000009; EGG38447.1; -; Genomic_DNA.
DR   RefSeq; WP_009589381.1; NZ_AEXS01000009.1.
DR   AlphaFoldDB; F3M2A4; -.
DR   OrthoDB; 2361460at2; -.
DR   Proteomes; UP000004272; 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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367153"
FT   TRANSMEM        37..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367153"
FT   TRANSMEM        67..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367153"
SQ   SEQUENCE   95 AA;  10387 MW;  C9FC11C526376634 CRC64;
     MLKQLFPIKH VAGYISSLVL SAVALVVLLD MPAASKVAVL LVTAILQAAV QLMLFMHVGE
     SEDKKSVYIN IAFALFVGLV TIFGTLFIFI WGWYA
//
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