ID D7UV06_LISGR Unreviewed; 109 AA.
AC D7UV06;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:EFI85082.1};
GN ORFNames=HMPREF0556_10281 {ECO:0000313|EMBL:EFI85082.1};
OS Listeria grayi DSM 20601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI85082.1, ECO:0000313|Proteomes:UP000010119};
RN [1] {ECO:0000313|EMBL:EFI85082.1, ECO:0000313|Proteomes:UP000010119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI85082.1,
RC ECO:0000313|Proteomes:UP000010119};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) 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:EFI85082.1}.
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DR EMBL; ACCR02000002; EFI85082.1; -; Genomic_DNA.
DR RefSeq; WP_003756760.1; NZ_GL538352.1.
DR AlphaFoldDB; D7UV06; -.
DR STRING; 525367.HMPREF0556_10281; -.
DR eggNOG; COG3125; Bacteria.
DR HOGENOM; CLU_140945_2_0_9; -.
DR Proteomes; UP000010119; 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 Reference proteome {ECO:0000313|Proteomes:UP000010119};
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 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
SQ SEQUENCE 109 AA; 12304 MW; 0C489A5F3CB78522 CRC64;
MAENKNSTQT HKAHGPWQHI IGFALSIILT LLAVWVALYS TLDHSVKVVI IFIFAFIQAM
LQLFMFMHMT EGKDGKVNTS GILFALFIAI IVVIGSYWVM EIGHMNHLM
//
