ID S2XKA2_9STAP Unreviewed; 96 AA.
AC S2XKA2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Quinol oxidase subunit 4 {ECO:0000256|RuleBase:RU367153};
DE EC=1.10.3.- {ECO:0000256|RuleBase:RU367153};
GN ORFNames=HMPREF1208_00461 {ECO:0000313|EMBL:EPD52401.1};
OS Staphylococcus sp. HGB0015.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1078083 {ECO:0000313|EMBL:EPD52401.1, ECO:0000313|Proteomes:UP000014407};
RN [1] {ECO:0000313|EMBL:EPD52401.1, ECO:0000313|Proteomes:UP000014407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0015 {ECO:0000313|EMBL:EPD52401.1,
RC ECO:0000313|Proteomes:UP000014407};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Staphylococcus sp. HGB0015.";
RL Submitted (APR-2013) 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:EPD52401.1}.
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DR EMBL; AGEO01000004; EPD52401.1; -; Genomic_DNA.
DR RefSeq; WP_016424723.1; NZ_KE150417.1.
DR AlphaFoldDB; S2XKA2; -.
DR GeneID; 72414834; -.
DR PATRIC; fig|1078083.3.peg.456; -.
DR eggNOG; COG3125; Bacteria.
DR HOGENOM; CLU_140945_2_0_9; -.
DR Proteomes; UP000014407; 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:UP000014407};
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 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
SQ SEQUENCE 96 AA; 10692 MW; A29AA0D57340D54A CRC64;
MNTIVKHTIG FIASIILTLL AVFVTLYTSL SFNAKVTIIF GFAFIQAFLQ LLMFMHLTEG
KNGRIQLAKV LFAIIITLVI VIGTYWVMQG GHGHHI
//