ID Q9LBY0_SHEVI Unreviewed; 111 AA.
AC Q9LBY0;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 4 {ECO:0000256|ARBA:ARBA00014689};
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 4 {ECO:0000256|ARBA:ARBA00032185};
DE AltName: Full=Oxidase bo(3) subunit 4 {ECO:0000256|ARBA:ARBA00030071};
DE AltName: Full=Ubiquinol oxidase polypeptide IV {ECO:0000256|ARBA:ARBA00030211};
DE AltName: Full=Ubiquinol oxidase subunit 4 {ECO:0000256|ARBA:ARBA00031887};
GN Name=cyoD {ECO:0000313|EMBL:BAA94867.1};
OS Shewanella violacea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60217 {ECO:0000313|EMBL:BAA94867.1};
RN [1] {ECO:0000313|EMBL:BAA94867.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11330692; DOI=10.1271/bbb.65.690;
RA Nakasone K., Yamada M., Qureshi M.H., Kato C., Horikoshi K.;
RT "Piezoresponse of the cyo-operon coding for quinol oxidase subunits in a
RT deep-sea piezophilic bacterium, Shewanella violacea.";
RL Biosci. Biotechnol. Biochem. 65:690-693(2001).
CC -!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component
CC of the aerobic respiratory chain of E.coli that predominates when cells
CC are grown at high aeration. Has proton pump activity across the
CC membrane in addition to electron transfer, pumping 2 protons/electron.
CC {ECO:0000256|ARBA:ARBA00025694}.
CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains and
CC two D chains. {ECO:0000256|ARBA:ARBA00011700}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase bacterial subunit 4
CC family. {ECO:0000256|ARBA:ARBA00008079}.
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DR EMBL; AB033827; BAA94867.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LBY0; -.
DR OMA; SLWIMHN; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR InterPro; IPR005171; Cyt_c_oxidase_su4_prok.
DR InterPro; IPR014210; Cyt_o_ubiqinol_oxidase_su4.
DR NCBIfam; TIGR02847; CyoD; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 111 AA; 12447 MW; 300E9C79259F6F2A CRC64;
MSQAHTSESL TSDDFMASVK SYLVGFLLSV ILTGIPFWAV MTHHFEKPIT LGLVLVMAVV
QIVVHLKYFL HLDFSKEGKI NTFSFLFTAL IMVMVMGLSV WIIYAANALM M
//
