ID A0A0G3EQE5_9BURK Unreviewed; 131 AA.
AC A0A0G3EQE5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=ABW99_00140 {ECO:0000313|EMBL:AKJ66876.1};
OS Pandoraea thiooxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ66876.1, ECO:0000313|Proteomes:UP000036700};
RN [1] {ECO:0000313|Proteomes:UP000036700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011568; AKJ66876.1; -; Genomic_DNA.
DR RefSeq; WP_047212395.1; NZ_CP014839.1.
DR AlphaFoldDB; A0A0G3EQE5; -.
DR STRING; 445709.ABW99_00140; -.
DR KEGG; ptx:ABW99_00140; -.
DR PATRIC; fig|445709.3.peg.38; -.
DR OrthoDB; 2375888at2; -.
DR Proteomes; UP000036700; Chromosome.
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.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036700};
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 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 131 AA; 14203 MW; 799A61B5CF9CC140 CRC64;
MSAHDTALGD AGAHDHDEDE ELPHSTFSGY MTGFVLAVAL TALPFWIVMG SVFHRSGVTA
AAILLIGAVQ IVVHMIYFLH MDGKVQGGWS LLALIFTIVL VAIALSGSIW VMYHLNENMM
PGMMQPMHNP P
//
