ID I2HWQ5_9BACI Unreviewed; 122 AA.
AC I2HWQ5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Quinol oxidase subunit 4 {ECO:0000256|RuleBase:RU367153};
DE EC=1.10.3.- {ECO:0000256|RuleBase:RU367153};
GN ORFNames=MY7_3528 {ECO:0000313|EMBL:EIF15164.1};
OS Bacillus sp. 5B6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1127743 {ECO:0000313|EMBL:EIF15164.1, ECO:0000313|Proteomes:UP000005799};
RN [1] {ECO:0000313|EMBL:EIF15164.1, ECO:0000313|Proteomes:UP000005799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5B6 {ECO:0000313|EMBL:EIF15164.1,
RC ECO:0000313|Proteomes:UP000005799};
RX PubMed=22740678; DOI=10.1128/JB.00682-12;
RA Kim B.K., Chung J.H., Kim S.Y., Jeong H., Kang S.G., Kwon S.K., Lee C.H.,
RA Song J.Y., Yu D.S., Ryu C.M., Kim J.F.;
RT "Genome Sequence of the Leaf-Colonizing Bacterium Bacillus sp. Strain 5B6,
RT Isolated from a Cherry Tree.";
RL J. Bacteriol. 194:3758-3759(2012).
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:EIF15164.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJST01000001; EIF15164.1; -; Genomic_DNA.
DR RefSeq; WP_007614576.1; NZ_AJST01000001.1.
DR AlphaFoldDB; I2HWQ5; -.
DR GeneID; 75093436; -.
DR PATRIC; fig|1127743.3.peg.3456; -.
DR Proteomes; UP000005799; 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..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367153"
SQ SEQUENCE 122 AA; 13484 MW; A4D765CD874F193F CRC64;
MANKSAEHSH FPWKHIVGFA LSIILTLLAL WVAVYTDLSS SAKLWIIFGF AFIQAGLQLL
MFMHMTESEN GGIQVGNTLF GFFGAIVIIL GSIWIFAAHY HHGDHMDGNP PGGAKHHSEH
QE
//
