QOX1_STAHJ
ID QOX1_STAHJ Reviewed; 662 AA.
AC Q4L564;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable quinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Quinol oxidase polypeptide I;
GN Name=qoxB; OrderedLocusNames=SH1902;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds a copper B center. {ECO:0000250};
CC -!- COFACTOR:
CC Name=ferriheme a; Xref=ChEBI:CHEBI:60532; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Note=Heme A3. {ECO:0000250};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; AP006716; BAE05211.1; -; Genomic_DNA.
DR RefSeq; WP_011276174.1; NC_007168.1.
DR AlphaFoldDB; Q4L564; -.
DR SMR; Q4L564; -.
DR STRING; 279808.SH1902; -.
DR EnsemblBacteria; BAE05211; BAE05211; SH1902.
DR GeneID; 58061981; -.
DR KEGG; sha:SH1902; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_9; -.
DR OMA; WAMMSIG; -.
DR OrthoDB; 316745at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014233; QoxB.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02882; QoxB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport;
KW Ion transport; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..662
FT /note="Probable quinol oxidase subunit 1"
FT /id="PRO_0000276752"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 102
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CROSSLNK 279..283
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 662 AA; 74961 MW; 0E784C90F85CF13B CRC64;
MNFPWDQLLV KGNWMITMAQ IGAPFLVIGL IAVITYFKLW KYLYKEWFTS VDHKKIGLMY
LICAVLMFVR GGIDALLLRT QLTIPDNTFL ESNHYNEIFS THGVIMIIFM AMPFVFGLWN
VVVPLQIGAR DVAFPVMNNI SFWLFFVGMI LFNLSFIIGG SPAAGWTNYA PLAGEFSPGP
GVNYYLVAIQ ISGIGTLMTG INFFVTILRC KTPTMKFMQM PMFTVTTFIT TLIVILAFPV
FTVVLALMTF DRVFGTAFFT VADGGMPMLW ANFFWVWGHP EVYIVILPAF GIYSEIIPTF
ARKRLFGHQS MVWATAGIAF LSFLVWVHHF FTMGNGALIN SFFSISTMLI GVPTGVKLFN
WLLTLYKGRI TFESPMLFSL AFIPNFLLGG VTGVMLAMAS ADYQYHNTYF LVAHFHYTLV
TGVVFACLAG LIFWYPKMMG YKLNEKLNAW CFWLFMIGFN VCFLPQFILG LDGMPRRLYT
YMPSDGWWLL NVISTIGALL MAVGFLFLVV SIVYSHIKAP REATGDNWDG LGRTLEWSTA
SAIPPKYNFA ITPDWNDYDT FVDMKEHGRH YLDNHNYKDI HMPNNTHTGV IMGIFMLLGG
FFLIFETVIP AAICLVGILG SLVYQSFVQD HGYHIPASEV AENEARLREA RIKEREAVGH
ES
