QOX1_STAAC
ID QOX1_STAAC Reviewed; 662 AA.
AC Q5HH24;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable quinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Quinol oxidase polypeptide I;
GN Name=qoxB; OrderedLocusNames=SACOL1069;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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; CP000046; AAW36533.1; -; Genomic_DNA.
DR RefSeq; WP_001010768.1; NC_002951.2.
DR AlphaFoldDB; Q5HH24; -.
DR SMR; Q5HH24; -.
DR EnsemblBacteria; AAW36533; AAW36533; SACOL1069.
DR KEGG; sac:SACOL1069; -.
DR HOGENOM; CLU_011899_7_1_9; -.
DR OMA; WAMMSIG; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000000530; 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_0000276742"
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 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..627
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; 75229 MW; FF2F5BE53DA5C13C CRC64;
MNFPWDQLLV KGNWMITMAQ IGAPFLVIGL IAVITYFKLW KYLYKEWFTS VDHKKIGVMY
LICAVLMFVR GGIDALLIRA QLTVPDNKFL ESNHYNEIFS THGVIMIIFM AMPFIFGLWN
IVVPLQIGAR DVAFPVLNNV SFWLFFAGMI LFNLSFIIGG SPAAGWTNYA PLAGEFSPGP
GVNYYLIAIQ ISGLGTLATG INFFVTILRC KTPTMKFMQM PMFTVTTFIT TLIVILAFPP
LTVALALMTT DRIFDTAFFT VAHGGMPMLW ANFFWVWGHP EVYIVILPAF GIYSEIIPTF
ARKRLFGHQS MVWATAGIAF LSFLVWVHHF FTMGNGALIN SFFSISTMLI GIPTGVKLFN
WLLTLYKGRI TFESPMLFSL AFIPNFLLGG VTGVMLAMAS ADYQYHNTYF LVAHFHYTLV
TGVVFACLAG LIFWYPKMMG YKLNETLNKW CFWFFMIGFN VCFLPQFILG LDGMPRRLYT
YMPSDGWFLL NLISTIGALL MAIGFLFLVV SIVYSHFKSP REATGDNWDG LGRTLEWTTA
SAIPPKYNFA ITPDWNDYDT FVDMKEHGRH YLDNHNYKDI HMPNNTPVGF WIGIFMTIGG
FFLIFETVIP ALICLFGIFG TMIYRSFQID HGYHIPAAEV AETEARLREA RIKEREAVSH
ES
