QOX2_STAES
ID QOX2_STAES Reviewed; 374 AA.
AC Q8CPP6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Probable quinol oxidase subunit 2;
DE EC=1.10.3.-;
DE AltName: Full=Quinol oxidase polypeptide II;
DE Flags: Precursor;
GN Name=qoxA; OrderedLocusNames=SE_0759;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. Subunit II transfers the electrons from a quinol to
CC the binuclear center of the catalytic subunit I (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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; AE015929; AAO04356.1; -; Genomic_DNA.
DR RefSeq; NP_764314.1; NC_004461.1.
DR RefSeq; WP_001831736.1; NZ_WBME01000028.1.
DR AlphaFoldDB; Q8CPP6; -.
DR SMR; Q8CPP6; -.
DR STRING; 176280.SE_0759; -.
DR EnsemblBacteria; AAO04356; AAO04356; SE_0759.
DR GeneID; 50019101; -.
DR KEGG; sep:SE_0759; -.
DR PATRIC; fig|176280.10.peg.731; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_6_0_9; -.
DR OMA; TAMNSFF; -.
DR Proteomes; UP000001411; 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:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR CDD; cd04212; CuRO_UO_II; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034227; CuRO_UO_II.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR InterPro; IPR006332; QoxA.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR01432; QOXA; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Lipoprotein; Membrane; Oxidoreductase;
KW Palmitate; Respiratory chain; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..374
FT /note="Probable quinol oxidase subunit 2"
FT /id="PRO_0000275880"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 317..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 374 AA; 42872 MW; 68682F878B29D412 CRC64;
MSKFKSLLLL FGTLILLSGC SNIEVFNAKG PVASSQKFLI IYSIIFMLVI VAVVLSMFAI
FIFKYSYKKN SESGKMHHNS LIETIWFVVP ILIVIALAIP TVKTLYDYEK PPEKDKDPLV
VYAVSAGYKW FFAYPDQHIE TVNTLTIPKD RPVVFKLQSM DTMTSFWIPQ LGGQKYAMTG
MTMNWTLTAD QLGTFRGRNS NFNGEGFSRQ TFKVHSVSQN DFDKWVKEAK GKKTLSQDTF
DKQLLPSTSN KELTFSGTHM AFVDPAADPE YIFYAYKRYN FEQKDPNFTA EEDLYKDVKD
KPIKPARKVH ITNPNYERHG MKPMILGNNE KYDNEFKKEE DHNSKEMEKI SKGAKDENAS
KLHKKEHDDH GGGH
