ID   QOX2_STAEQ              Reviewed;         374 AA.
AC   Q5HQA9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=SERP0646;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
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. 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}.
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DR   EMBL; CP000029; AAW53984.1; -; Genomic_DNA.
DR   RefSeq; WP_001831736.1; NC_002976.3.
DR   AlphaFoldDB; Q5HQA9; -.
DR   SMR; Q5HQA9; -.
DR   STRING; 176279.SERP0646; -.
DR   EnsemblBacteria; AAW53984; AAW53984; SERP0646.
DR   GeneID; 50019101; -.
DR   KEGG; ser:SERP0646; -.
DR   eggNOG; COG1622; Bacteria.
DR   HOGENOM; CLU_036876_6_0_9; -.
DR   OMA; TAMNSFF; -.
DR   OrthoDB; 1654242at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Respiratory chain; Signal; Transmembrane;
KW   Transmembrane helix; 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_0000275881"
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