ID   QOX2_SULAC              Reviewed;         168 AA.
AC   P39479; Q4J748;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Quinol oxidase subunit 2;
DE            EC=1.10.3.-;
DE   AltName: Full=Cytochrome aa3 subunit 2;
DE   AltName: Full=Oxidase aa(3) subunit 2;
DE   AltName: Full=Quinol oxidase polypeptide II;
GN   Name=soxA; OrderedLocusNames=Saci_2089;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=1372250; DOI=10.1002/j.1460-2075.1992.tb05117.x;
RA   Luebben M., Kolmerer B., Saraste M.;
RT   "An archaebacterial terminal oxidase combines core structures of two
RT   mitochondrial respiratory complexes.";
RL   EMBO J. 11:805-812(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: The terminal oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex.
CC   -!- FUNCTION: Subunit 2 transfers the electrons from caldariella quinol to
CC       the bimetallic center of the catalytic subunit 1 that is formed by heme
CC       A3 and Cu(B).
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; Single-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X62643; CAA44509.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY81383.1; -; Genomic_DNA.
DR   PIR; S21041; S21041.
DR   RefSeq; WP_011278885.1; NC_007181.1.
DR   AlphaFoldDB; P39479; -.
DR   SMR; P39479; -.
DR   STRING; 330779.Saci_2089; -.
DR   TCDB; 3.D.4.1.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR   EnsemblBacteria; AAY81383; AAY81383; Saci_2089.
DR   GeneID; 3472602; -.
DR   KEGG; sai:Saci_2089; -.
DR   PATRIC; fig|330779.12.peg.2091; -.
DR   eggNOG; arCOG01236; Archaea.
DR   HOGENOM; CLU_1582965_0_0_2; -.
DR   OMA; ELAWFIV; -.
DR   BioCyc; MetaCyc:MON-21017; -.
DR   BRENDA; 7.1.1.4; 6160.
DR   Proteomes; UP000001018; 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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; ISS:UniProtKB.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; ISS:UniProtKB.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR008972; Cupredoxin.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Membrane; Oxidoreductase;
KW   Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..168
FT                   /note="Quinol oxidase subunit 2"
FT                   /id="PRO_0000183725"
FT   TRANSMEM        9..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   168 AA;  18874 MW;  7B5C98CA24D06846 CRC64;
     MDIKEHAEEV WFIVMLVLVL IFFSWNVYYL STGKSFSLDY GLPTYSGLPE QAQKAVQYFD
     SHPPSPGQYS EVINGMLVVN LTATQYKWTP DLIVVNKSEP VVLIINSPQV DTGFYLRTPD
     GVINLNNVAG ITSYAYFVIN QPGNYTWRDA EYAGYNSSYM TGTVEVVG