ID   AOX2_AERPE              Reviewed;         234 AA.
AC   Q9YDX7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Heme-copper oxidase subunit 2;
DE            EC=1.9.3.-;
DE   AltName: Full=Heme-copper oxidase subunit II;
GN   Name=aoxA; OrderedLocusNames=APE_0792.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RA   Wakagi T., Ishikawa R.;
RT   "Heme-copper-oxidase.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA79770.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB020482; BAA86071.1; -; Genomic_DNA.
DR   EMBL; BA000002; BAA79770.2; ALT_INIT; Genomic_DNA.
DR   PIR; B72671; B72671.
DR   AlphaFoldDB; Q9YDX7; -.
DR   SMR; Q9YDX7; -.
DR   STRING; 272557.APE_0792.1; -.
DR   EnsemblBacteria; BAA79770; BAA79770; APE_0792.1.
DR   KEGG; ape:APE_0792.1; -.
DR   eggNOG; arCOG01235; Archaea.
DR   Proteomes; UP000002518; 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   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR045187; CcO_II.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF00116; COX2; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02866; CoxB; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Copper; Electron transport; Membrane; Metal-binding;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..234
FT                   /note="Heme-copper oxidase subunit 2"
FT                   /id="PRO_0000183723"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         151
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
FT   BINDING         188
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
FT   BINDING         192
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
FT   BINDING         196
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   234 AA;  26132 MW;  A89C9EB6D1361B6F CRC64;
     MDVIPTEAIW WRLFLLFTAV GVLAAGTVTA FFIYSLFKYR SSGQALGEDQ GTAGRIYRIM
     VESPVSGKSK YLLFVTGIIV MGLIVATIDE TLYLEKSPPV EDALVVMVIG FQFGWQFEYS
     VGGETVTTLN YLVVPSDTLI EFRVTSRDVF HAFGIPEFKN KIDAIPGILN SMWIKTPDEP
     GKVYNAYCYE LCGIGHSLMV GKVIVVDKEE FYNAYNSGPD VFSEYVNNVI SKYK