ID   COX2_THEVL              Reviewed;         327 AA.
AC   P98054;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome aa3 subunit 2;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
DE   AltName: Full=Oxidase aa(3) subunit 2;
DE   Flags: Precursor;
GN   Name=ctaC;
OS   Thermostichus vulcanus (Synechococcus vulcanus).
OC   Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX   NCBI_TaxID=32053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1659815; DOI=10.1016/s0006-291x(05)81438-x;
RA   Tano H., Sone N.;
RT   "The cytochrome C oxidase genes in blue-green algae and characteristics of
RT   the deduced protein sequence for subunit II of the thermophilic
RT   cyanobacterium Synechococcus vulcanus.";
RL   Biochem. Biophys. Res. Commun. 181:437-442(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8399373; DOI=10.1016/0005-2728(93)90012-5;
RA   Sone N., Tano H., Ishizuka M.;
RT   "The genes in the thermophilic cyanobacterium Synechococcus vulcanus
RT   encoding cytochrome-c oxidase.";
RL   Biochim. Biophys. Acta 1183:130-138(1993).
CC   -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC       complex. Electrons originating in cytochrome c are transferred via heme
CC       a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds a copper A center.;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; D16254; BAA41040.1; -; Genomic_DNA.
DR   AlphaFoldDB; P98054; -.
DR   SMR; P98054; -.
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:UniProtKB-EC.
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; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Copper; Electron transport; Membrane; Metal-binding;
KW   Respiratory chain; Signal; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..327
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000006064"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         221
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
FT   BINDING         255
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
FT   BINDING         259
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
FT   BINDING         263
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  35356 MW;  2C28F9C68D3B7A13 CRC64;
     MEQIPASIWT LTAGVVVTLI SFWVGHHHGL LPEQASEQAP LVDNFFDIML TIGTALFLVV
     QGAIILFVIR YRRRAGEEGD GLPVEGNLPL EAFWTAIPAL IVIFLGIYSV DIFQRMGGLN
     PGDHAMHSMH APKSGMAVVA QAPSKTTSDA TALLAAAQPP EIGIGASPDV QGKAPDLVVD
     VAGMQYAWIF TYPDSGIVSG ELHIPVGKDV QLNLSARDVI HSFWVPQFRL KQDAIPGVPT
     TRFKATKVGT YPVVCAELCG GYHGAMRTQV IVHTPEDFET WRRQNQAIAT APVIPSLRDR
     HIHEMGVTAE LVAQVEAIAH DPSAEKL