ID   COX2_NOCFA              Reviewed;         375 AA.
AC   Q5YZ37;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable 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;
GN   Name=ctaC; OrderedLocusNames=NFA_17080;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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) (By
CC       similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds a copper A center. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
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}.
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DR   EMBL; AP006618; BAD56554.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YZ37; -.
DR   SMR; Q5YZ37; -.
DR   STRING; 247156.NFA_17080; -.
DR   EnsemblBacteria; BAD56554; BAD56554; NFA_17080.
DR   KEGG; nfa:NFA_17080; -.
DR   eggNOG; COG1622; Bacteria.
DR   HOGENOM; CLU_036876_3_1_11; -.
DR   OMA; HAFMPIA; -.
DR   Proteomes; UP000006820; 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: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; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF00116; COX2; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 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   Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..375
FT                   /note="Probable cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000183718"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          353..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         264
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255"
FT   BINDING         305
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255"
FT   BINDING         309
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255"
FT   BINDING         313
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  41976 MW;  51FE78E89A462104 CRC64;
     MCGDQEGVSV AHKASEEIGA RPVRGRQGRI LRRAGLAVSL GITAMLVSGC SIDNVWLRFG
     WPSGVTPQAT RMRELWTWSI IAALAMGVLV WGLTFWTVVF HRKKKDSPEF PRQTGYNVPL
     ELTYTAIPFV IIAVLFYFTV VVQNYVHEKV ADPDVTVDVT AFQWNWKFGY REVDFKDGGY
     QFNGIDTARE EAAQAQLKEY EERVDTEHGH PQPGPVHGKP ENDILSYLHY DTVETVGTST
     EIPVLVLPTG KVIEFQLAAA DVIHAFWVPE FLFKRDVMPN PKENHSDNVF QITEIEKEGA
     FVGRCAEMCG TYHSMMNFEV RAVSPEKFTR YLDERRAGKT NAEALAAIGE SPVATSTRPF
     NTDRTVKSAA APEAE