ID   COX4_PARDE              Reviewed;          50 AA.
AC   P77921;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Cytochrome c oxidase subunit 4;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome aa3 subunit 4;
DE   AltName: Full=Cytochrome c oxidase polypeptide IV;
GN   Name=ctaH;
OS   Paracoccus denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Pd 1222;
RX   PubMed=9038156; DOI=10.1074/jbc.272.9.5514;
RA   Witt H., Ludwig B.;
RT   "Isolation, analysis, and deletion of the gene coding for subunit IV of
RT   cytochrome c oxidase in Paracoccus denitrificans.";
RL   J. Biol. Chem. 272:5514-5517(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-32.
RX   PubMed=8068652; DOI=10.1021/bi00198a044;
RA   Haltia T., Semo N., Arrondo J.L., Goni F.M., Freire E.;
RT   "Thermodynamic and structural stability of cytochrome c oxidase from
RT   Paracoccus denitrificans.";
RL   Biochemistry 33:9731-9740(1994).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=7651515; DOI=10.1038/376660a0;
RA   Iwata S., Ostermeier C., Ludwig B., Michel H.;
RT   "Structure at 2.8-A resolution of cytochrome c oxidase from Paracoccus
RT   denitrificans.";
RL   Nature 376:660-669(1995).
CC   -!- FUNCTION: Not required for enzymatic activity or proton pumping of the
CC       cytochrome c oxidase complex. {ECO:0000269|PubMed:9038156}.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
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DR   EMBL; Y08372; CAA69659.1; -; Genomic_DNA.
DR   RefSeq; WP_041529744.1; NZ_PPGA01000010.1.
DR   PDB; 1QLE; X-ray; 3.00 A; D=8-50.
DR   PDB; 7ATE; EM; 2.40 A; D=1-50.
DR   PDB; 7ATN; EM; 2.66 A; D=1-50.
DR   PDB; 7AU3; EM; 2.56 A; D=1-50.
DR   PDB; 7AU6; EM; 2.40 A; D=1-50.
DR   PDBsum; 1QLE; -.
DR   PDBsum; 7ATE; -.
DR   PDBsum; 7ATN; -.
DR   PDBsum; 7AU3; -.
DR   PDBsum; 7AU6; -.
DR   AlphaFoldDB; P77921; -.
DR   EMDB; EMD-11921; -.
DR   EMDB; EMD-11922; -.
DR   EMDB; EMD-11924; -.
DR   EMDB; EMD-11925; -.
DR   SMR; P77921; -.
DR   GeneID; 75499980; -.
DR   EvolutionaryTrace; P77921; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.5.160; Bacterial aa3 type cytochrome c oxidase subunit IV; 1.
DR   InterPro; IPR036596; Cyt-C_aa3_sf.
DR   InterPro; IPR012422; Cyt_c_oxidase_su4_bac-aa3.
DR   Pfam; PF07835; COX4_pro_2; 1.
DR   SUPFAM; SSF81469; Bacterial aa3 type cytochrome c oxidase subunit IV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane;
KW   Direct protein sequencing; Membrane; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8068652"
FT   CHAIN           2..50
FT                   /note="Cytochrome c oxidase subunit 4"
FT                   /id="PRO_0000183904"
FT   TOPO_DOM        2..17
FT                   /note="Cytoplasmic"
FT   TRANSMEM        18..49
FT                   /note="Helical"
FT   TOPO_DOM        50
FT                   /note="Periplasmic"
FT   HELIX           18..49
FT                   /evidence="ECO:0007829|PDB:7ATE"
SQ   SEQUENCE   50 AA;  5501 MW;  1D6B6674CAF5EC88 CRC64;
     MASHHEITDH KHGEMDIRHQ QATFAGFIKG ATWVSILSIA VLVFLALANS
//