ID   COX1_ALKPO              Reviewed;         625 AA.
AC   Q04440; D3FU49;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 3.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome aa3 subunit 1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=ctaD; OrderedLocusNames=BpOF4_00910;
OS   Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS   (Bacillus pseudofirmus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX   NCBI_TaxID=398511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RX   PubMed=7678007; DOI=10.1016/s0021-9258(18)54205-8;
RA   Quirk P.G., Hicks D.B., Krulwich T.A.;
RT   "Cloning of the cta operon from alkaliphilic Bacillus firmus OF4 and
RT   characterization of the pH-regulated cytochrome caa3 oxidase it encodes.";
RL   J. Biol. Chem. 268:678-685(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX   PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA   Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA   Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA   Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA   Hu F.Z., Krulwich T.A.;
RT   "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT   support the ability to grow in an external pH range from 7.5 to 11.4.";
RL   Environ. Microbiol. 13:3289-3309(2011).
CC   -!- FUNCTION: Cytochrome c 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. CO I is the catalytic
CC       subunit of the enzyme. Electrons originating in cytochrome c are
CC       transferred via the copper A center of subunit 2 and heme A of subunit
CC       1 to the bimetallic center formed by heme A3 and copper 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   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Elevated expression at high pH.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; M94110; AAA22365.1; -; Genomic_DNA.
DR   EMBL; CP001878; ADC48251.1; -; Genomic_DNA.
DR   RefSeq; WP_012959533.1; NC_013791.2.
DR   AlphaFoldDB; Q04440; -.
DR   SMR; Q04440; -.
DR   STRING; 398511.BpOF4_00910; -.
DR   KEGG; bpf:BpOF4_00910; -.
DR   eggNOG; COG0843; Bacteria.
DR   HOGENOM; CLU_011899_7_1_9; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001544; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01662; Ubiquinol_Oxidase_I; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR   NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF44; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Copper; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Membrane; Metal-binding; Reference proteome; Respiratory chain;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7678007"
FT   CHAIN           2..625
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183434"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         69
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   BINDING         246
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         250
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         295
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         296
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         381
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   BINDING         383
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   CROSSLNK        246..250
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        575
FT                   /note="N -> K (in Ref. 1; AAA22365)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   625 AA;  69871 MW;  6D8058522B7C54A4 CRC64;
     MATQKQEKSV IWDWLTTVDH KKIAIMYLIA GTLFFVKAGV MALFMRIQLM YPEMNFLSGQ
     TFNEFITMHG TIMLFLAATP LLFAFMNYVI PLQIGARDVA FPFVNALGFW IFFFGGLLLS
     LSWFFGGGPD AGWTAYVPLS SRDYGGLGID FYVLGLQVSG IGTLISAINF LVTIVNMRAP
     GMTMMRLPLF VWTSFISSTL ILFAFTPLAA GLALLMLDRL FEAQYFIPSM GGNVVLWQHI
     FWIFGHPEVY ILVLPAFGII SEVIPAFSRK RLFGYTAMVF ATMIIAFLGF MVWAHHMFTV
     GMGPVANSIF AVATMTIAVP TGIKIFNWLF TMWGGKITFN TAMLFASSFV PTFVLGGVTG
     VMLAMAPVDY LYHDTYFVVA HFHYIIVGGI VLSLFAGLFY WYPKMFGHML NETLGKLFFW
     VFYIGFHLTF FVQHLLGLMG MPRRVYTYLG DQGLDAFNFI STIGTFFMSA GVILLVINVI
     YSAFKGERVT VADPWDARTL EWATPTPVPE YNFAQTPQVR SLDPLFYEKI HGDGTMKPAE
     PVTDIHMPNG SILPFIMSIG LFFAGFGLIM LNMDNPIINP WIVAIGGLAL TFGCMFVRSI
     KEDHGYHIPA EQVKADLAEL KKGGN
//