ID   CYOA_BUCAI              Reviewed;         296 AA.
AC   P57544;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 2;
DE   AltName: Full=Cytochrome o ubiquinol oxidase subunit 2;
DE            Short=Cytochrome o subunit 2;
DE   AltName: Full=Oxidase bo(3) subunit 2;
DE   AltName: Full=Ubiquinol oxidase polypeptide II;
DE   AltName: Full=Ubiquinol oxidase subunit 2;
DE   Flags: Precursor;
GN   Name=cyoA; OrderedLocusNames=BU472;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component
CC       of the aerobic respiratory chain of E.coli that predominates when cells
CC       are grown at high aeration. Has proton pump activity across the
CC       membrane in addition to electron transfer, pumping 2 protons/electron
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains and
CC       two D chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB13169.1; -; Genomic_DNA.
DR   RefSeq; NP_240283.1; NC_002528.1.
DR   RefSeq; WP_010896133.1; NC_002528.1.
DR   AlphaFoldDB; P57544; -.
DR   SMR; P57544; -.
DR   STRING; 107806.10039135; -.
DR   EnsemblBacteria; BAB13169; BAB13169; BAB13169.
DR   KEGG; buc:BU472; -.
DR   PATRIC; fig|107806.10.peg.481; -.
DR   eggNOG; COG1622; Bacteria.
DR   HOGENOM; CLU_036876_6_1_6; -.
DR   OMA; TAMNSFF; -.
DR   Proteomes; UP000001806; 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:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR   CDD; cd04212; CuRO_UO_II; 1.
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; IPR010514; COX_ARM.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034227; CuRO_UO_II.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   InterPro; IPR006333; Cyt_o_ubiquinol_oxidase_su2.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF06481; COX_ARM; 1.
DR   PIRSF; PIRSF000292; Ubi_od_II; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   TIGRFAMs; TIGR01433; CyoA; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Lipoprotein; Membrane; Oxidoreductase;
KW   Palmitate; Reference proteome; Respiratory chain; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..296
FT                   /note="Cytochrome bo(3) ubiquinol oxidase subunit 2"
FT                   /id="PRO_0000006072"
FT   TOPO_DOM        16..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   296 AA;  34180 MW;  1AB2B4F0408FFBAC CRC64;
     MKTLSLILIF FFLNGCNNPL LNSHGTIATE EYSLILISFI MMLFIIIPVI FMTIYFSLKY
     RSTNVNQIYK PNWCDSKKIE IVVWTIPIII VSFLAFLSWS YTHKLDPKKS IVSLNNPIKI
     DAVALDWKWL FIYPDYNIAT INEIMFPVNR PIVFRITSNS VMNAFFIPSL GSQIYAMPGM
     TTKLNLIAND VGKYKGISSN YSGHGFSNMK FTAISVLKNS TFLDWVKKVQ ASSIKLNTMK
     TFDIISIPNE NYSIEYFSSV KKNLFNKIKN QYSIKHFILD ENLSHEIVKK NFNMEK