ID   CYOA_BUCAP              Reviewed;         290 AA.
AC   Q8K993;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 134.
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=BUsg_456;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67999.1; -; Genomic_DNA.
DR   RefSeq; WP_011053966.1; NC_004061.1.
DR   AlphaFoldDB; Q8K993; -.
DR   SMR; Q8K993; -.
DR   STRING; 198804.BUsg_456; -.
DR   KEGG; bas:BUsg_456; -.
DR   eggNOG; COG1622; Bacteria.
DR   HOGENOM; CLU_036876_6_1_6; -.
DR   Proteomes; UP000000416; Chromosome.
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; Cupredoxins - blue copper proteins; 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   NCBIfam; TIGR01433; CyoA; 1.
DR   PANTHER; PTHR22888:SF18; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF06481; COX_ARM; 1.
DR   PIRSF; PIRSF000292; Ubi_od_II; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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; Respiratory chain; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..290
FT                   /note="Cytochrome bo(3) ubiquinol oxidase subunit 2"
FT                   /id="PRO_0000006073"
FT   TOPO_DOM        25..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   LIPID           25
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           25
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   290 AA;  33730 MW;  3D80A02A84732963 CRC64;
     MISINFNNFF KTLLLILIAF TLHGCDSILF NPHGIIAIQE CSILLISFLI MLFVIIPVIF
     MTIYFSVKYR ASNINAKYKP DWCDSKKIEI IVWTIPISII LFLAFVTWNY SHILDPKKSI
     ISKYKPIKID VVSLDWRWLF IYPEYHIATI NEIMFPINRS IIFHITSNSV MNSFFIPSLG
     SQIYAMPGMM TTLNLMSNSP GKYKGISSNY SGKGFSNMKF TAISVLNIKD FENWIKKAQQ
     SPKKLNKMSI FNIISLPNEN HFIEYFSDVK KNLFYEIINQ TYSKNKVFKH
//