CYOA_BUCBP
ID CYOA_BUCBP Reviewed; 286 AA.
AC Q89AA3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=bbp_417;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO27127.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE016826; AAO27127.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044010653.1; NC_004545.1.
DR AlphaFoldDB; Q89AA3; -.
DR SMR; Q89AA3; -.
DR STRING; 224915.bbp_417; -.
DR EnsemblBacteria; AAO27127; AAO27127; bbp_417.
DR GeneID; 56470952; -.
DR KEGG; bab:bbp_417; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_6_1_6; -.
DR OMA; TSLDWKW; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000000601; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..286
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 2"
FT /id="PRO_0000006074"
FT TOPO_DOM 25..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..286
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 286 AA; 33106 MW; 8B2397BB39E88CF0 CRC64;
MQFIKYKSYI LKFLLVSCIF CINGCDCTIL CPNGLIAQEQ RFVLFVSFFT MLLIIIPVIF
MTIFFVLRYR ESNFSKTYDP KWSHSNIIEL LIWGIPIIII VFLSIFSWKS VHDLDPKKPI
VSNVQPIKIN VISLDWKWLF IYPDQKIATI NKLIIPINTP IIFNLTSGSV MNSFFIPSLG
SQIYVMPGMK TNLNLIANKL GQFKGFSSNY SGKGFSNMKF DVLVTSDHIF FYEWVKKIQK
SKYKLNSMYQ FNQLAIPSDN NAIKYFSNLK ENLFNVVIAN VLKISL