ID   CYOA_PSEPU              Reviewed;         314 AA.
AC   Q9WWR1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
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;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IH-2000;
RX   PubMed=9868765; DOI=10.1111/j.1574-6968.1998.tb13321.x;
RA   Hirayama H., Takami H., Inoue A., Horikoshi K.;
RT   "Isolation and characterization of toluene-sensitive mutants from
RT   Pseudomonas putida IH-2000.";
RL   FEMS Microbiol. Lett. 169:219-225(1998).
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 inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AB016787; BAA76356.1; -; Genomic_DNA.
DR   RefSeq; WP_046616069.1; NZ_JADLKC010000073.1.
DR   AlphaFoldDB; Q9WWR1; -.
DR   SMR; Q9WWR1; -.
DR   STRING; 1240350.AMZE01000009_gene4204; -.
DR   PRIDE; Q9WWR1; -.
DR   eggNOG; COG1622; Bacteria.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Lipoprotein;
KW   Membrane; Oxidoreductase; Palmitate; Respiratory chain; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           24..314
FT                   /note="Cytochrome bo(3) ubiquinol oxidase subunit 2"
FT                   /id="PRO_0000006075"
FT   TOPO_DOM        24..42
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..314
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          278..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   314 AA;  34702 MW;  96EE04FC3AA77F07 CRC64;
     MSKKRYPRLF GILPFLGMLL LSGCNWTLLD PKGQVGIEQK NLILIATGLM LLVVIPVIIM
     TVVFAWKYRA SNKAATYTPD WSHSTKIEAA VWIIPILIII ALGYFTYHST HKLDPYRPLD
     SDVKPVQIDV VALDWKWLFI YPEQGIATVN KIVFPANTPV NFRVTSDAVM NSFFIPGLGG
     QIYAMAGMTT KLHLIANENG EFDGISANYS GAGFTGMKFK ATATSQEDFD KWVAEVKQSP
     KKLDKAEYEA LAKPSENNPV ALYSEASPDQ FQLIVDKYEG MNRGRPSHEE AGSKDLATTK
     GVESSMQPAA GAEE