ID   A0A3B7QPG9_STRFR        Unreviewed;       320 AA.
AC   A0A3B7QPG9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
DE   AltName: Full=Cytochrome aa3 subunit 2 {ECO:0000256|ARBA:ARBA00031399};
GN   Name=coxB {ECO:0000313|EMBL:AYA19110.1};
GN   ORFNames=D3X13_25260 {ECO:0000313|EMBL:AYA19110.1};
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906 {ECO:0000313|EMBL:AYA19110.1, ECO:0000313|Proteomes:UP000263139};
RN   [1] {ECO:0000313|EMBL:AYA19110.1, ECO:0000313|Proteomes:UP000263139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NKZ-259 {ECO:0000313|EMBL:AYA19110.1,
RC   ECO:0000313|Proteomes:UP000263139};
RA   Ge B.;
RT   "comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC       complex. Electrons originating in cytochrome c are transferred via heme
CC       a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
CC       {ECO:0000256|ARBA:ARBA00024688}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000256|ARBA:ARBA00007866}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP032266; AYA19110.1; -; Genomic_DNA.
DR   RefSeq; WP_076686696.1; NZ_CP032266.1.
DR   AlphaFoldDB; A0A3B7QPG9; -.
DR   EnsemblBacteria; AYA19110; AYA19110; D3X13_25260.
DR   Proteomes; UP000263139; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   CDD; cd13919; CuRO_HCO_II_like_5; 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; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   NCBIfam; TIGR02866; CoxB; 1.
DR   PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR   Pfam; PF00116; COX2; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:AYA19110.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        63..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          135..292
FT                   /note="Cytochrome oxidase subunit II copper A binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50857"
SQ   SEQUENCE   320 AA;  35937 MW;  357102DB5467CE6A CRC64;
     MSPNGSDRSS RRPMRRKLPQ VLTAGLILAT ATGCTYKDFP RLGMPTPVTE EAPRILSLWQ
     GSWAAALATG VLVWGLILWS VIFHRRSRTK VEVPLQTRYN MPIEALYTVV PLIIVSVLFY
     FTARDESKLL KLEDKPAHTI NVVGFQWSWG FNYVEDVKGS DKEDAKTSKD LDAIPKRFRD
     DFPAGAGGVY DVGTPGERNP QNGNPGPTLW LPKGEKVRFV LTSRDVIHSF WVVPFLMKQD
     VIPGHTNAFE VTPNKEGTFM GKCAELCGVD HSRMLFNVKV VSPERYQKHL EELAKKNQTG
     YIPAGIEQTG HEKNRETNNL
//