COX2_STRAW
ID COX2_STRAW Reviewed; 319 AA.
AC Q82AL0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 2;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
DE Flags: Precursor;
GN Name=ctaC; OrderedLocusNames=SAV_6047;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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) (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds a copper A center. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; BA000030; BAC73758.1; -; Genomic_DNA.
DR RefSeq; WP_010987448.1; NZ_JZJK01000089.1.
DR AlphaFoldDB; Q82AL0; -.
DR SMR; Q82AL0; -.
DR STRING; 227882.SAV_6047; -.
DR EnsemblBacteria; BAC73758; BAC73758; SAVERM_6047.
DR KEGG; sma:SAVERM_6047; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_3_0_11; -.
DR OMA; HAFMPIA; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000000428; 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:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
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; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Signal; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..319
FT /note="Probable cytochrome c oxidase subunit 2"
FT /id="PRO_0000006062"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 227
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
FT BINDING 262
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
FT BINDING 266
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
FT BINDING 270
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
SQ SEQUENCE 319 AA; 35494 MW; CE85FD7EDCC1C39D CRC64;
MSPNGSDRSP RRPMRRKLLQ ALTAGLVLAT ATGCTYKDFP RLGMPTPVTE EAPRILSLWQ
GSWAAALATG VLVWGLILWA TIFHRRSRTK VEVPPQTRYN MPIEALYTVV PLIIVSVLFY
FTARDESKLL DLSKKPDVTV NVVGFQWSWG FNYIENVDGS TGNAKTDKNL AAIPDRFKEA
FPANAGGVYD VGTPGTRNPQ TNNPGPTLWL PKGKTVRFVL TSRDVIHSFW VVPFLMKQDV
IPGHTNSFQV TPNREGTFLG KCAELCGVDH SRMLFNVKVV SPERYQQHLK DLAKKGQTGY
VPAGIAQTSH EKNRETNNL
