COX2_STRCO
ID COX2_STRCO Reviewed; 319 AA.
AC Q9X814;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 AltName: Full=Mtb92;
DE Flags: Precursor;
GN Name=ctaC; OrderedLocusNames=SCO2156; ORFNames=SC6G10.29c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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}.
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; AL939111; CAB39883.1; -; Genomic_DNA.
DR PIR; T35538; T35538.
DR RefSeq; NP_626412.1; NC_003888.3.
DR RefSeq; WP_011028168.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9X814; -.
DR SMR; Q9X814; -.
DR STRING; 100226.SCO2156; -.
DR TCDB; 3.D.4.4.5; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PRIDE; Q9X814; -.
DR GeneID; 1097590; -.
DR KEGG; sco:SCO2156; -.
DR PATRIC; fig|100226.15.peg.2191; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_3_0_11; -.
DR InParanoid; Q9X814; -.
DR OMA; HAFMPIA; -.
DR PhylomeDB; Q9X814; -.
DR Proteomes; UP000001973; 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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
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_0000006063"
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; 35447 MW; EC266914F4DFA79C CRC64;
MSPNGSDRSP RRPMRRKLLQ ALTAGLVLAT ATGCTYEDFP RLGMPTPTTE EAPRILSLWQ
GSWAAALATG VLVWGLILWS VFFHRRSRTK VEVPPQTRYN LPIEALYTMV PLVIVSVLFY
FTARDESDLM SLNKKPDLTV NVVGFQWSWC FNHIEDVPGS TGDAKTSKEL AGIPDRFIED
FPANAGGVYD CGTPGTENPQ TGNPGPTLWL PKGKTVRFVL TSRDVIHSFW VVPFLMKQDV
IPGHTNAFEV TPNKEGTFLG KCAELCGVDH SRMLFNVKVV SPERYEQHLQ DLAKKGQTGY
VPAGIAQTSH EKNRETNNL
