COX2_CERSP
ID COX2_CERSP Reviewed; 303 AA.
AC Q03736;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=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=Oxidase aa(3) subunit 2;
DE Flags: Precursor;
GN Name=ctaC; Synonyms=coxII, ctaB;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1648008; DOI=10.1016/0378-1119(91)90235-4;
RA Cao J., Shapleigh J., Gennis R., Revzin A., Ferguson-Miller S.;
RT "The gene encoding cytochrome c oxidase subunit II from Rhodobacter
RT sphaeroides; comparison of the deduced amino acid sequence with sequences
RT of corresponding peptides from other species.";
RL Gene 101:133-137(1991).
RN [2]
RP SEQUENCE REVISION.
RA Hiser C., Ferguson-Miller S.;
RL Submitted (JUL-2001) 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 -!- 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;
CC Note=Binds a copper A center.;
CC -!- INTERACTION:
CC Q03736; P33517: ctaD; NbExp=3; IntAct=EBI-1033998, EBI-1034008;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; M57680; AAA26100.3; -; Genomic_DNA.
DR PIR; JQ1013; JQ1013.
DR RefSeq; WP_011337012.1; NZ_WSNV01000001.1.
DR PDB; 1M56; X-ray; 2.30 A; B/H=26-289.
DR PDB; 1M57; X-ray; 3.00 A; B/H=26-289.
DR PDB; 2GSM; X-ray; 2.00 A; B/D=26-281.
DR PDB; 3DTU; X-ray; 2.15 A; B/D=26-281.
DR PDB; 3FYE; X-ray; 2.15 A; B/D=26-281.
DR PDB; 3FYI; X-ray; 2.20 A; B/D=26-281.
DR PDB; 5WEH; X-ray; 3.45 A; B/H=26-281.
DR PDB; 6CI0; X-ray; 2.40 A; B/D=29-281.
DR PDBsum; 1M56; -.
DR PDBsum; 1M57; -.
DR PDBsum; 2GSM; -.
DR PDBsum; 3DTU; -.
DR PDBsum; 3FYE; -.
DR PDBsum; 3FYI; -.
DR PDBsum; 5WEH; -.
DR PDBsum; 6CI0; -.
DR AlphaFoldDB; Q03736; -.
DR SMR; Q03736; -.
DR DIP; DIP-38012N; -.
DR IntAct; Q03736; 1.
DR DrugBank; DB03619; Deoxycholic acid.
DR TCDB; 3.D.4.6.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR OrthoDB; 1654242at2; -.
DR EvolutionaryTrace; Q03736; -.
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; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 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.
DR PROSITE; PS50999; COX2_TM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Electron transport; Membrane;
KW Metal-binding; Respiratory chain; Signal; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..303
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000006061"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 252
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 256
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 260
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 49..82
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 98..127
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 204..215
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1M56"
SQ SEQUENCE 303 AA; 32931 MW; 2F363ADA39EFEBF8 CRC64;
MRHSTTLTGC ATGAAGLLAA TAAAAQQQSL EIIGRPQPGG TGFQPSASPV ATQIHWLDGF
ILVIIAAITI FVTLLILYAV WRFHEKRNKV PARFTHNSPL EIAWTIVPIV ILVAIGAFSL
PVLFNQQEIP EADVTVKVTG YQWYWGYEYP DEEISFESYM IGSPATGGDN RMSPEVEQQL
IEAGYSRDEF LLATDTAMVV PVNKTVVVQV TGADVIHSWT VPAFGVKQDA VPGRLAQLWF
RAEREGIFFG QCSELCGISH AYMPITVKVV SEEAYAAWLE QARGGTYELS SVLPATPAGV
SVE
