ID A0A1Y1SAV4_9GAMM Unreviewed; 388 AA.
AC A0A1Y1SAV4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU004024};
GN ORFNames=ATO7_15173 {ECO:0000313|EMBL:ORE85575.1};
OS Oceanococcus atlanticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Oceanococcus.
OX NCBI_TaxID=1317117 {ECO:0000313|EMBL:ORE85575.1, ECO:0000313|Proteomes:UP000192342};
RN [1] {ECO:0000313|EMBL:ORE85575.1, ECO:0000313|Proteomes:UP000192342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S10r2 {ECO:0000313|EMBL:ORE85575.1,
RC ECO:0000313|Proteomes:UP000192342};
RA Lai Q., Li G., Shao Z.;
RT "Oceanococcus atlanticus 22II-S10r2 Genome Sequencing.";
RL Submitted (APR-2013) 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, ECO:0000256|RuleBase:RU004024}.
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 Evidence={ECO:0000256|RuleBase:RU004024};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU004024};
CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU004024};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU000456};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000456}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000256|ARBA:ARBA00007866, ECO:0000256|RuleBase:RU000456}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORE85575.1}.
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DR EMBL; AQQV01000004; ORE85575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1SAV4; -.
DR STRING; 1317117.ATO7_15173; -.
DR Proteomes; UP000192342; Unassembled WGS sequence.
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:0020037; F:heme binding; IEA:InterPro.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
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 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 Pfam; PF02790; COX2_TM; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PRINTS; PR01166; CYCOXIDASEII.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU004024};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU000456};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000192342};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU000456}; Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000456};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000456}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..388
FT /note="Cytochrome c oxidase subunit 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013276845"
FT TRANSMEM 38..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..111
FT /note="Cytochrome oxidase subunit II transmembrane region
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT DOMAIN 112..254
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 293..371
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 388 AA; 42224 MW; 53242EB1DA490426 CRC64;
MGRLIWGLSG MVLASLAHAA EYNMPVGVTE ISREVHGLHM LIFYICCAIG AAVFGVMIYS
IIAHRKSVHP KPADFHESIK VEIAWTVLPF VILIAMAIPA AGTLIKMEDT SDADITIKIT
GYQWKWHYEY MDEGVSFFSN MDAKSNVARQ LNSGINPADV PNYLLEVDEP LVLPVGKKVR
LLLTSNDVIH AWWVPELATK KDAVPGYINQ LWTKIDEPGI YRGQCAELCG RDHGFMPVVV
RAVQLEEYER WIAERGGKVG GADEQSAAAE PVEVASADAP AVSSEPAELT RDQLMSEGEK
VYKNYCSACH QADGSGMAAA NFPPLTGSQI ANGPVDAHID MVLQGKNAMA AFAYLKDREI
AAVVTYERNA LGNAAGDVVQ PAQIAARR
//
