ID A0A1I0HNN1_THASX Unreviewed; 514 AA.
AC A0A1I0HNN1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05660429_02878 {ECO:0000313|EMBL:SET85719.1};
OS Thalassotalea agarivorans (Thalassomonas agarivorans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=349064 {ECO:0000313|EMBL:SET85719.1, ECO:0000313|Proteomes:UP000199308};
RN [1] {ECO:0000313|EMBL:SET85719.1, ECO:0000313|Proteomes:UP000199308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19706 {ECO:0000313|EMBL:SET85719.1,
RC ECO:0000313|Proteomes:UP000199308};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOHK01000017; SET85719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0HNN1; -.
DR STRING; 349064.SAMN05660429_02878; -.
DR Proteomes; UP000199308; 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; 2.
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; 2.
DR PRINTS; PR01166; CYCOXIDASEII.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
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; 2.
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:UP000199308};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..514
FT /note="Cytochrome c oxidase subunit 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011652112"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..114
FT /note="Cytochrome oxidase subunit II transmembrane region
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT DOMAIN 115..256
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 280..360
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 414..495
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 514 AA; 55667 MW; 584E60F19DEDD8E2 CRC64;
MIRRNLALLL ISGLFANSAM AQSKYNLTEG VTAISKEVYD LHMLIMYICV VIGVIVFGAM
FWSMYFHRKS KGVKAATFHE STKVEILWTA IPIIILVAMA IPATQTLIKM EDNSAADMTV
QVTGSQWKWH YKYFEEDIEF YSVLSTPRDE FDDLDGVASD KGENYLLEVD KPLVIPTGKK
VRFVITSDDV IHSWWVPAFA VKQDANPGFI NEAWTKVDVP GVYRGQCAEL CGKDHGYMPV
VVEVKSQEDY DAWVAEQKEL QAQAAEAEKA SLNAQMTMDE AMDLGETIYV AHCAACHQAS
GQGLPPAFPA LKGSPIALGD ANAHIDIVYN GKAGTGMQGY GKQLSLKELA AVVTYERNAW
GNNVGDIVQA SDVQAFTTGG GGADSAQAPA QAEEAASVEE KPAEDLTKVY SKDELMTLGE
QVYMQACVAC HQAGGQGLPP TFPSLLKSPI ITGDVTAHID MVLNGSKKNP AMAAFANQLT
KTEIAAVVTY ERNAWGNDTG DVVQPADVDA VSAK
//
