ID U2ZKD9_VIBPR Unreviewed; 388 AA.
AC U2ZKD9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU004024};
GN Name=coxB {ECO:0000313|EMBL:GAD68221.1};
GN ORFNames=VPR01S_12_00290 {ECO:0000313|EMBL:GAD68221.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD68221.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD68221.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD68221.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-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:GAD68221.1}.
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DR EMBL; BATJ01000012; GAD68221.1; -; Genomic_DNA.
DR AlphaFoldDB; U2ZKD9; -.
DR STRING; 1219065.VPR01S_12_00290; -.
DR eggNOG; COG1622; Bacteria.
DR Proteomes; UP000016570; 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:UP000016570};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU000456};
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 TRANSMEM 49..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..119
FT /note="Cytochrome oxidase subunit II transmembrane region
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT DOMAIN 120..257
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 281..361
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 388 AA; 42987 MW; B5A491F9AB201C2D CRC64;
MKRSLIDPRT LTSFLFVGFA FPAMSAEHSL NMTRGVTEIS GKVYELHMLI FYICCAIAIV
VFGAMFYSIF KHRKSKGAVA AHFHESTRVE IVWTVIPIII LVLMAIPATK TLVAMEDTSQ
SDLTIKITGS QWKWHYSYFN EEVEFFSLLA TSQKSIEGVE EKGAHYLLEV DNPLVVPIHR
KIRFLLTSDD VIHSWWVPAF AVKKDTVPGF INEAWTRIDE PGVYRGQCAE LCGRAHGFMP
IVVQAMEEAD YEQWLSDKKA ELAQAKQEAA SALTASLSKE ELMQQGESVY TARCAVCHQA
NGMGVPGAFP AIKGSKVATG DLDVHLDTIV HGRPGTAMQA FANQLTDKEI AAVVTYQRNA
WGNDTGDVVQ ASDVNAFKMQ GQESKEGQ
//
