ID U4KHM8_9VIBR Unreviewed; 352 AA.
AC U4KHM8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU004024};
GN ORFNames=VIBNI_B1656 {ECO:0000313|EMBL:CCO61389.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61389.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61389.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203527; CCO61389.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KHM8; -.
DR STRING; 28173.VIBNI_B1656; -.
DR KEGG; vni:VIBNI_B1656; -.
DR PATRIC; fig|1260221.3.peg.5243; -.
DR eggNOG; COG1622; Bacteria.
DR Proteomes; UP000016895; Chromosome 2.
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:UP000016895};
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 18..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..88
FT /note="Cytochrome oxidase subunit II transmembrane region
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT DOMAIN 89..226
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 250..330
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 352 AA; 39003 MW; D9D1C84B1CECB6F7 CRC64;
MTRGVTRISE QVYDLHMLIF YICVVIAVVV FGVMFYAIFK HRKSQGAVAA NFHESTKVEI
IWTVIPILIL VAMAVPATTT LIEMEDTSQS DLTVKITGSQ WKWHYSYFGE DVEFFSLLAT
SSKQIEGDEV KGANYLLEVD NPLVLPINRK VRFLLTSDDV IHSWWVPDFA VKKDTIPGFI
NEAWTRIDEP GVYRGQCAEL CGRNHGFMPI VVHAMEEQEF DEWLVAQKLA AKQAAEEAKA
ALSKELSMDE LMAMGEQVYN ERCAVCHQAN GLGVPGVFPA MKDSPVTLGD MTTHIDVVLN
GVAGTAMQAF GNQLTDEQIA AVVTYERNAW GNDKGDMAQA SDVNALRGGE GQ
//
