ID A0A0S2SQ06_9GAMM Unreviewed; 324 AA.
AC A0A0S2SQ06;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit {ECO:0000256|PIRNR:PIRNR000006};
GN Name=ccoP2 {ECO:0000313|EMBL:ALP43777.1};
GN ORFNames=ATO46_18250 {ECO:0000313|EMBL:KUE79719.1}, WL1483_4358
GN {ECO:0000313|EMBL:ALP43777.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:ALP43777.1, ECO:0000313|Proteomes:UP000058114};
RN [1] {ECO:0000313|Proteomes:UP000058114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WL1483 {ECO:0000313|Proteomes:UP000058114};
RA Liu L.;
RT "Complete Genome Sequence of Aeromonas schubertii strain WL1483.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KUE79719.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE79719.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALP43777.1, ECO:0000313|Proteomes:UP000058114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WL1483 {ECO:0000313|EMBL:ALP43777.1,
RC ECO:0000313|Proteomes:UP000058114};
RX PubMed=26798095;
RA Liu L., Li N., Zhang D., Fu X., Shi C., Lin Q., Hao G.;
RT "Complete Genome Sequence of the Highly Virulent Aeromonas schubertii
RT Strain WL1483, Isolated from Diseased Snakehead Fish (Channa argus) in
RT China.";
RL Genome Announc. 4:e01567-15(2016).
CC -!- FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase
CC complex. {ECO:0000256|PIRNR:PIRNR000006}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRNR:PIRNR000006,
CC ECO:0000256|PIRSR:PIRSR000006-2};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000256|PIRNR:PIRNR000006,
CC ECO:0000256|PIRSR:PIRSR000006-2};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|PIRNR:PIRNR000006}.
CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase.
CC {ECO:0000256|PIRNR:PIRNR000006}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR000006}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family.
CC {ECO:0000256|ARBA:ARBA00006113, ECO:0000256|PIRNR:PIRNR000006}.
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DR EMBL; CP013067; ALP43777.1; -; Genomic_DNA.
DR EMBL; LPUO01000020; KUE79719.1; -; Genomic_DNA.
DR RefSeq; WP_050667482.1; NZ_LPUO01000020.1.
DR STRING; 652.WL1483_4358; -.
DR KEGG; asr:WL1483_4358; -.
DR PATRIC; fig|652.5.peg.2411; -.
DR OrthoDB; 9811281at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000054876; Unassembled WGS sequence.
DR Proteomes; UP000058114; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 6.10.280.130; -; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR032858; CcoP_N.
DR InterPro; IPR038414; CcoP_N_sf.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3.
DR NCBIfam; TIGR00782; ccoP; 1.
DR PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR PANTHER; PTHR33751:SF1; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 2.
DR Pfam; PF14715; FixP_N; 1.
DR PIRSF; PIRSF000006; Cbb3-Cox_fixP; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000006};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000006};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000006};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000006}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|PIRNR:PIRNR000006};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000006}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..234
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 241..321
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 168
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2"
FT BINDING 171
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2"
FT BINDING 172
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1"
FT BINDING 211
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1"
FT BINDING 253
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2"
FT BINDING 256
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2"
FT BINDING 257
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1"
FT BINDING 298
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1"
SQ SEQUENCE 324 AA; 35529 MW; ED9F59DC2E5F680D CRC64;
MSTLLSIFVT VITLGTILGC FALLWWCLKD KMGVEEGQPM GHAFDGIEEI NNPLPKWWTY
LFIIMIVFGL VYLASYPGLG NWKGLLGWQS SNQDIRSLAD SKAATASAQE QGRVVQYDRE
HAKADELYGA KFRELTYSAD GKTYKAIEEI AKDPEALKVG QRLFLQNCAL CHGSDARGGK
GFPNLTDGEW QWGGKPDQIK TTIMNGRHAA MPAWGETLGK DGVKEVTAYV LSLSGRTVDP
VMARKGQARF AMCAACHGAE GKGGEAFGAP DLTNTTWLYG GSRQTVEETI THGRQGVMPA
WKDVLGEDKV HLLASYVYSL SHQQ
//
