ID A0A0A1YJD6_9PSED Unreviewed; 329 AA.
AC A0A0A1YJD6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit {ECO:0000256|PIRNR:PIRNR000006};
GN ORFNames=TMS3_0117210 {ECO:0000313|EMBL:KFX69201.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX69201.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX69201.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX69201.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(2014).
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}.
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:KFX69201.1}.
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DR EMBL; AWSQ01000004; KFX69201.1; -; Genomic_DNA.
DR RefSeq; WP_025166435.1; NZ_AWSQ01000004.1.
DR AlphaFoldDB; A0A0A1YJD6; -.
DR STRING; 1395571.TMS3_0117210; -.
DR eggNOG; COG2010; Bacteria.
DR OrthoDB; 9811281at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000030063; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030063};
KW 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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..232
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 242..323
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 166
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 169
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 170
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 209
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 255
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 258
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 259
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 300
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 329 AA; 36158 MW; EC4A1FD47F4DD815 CRC64;
MTTFWNWYVT ILSLGTIFAL TWLIFGTRKG QRQESTEETV GHVFDGIEEY DNPLPKWWFM
LFIGTIIFAL GYLVLYPGLG NWKGLLPGYD YLDNEAKTPF AANVQIADGE QRNAGWTGVH
QWEKEMAKAD AQYGPIFAKY AAMPIEQVAQ DEQALKMGGR LFASNCSVCH GSDAKGAYGF
PNLTDNDWLY GGAAETIKTT IMGGRQAAMP AWKDSLGEEG IKNVAGYVRS LSGLKTPESV
EVDLAAGQQT FAANCAVCHG PDAKGQQAMG APNLTDKTWL YGSSFAQVQQ TLRYGRNGRM
PSQEAFLGND KVHLLAAYVY SLSQKPAQQ
//
