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Database: UniProt
Entry: A0A1X0N9J4_9PSED
LinkDB: A0A1X0N9J4_9PSED
Original site: A0A1X0N9J4_9PSED 
ID   A0A1X0N9J4_9PSED        Unreviewed;       329 AA.
AC   A0A1X0N9J4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Cbb3-type cytochrome c oxidase subunit {ECO:0000256|PIRNR:PIRNR000006};
GN   ORFNames=BZK31_05905 {ECO:0000313|EMBL:ORC60667.1};
OS   Pseudomonas floridensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1958950 {ECO:0000313|EMBL:ORC60667.1, ECO:0000313|Proteomes:UP000192815};
RN   [1] {ECO:0000313|Proteomes:UP000192815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEV388 {ECO:0000313|Proteomes:UP000192815};
RA   Timilsina S., Vallad G.E., Jones J.B.;
RT   "Pseudomonas floridae sp. nov., a novel pathogenic bacterial species
RT   isolated from tomato.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:ORC60667.1}.
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DR   EMBL; MUIO01000017; ORC60667.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0N9J4; -.
DR   STRING; 1958950.BZK31_05905; -.
DR   OrthoDB; 9811281at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000192815; 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:SF1; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT CCOP; 1.
DR   PANTHER; PTHR33751; 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        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          144..223
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          234..316
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         157
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         160
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         161
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         200
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         247
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         250
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         251
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         293
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;  36068 MW;  B00CF085A3D299E2 CRC64;
     MSTFWSLYVT VLTLGTIVAL VWLLLATRKG ERKEPTEETM GHSFDGIEEY DNPLPKWWFM
     LFMGTIVFAL GYLLLYPGLG NWQGLLPGYA YLDTEKHLKF ADGKQGWTGV HEWEKEVARA
     EARFGPLFAR YAAMPVEEVA KDPQALGMGA RLFASNCSVC HGSDAKGAYG FPNLTDDNWR
     WGGDAQSIKT SILNGRHAVM PAWGEVLGEQ GVRDVSAYVM TMMKDRPLPE GARADPLAGQ
     KIYATNCVAC HGAEGKGLAV LGAPDLTHPG GFIYGSGFAQ LQQTIRYGRQ GQMPTQQATQ
     GDDRVHILAA YVYSLSRQAQ PAHDSTAAK
//
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