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Database: UniProt
Entry: A0A212T243_9BURK
LinkDB: A0A212T243_9BURK
Original site: A0A212T243_9BURK 
ID   A0A212T243_9BURK        Unreviewed;       307 AA.
AC   A0A212T243;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cbb3-type cytochrome c oxidase subunit {ECO:0000256|PIRNR:PIRNR000006};
GN   ORFNames=SAMN06295916_0211 {ECO:0000313|EMBL:SNC60123.1};
OS   Polynucleobacter victoriensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=2049319 {ECO:0000313|EMBL:SNC60123.1, ECO:0000313|Proteomes:UP000197215};
RN   [1] {ECO:0000313|EMBL:SNC60123.1, ECO:0000313|Proteomes:UP000197215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-VicM1 {ECO:0000313|EMBL:SNC60123.1,
RC   ECO:0000313|Proteomes:UP000197215};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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}.
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DR   EMBL; FYEX01000001; SNC60123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212T243; -.
DR   OrthoDB; 9811281at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000197215; 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:UP000197215};
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        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          133..211
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          218..299
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         146
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         149
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         150
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         189
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         231
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         234
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         235
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         276
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   307 AA;  33168 MW;  C6A1D2859344E2E7 CRC64;
     MSDFFSSGWG VYIALVTGVG IVWCLYLLFS QRKTNVTYKP DGSVADTGHV WDDDLRELNN
     PLPRWWMWMF LLSCIFGIVY LTLYPGMGEY KGTLGYSTTG AHDASVAQAN DQLKPVYAKY
     MGLDVKQVAA DPAAREMGQR LFLNHCAQCH GSDAGGSKGF PNLSDSDWLY GGEPQDIKTT
     ILGGRAGVMP PFAHLESGQV SDVANYVRNL SGLAADQIKV GRGAEVFKAN CAACHGGDGK
     GNTAMGAPNL TDKVWLYGSS EATIVETVTK GRNGMMPAHE AILTPEKVHL LAAYVWGLSN
     VKDKTAK
//
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