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Database: UniProt
Entry: K2KJZ0_9GAMM
LinkDB: K2KJZ0_9GAMM
Original site: K2KJZ0_9GAMM 
ID   K2KJZ0_9GAMM            Unreviewed;       317 AA.
AC   K2KJZ0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Cbb3-type cytochrome c oxidase subunit {ECO:0000256|PIRNR:PIRNR000006};
GN   ORFNames=A10D4_02132 {ECO:0000313|EMBL:EKE87002.1};
OS   Idiomarina xiamenensis 10-D-4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE87002.1, ECO:0000313|Proteomes:UP000014115};
RN   [1] {ECO:0000313|EMBL:EKE87002.1, ECO:0000313|Proteomes:UP000014115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-D-4 {ECO:0000313|EMBL:EKE87002.1,
RC   ECO:0000313|Proteomes:UP000014115};
RX   PubMed=23209204; DOI=10.1128/JB.01855-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL   J. Bacteriol. 194:6938-6938(2012).
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:EKE87002.1}.
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DR   EMBL; AMRG01000002; EKE87002.1; -; Genomic_DNA.
DR   RefSeq; WP_008487435.1; NZ_AMRG01000002.1.
DR   AlphaFoldDB; K2KJZ0; -.
DR   STRING; 740709.A10D4_02132; -.
DR   PATRIC; fig|740709.3.peg.429; -.
DR   eggNOG; COG2010; Bacteria.
DR   OrthoDB; 9811281at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000014115; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014115};
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        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          148..227
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          234..314
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         161
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         164
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         165
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         204
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         246
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         249
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                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000006-1"
FT   BINDING         291
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   317 AA;  34839 MW;  580F24B5189A4916 CRC64;
     MSSFWSAWVI VLTLGLLVAI IVLLRWNMKN YTDVAEGEEM GHEFDGIVEI NNPLPKWWTY
     LFWICIVWGF VYLALYPGLG NFQGLLGWKS SNQDVRSLAE SRAAEKRAEE EGLIVEYDRQ
     MRAAEAEYGP IFAAYAARSI EDLAADPEAV AVGQRLFLQN CSQCHGSNAM GGPGFPNLTD
     DDWLHGGSPA KIKETIIGGR QGAMPAFGEQ FTDQQITEVA TYVLSLSGRK VDPELAAAGK
     TRFAVCSACH GVDGKGNQDI GSANLTDNIW LYGGSQAKVE ETLRYGRNGV MPAWKDILGE
     DKVHVVAAYI YSLSNEQ
//
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