ID I0EPY6_HELC0 Unreviewed; 292 AA.
AC I0EPY6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Cytochrome c oxidase subunit III {ECO:0000256|ARBA:ARBA00029635};
GN OrderedLocusNames=HCW_08750 {ECO:0000313|EMBL:AFI05005.1};
OS Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI05005.1, ECO:0000313|Proteomes:UP000005010};
RN [1] {ECO:0000313|Proteomes:UP000005010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR000006-2};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000256|PIRSR:PIRSR000006-
CC 2};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family.
CC {ECO:0000256|ARBA:ARBA00006113}.
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DR EMBL; CP003479; AFI05005.1; -; Genomic_DNA.
DR RefSeq; WP_014661865.1; NC_017737.1.
DR AlphaFoldDB; I0EPY6; -.
DR STRING; 182217.HCW_08750; -.
DR KEGG; hce:HCW_08750; -.
DR PATRIC; fig|182217.3.peg.1853; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_986691_0_0_7; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000005010; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000006-2};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000006-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000006-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..195
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 205..288
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 129
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 132
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 133
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 174
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 219
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 222
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 223
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 264
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 292 AA; 32543 MW; 2317502623C13E1F CRC64;
MEFLSDNINV FGLVAALVIL VLTIYESSSL IKEMRDSKSQ GELMDNGHLF DGIGEFANNI
PVGWVVSFMC VIVYAFWYFF FGYPLNSFSQ IGQYNEEVKQ YNKKFEEKWK NLGQKELVDM
GQGIFLVHCS QCHGVTAEGL HNSAQNLVHW GKEEGIMDTI KHGSKGMDYL AGEMPAMDMD
EKDAKAIASY VMAEISSVKK TKNPQLIDKG KELFESAGCA GCHGSDGKGL QDNQVFAANL
TTYGAEGFLR NVLTHGKRGN IGHMPSFKYK NFNDLQVKAL AEFIKSLQPL ED
//
