CCOP_AZOBR
ID CCOP_AZOBR Reviewed; 295 AA.
AC Q9ZHR4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000250|UniProtKB:D5ARP7, ECO:0000312|EMBL:AAC72074.1};
DE Short=Cbb3-Cox subunit CcoP {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=C-type cytochrome CcoP {ECO:0000250|UniProtKB:Q52689};
DE Short=Cyt c(P) {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=Cytochrome c oxidase subunit III {ECO:0000250|UniProtKB:D5ARP7};
GN Name=ccoP {ECO:0000250|UniProtKB:D9IA45};
GN Synonyms=cytP {ECO:0000312|EMBL:AAC72074.1};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC72074.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND COFACTOR.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7
RC {ECO:0000312|EMBL:AAC72074.1};
RX PubMed=9791120; DOI=10.1128/jb.180.21.5689-5696.1998;
RA Marchal K., Sun J., Keijers V., Haaker H., Vanderleyden J.;
RT "A cytochrome cbb3 (cytochrome c) terminal oxidase in Azospirillum
RT brasilense Sp7 supports microaerobic growth.";
RL J. Bacteriol. 180:5689-5696(1998).
CC -!- FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase
CC complex. CcoP subunit is required for transferring electrons from donor
CC cytochrome c via its heme groups to CcoO subunit. From there, electrons
CC are shuttled to the catalytic binuclear center of CcoN subunit where
CC oxygen reduction takes place. The complex also functions as a proton
CC pump (By similarity). {ECO:0000250|UniProtKB:D5ARP7,
CC ECO:0000250|UniProtKB:D9IA45, ECO:0000250|UniProtKB:Q3J015}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:9791120};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:9791120};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:D5ARP7}.
CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
CC composed of CcoN, CcoO, CcoQ and CcoP. {ECO:0000250|UniProtKB:D5ARP7}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF054871; AAC72074.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZHR4; -.
DR SMR; Q9ZHR4; -.
DR PRIDE; Q9ZHR4; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.760.10; -; 2.
DR Gene3D; 6.10.280.130; -; 1.
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 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; SSF46626; 2.
DR TIGRFAMs; TIGR00782; ccoP; 1.
DR PROSITE; PS51007; CYTC; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Repeat; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP"
FT /id="PRO_0000412282"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..295
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT DOMAIN 108..200
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 207..292
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 121
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 124
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 125
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:0000250|UniProtKB:D9IA45"
FT BINDING 175
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:0000250|UniProtKB:D9IA45"
FT BINDING 220
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 223
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 224
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:0000250|UniProtKB:D9IA45"
FT BINDING 269
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:0000250|UniProtKB:D9IA45"
SQ SEQUENCE 295 AA; 31807 MW; 8F38D57A6E25F50F CRC64;
MAQKEKDALS GVETTGHEWD GLRELNNPLP KWWLYIFYVC IAWSLVYYVL YPAWPLGKSY
TKGLLGYSQR EELVQKVADG KKAQEKYLTA IAATSVEDIQ KNKDLLAFAM AGGRSYFNEN
CAACHGAGGQ GAKGFPTLAD DVWLWGGTTA DIYKTIQHGI RADDGDTRGT VGIGMTAFGR
DGILNRDQIG QVAEYILSLN KRSTDAAAAE KGKTVYDENC AACHGENAQG SLAVGMEVGA
PPLVTGNWLY GGDKATLVQT ITNGRAGVMP AWSKRLDDAT IKSLAVYVHN LGGGK
