CCOP_RUBGE
ID CCOP_RUBGE Reviewed; 304 AA.
AC Q5GCA5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000250|UniProtKB:D5ARP7};
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:0000312|EMBL:AAW66135.1};
GN Name=ccoP {ECO:0000312|EMBL:AAW66135.1};
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAW66135.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND COFACTOR.
RC STRAIN=1 {ECO:0000312|EMBL:AAW66135.1};
RX PubMed=17178720; DOI=10.1074/jbc.m605985200;
RA Ouchane S., Picaud M., Therizols P., Reiss-Husson F., Astier C.;
RT "Global regulation of photosynthesis and respiration by FnrL: the first two
RT targets in the tetrapyrrole pathway.";
RL J. Biol. Chem. 282:7690-7699(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAW66135.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY OF THE CYTOCHROME C
RP OXIDASE COMPLEX, AND COFACTOR.
RC STRAIN=1 {ECO:0000312|EMBL:AAW66135.1};
RX PubMed=20363758; DOI=10.1074/jbc.m110.116020;
RA Hassani B.K., Astier C., Nitschke W., Ouchane S.;
RT "CtpA, a copper-translocating P-type ATPase involved in the biogenesis of
RT multiple copper-requiring enzymes.";
RL J. Biol. Chem. 285:19330-19337(2010).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAW66135.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY OF THE CYTOCHROME
RP C OXIDASE COMPLEX.
RC STRAIN=1 {ECO:0000312|EMBL:AAW66135.1};
RX PubMed=20335164; DOI=10.1074/jbc.m109.086066;
RA Hassani B.K., Steunou A.S., Liotenberg S., Reiss-Husson F., Astier C.,
RA Ouchane S.;
RT "Adaptation to oxygen: role of terminal oxidases in photosynthesis
RT initiation in the purple photosynthetic bacterium, Rubrivivax
RT gelatinosus.";
RL J. Biol. Chem. 285:19891-19899(2010).
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:17178720,
CC ECO:0000269|PubMed:20363758};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:17178720, ECO:0000269|PubMed:20363758};
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}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR EMBL; AY648960; AAW66135.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5GCA5; -.
DR SMR; Q5GCA5; -.
DR BRENDA; 7.1.1.9; 5401.
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 1: Evidence at protein level;
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..304
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP"
FT /id="PRO_0000412294"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 129..209
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 216..296
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 142
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 145
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 146
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 185
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 228
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 231
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 232
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 273
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 304 AA; 32673 MW; 50F115B26F5743A6 CRC64;
MSDFFNSGWS LYVAGITVVS LIFCLVVLIV ASRRKVMADD NTTGHVWDED LQELNNPLPR
WWAGLFLVTI AFAVIYLALY PGLGSNKGTL DWTSTGQHSA EMEKARAQMA PLYAKFVSQP
AEALAKDPQA MAIGERLFAN NCAQCHGADA RGSKGFPNLT DNDWLHGGTH DKIKETITGG
RVGNMPPMAA AVGTPEDVKN VAQYVLSLSG APHNEVAAQL GKAKFAVCAA CHGPDGKGMQ
AVGSANLTDK IWLHGLRRTG HHRLINNGKT NIMPAQASRL SPEQIHVLGA YVWSLSQTST
VAAR
