CCOP_RHOCA
ID CCOP_RHOCA Reviewed; 297 AA.
AC Q52689;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000303|PubMed:16343536, ECO:0000303|PubMed:18556791};
DE Short=Cbb3-Cox subunit CcoP {ECO:0000303|PubMed:18556791};
DE AltName: Full=C-type cytochrome CcoP {ECO:0000303|PubMed:16343536, ECO:0000303|PubMed:18556791};
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:0000312|EMBL:CAA56436.1};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1] {ECO:0000312|EMBL:CAA56436.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 938 / 37b4 {ECO:0000312|EMBL:CAA56436.1};
RX PubMed=7891558; DOI=10.1111/j.1365-2958.1994.tb01308.x;
RA Thony-Meyer L., Beck C., Preisig O., Hennecke H.;
RT "The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that
RT functions in aerobic respiration of Rhodobacter capsulatus.";
RL Mol. Microbiol. 14:705-716(1994).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, SUBUNIT,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16343536; DOI=10.1016/j.jmb.2005.11.039;
RA Kulajta C., Thumfart J.O., Haid S., Daldal F., Koch H.G.;
RT "Multi-step assembly pathway of the cbb3-type cytochrome c oxidase
RT complex.";
RL J. Mol. Biol. 355:989-1004(2006).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, AND
RP INTERACTION WITH CCOQ.
RX PubMed=18556791; DOI=10.1128/jb.00534-08;
RA Peters A., Kulajta C., Pawlik G., Daldal F., Koch H.G.;
RT "Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP
RT interactions.";
RL J. Bacteriol. 190:5576-5586(2008).
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. {ECO:0000250|UniProtKB:D5ARP7, ECO:0000250|UniProtKB:Q3J015,
CC ECO:0000269|PubMed:16343536, ECO:0000269|PubMed:18556791,
CC ECO:0000303|PubMed:16343536, ECO:0000303|PubMed:18556791}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000305|PubMed:16343536, ECO:0000305|PubMed:18556791}.
CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
CC composed of CcoN, CcoO, CcoQ and CcoP. Interacts with CcoQ.
CC {ECO:0000269|PubMed:16343536, ECO:0000269|PubMed:18556791}.
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}.
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DR EMBL; X80134; CAA56436.1; -; Genomic_DNA.
DR PIR; S65861; S49348.
DR RefSeq; WP_074555342.1; NZ_FNAY01000017.1.
DR AlphaFoldDB; Q52689; -.
DR SMR; Q52689; -.
DR IntAct; Q52689; 2.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 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..297
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP"
FT /id="PRO_0000412291"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..297
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT DOMAIN 108..199
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 206..294
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 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:0000250|UniProtKB:D9IA45"
FT BINDING 219
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 222
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 /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
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:0000250|UniProtKB:D9IA45"
SQ SEQUENCE 297 AA; 31899 MW; D0FF60591E6FA869 CRC64;
MSKKPTTKKE VQTTGHQWDG IEELNTPLPR WWLWTFYATI IWGVAYSIAM PAWPIFSDKA
TPGLLGSSTR ADVEKDIAKF AEMNKAVEEK LVATDLTAIA ADPELVTYTR NAGAAVFRTW
CAQCHGAGAG GNTGFPSLLD GDWLHGGAIE TIYTNVKHGI RDPLDPDTLL VANMPAHLTD
ELLEPAQIDE VVQYVLQISG QPADEVKATA GQQIFAENCA SCHGEDAKGL VEMGAPNLTD
GIWLYGGDVA TLTSTIQYGR GGVMPSWSWA ADGAKPRLSE AQIRAVASYV HSLGGGQ
