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Cbb3-type cytochrome c oxidase subunit CcoP (Cbb3-Cox subunit CcoP) (C-type cytochrome CcoP) (Cyt c(P)) (Cytochrome c oxidase subunit III)

 CCOP_RHOS4              Reviewed;         290 AA.
Q3J015; P72340; Q53114;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
25-APR-2018, entry version 79.
RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000312|EMBL:ABA79869.1};
Short=Cbb3-Cox subunit CcoP {ECO:0000250|UniProtKB:D5ARP7};
AltName: Full=C-type cytochrome CcoP {ECO:0000250|UniProtKB:Q52689};
Short=Cyt c(P) {ECO:0000250|UniProtKB:D5ARP7};
AltName: Full=Cytochrome c oxidase subunit III {ECO:0000250|UniProtKB:D5ARP7};
Name=ccoP {ECO:0000312|EMBL:ABA79869.1};
OrderedLocusNames=RHOS4_23010; ORFNames=RSP_0693;
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
158).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Rhodobacter.
NCBI_TaxID=272943;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB02559.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY OF THE
CYTOCHROME C OXIDASE COMPLEX, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
{ECO:0000312|EMBL:AAB02559.1};
PubMed=9711295; DOI=10.1016/S0005-2728(98)00095-4;
Toledo-Cuevas M., Barquera B., Gennis R.B., Wikstrom M.,
Garcia-Horsman J.A.;
"The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a
proton-pumping heme-copper oxidase.";
Biochim. Biophys. Acta 1365:421-434(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
{ECO:0000312|EMBL:ABA79869.1};
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
Kaplan S.;
"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:AAC44983.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-290, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
{ECO:0000312|EMBL:AAC44983.1};
PubMed=9068641; DOI=10.1128/jb.179.6.1951-1961.1997;
O'Gara J.P., Kaplan S.;
"Evidence for the role of redox carriers in photosynthesis gene
expression and carotenoid biosynthesis in Rhodobacter sphaeroides
2.4.1.";
J. Bacteriol. 179:1951-1961(1997).
[4] {ECO:0000305, ECO:0000312|EMBL:AAC44983.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-290, AND CATALYTIC ACTIVITY
OF THE CYTOCHROME C OXIDASE COMPLEX.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
{ECO:0000312|EMBL:AAC44983.1};
PubMed=10852880; DOI=10.1128/JB.182.12.3475-3481.2000;
Roh J.H., Kaplan S.;
"Genetic and phenotypic analyses of the rdx locus of Rhodobacter
sphaeroides 2.4.1.";
J. Bacteriol. 182:3475-3481(2000).
[5] {ECO:0000305}
CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
{ECO:0000269|PubMed:10052939};
PubMed=10052939; DOI=10.1021/bi9825100;
Oh J.I., Kaplan S.;
"The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1:
structural and functional implications for the regulation of spectral
complex formation.";
Biochemistry 38:2688-2696(1999).
[6] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX,
COFACTOR, AND SUBUNIT.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
{ECO:0000269|PubMed:11864982};
PubMed=11864982; DOI=10.1074/jbc.M200198200;
Oh J.I., Kaplan S.;
"Oxygen adaptation. The role of the CcoQ subunit of the cbb3
cytochrome c oxidase of Rhodobacter sphaeroides 2.4.1.";
J. Biol. Chem. 277:16220-16228(2002).
-!- FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c
oxidase complex. CcoP subunit is required for transferring
electrons from donor cytochrome c via its heme groups to CcoO
subunit. From there, electrons are shuttled to the catalytic
binuclear center of CcoN subunit where oxygen reduction takes
place. The complex also functions as a proton pump.
{ECO:0000250|UniProtKB:D5ARP7, ECO:0000250|UniProtKB:D9IA45,
ECO:0000269|PubMed:11864982, ECO:0000269|PubMed:9711295}.
-!- COFACTOR:
Name=heme c; Xref=ChEBI:CHEBI:61717;
Evidence={ECO:0000250|UniProtKB:D9IA45,
ECO:0000269|PubMed:11864982};
Note=Binds 2 heme C groups per subunit.
{ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:11864982};
-!- PATHWAY: Energy metabolism; oxidative phosphorylation.
{ECO:0000250|UniProtKB:D5ARP7}.
-!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
composed of CcoN, CcoO, CcoQ and CcoP.
{ECO:0000250|UniProtKB:D5ARP7, ECO:0000269|PubMed:11864982}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:9711295}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q8KS19, ECO:0000255,
ECO:0000269|PubMed:9711295}.
-!- DISRUPTION PHENOTYPE: Single ccoP mutant as well as ccoP rdxB
double mutant give rise to colonies with very deep red
pigmentation compared to wild-type when grown on SIS agar plates
in the presence of O(2). The same mutants don't have cytochrome c
oxidase activity and they accumulate high levels of a yellow
carotenoid spheroidenone (SO) during anoxygenic photosynthetic and
diazotrophic growth. Expression of crtA in the ccoP rdxB double
mutant is approximately 60% higher than that observed for wild-
type. Disruption of crtA together with ccoP and rdxB mutants
prevent the accumulation of SO. CcoP and rdxB mutants, either
singly or in combination, are found to synthesize photosynthetic
complexes compared with wild-type when grown in the presence of
30% oxygen. They show a greater than 10-fold increase in levels of
transcription of genes encoding photosynthetic light-harvesting
complexes compared to the levels with wild-type. CcoP single
mutant shows increased levels of photopigments bacteriochlorophyll
and carotenoid under aerobic conditions. It produces more light-
harvesting complexes and photopigments under photosynthetic
conditions than under anaerobic dark conditions. It has no
cytochrome c oxidase activity under anaerobic dark conditions.
Addition of dimethyl sulfoxide (DMSO) to photosynthetic cultures
of the ccoP mutant leads to decreased levels of photosynthetic
light-harvesting complexes. {ECO:0000269|PubMed:10052939,
ECO:0000269|PubMed:9068641}.
-!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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EMBL; U58092; AAB02559.1; -; Genomic_DNA.
EMBL; CP000143; ABA79869.1; -; Genomic_DNA.
EMBL; AF202779; AAC44983.1; -; Genomic_DNA.
RefSeq; WP_011338422.1; NZ_AKVW01000001.1.
RefSeq; YP_353770.1; NC_007493.2.
ProteinModelPortal; Q3J015; -.
SMR; Q3J015; -.
STRING; 272943.RSP_0693; -.
EnsemblBacteria; ABA79869; ABA79869; RSP_0693.
GeneID; 3718343; -.
KEGG; rsp:RSP_0693; -.
PATRIC; fig|272943.9.peg.2645; -.
eggNOG; ENOG4105D6P; Bacteria.
eggNOG; COG2010; LUCA.
HOGENOM; HOG000277941; -.
KO; K00406; -.
OMA; TDNDWLY; -.
OrthoDB; POG091H05TP; -.
PhylomeDB; Q3J015; -.
UniPathway; UPA00705; -.
Proteomes; UP000002703; Chromosome 1.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.760.10; -; 3.
Gene3D; 1.20.58.1490; -; 1.
InterPro; IPR032858; CcoP_N.
InterPro; IPR038414; CcoP_N_sf.
InterPro; IPR009056; Cyt_c-like_dom.
InterPro; IPR036909; Cyt_c-like_dom_sf.
InterPro; IPR008168; Cyt_C_IC.
InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3.
Pfam; PF13442; Cytochrome_CBB3; 2.
Pfam; PF14715; FixP_N; 1.
PIRSF; PIRSF000006; Cbb3-Cox_fixP; 1.
PRINTS; PR00605; CYTCHROMECIC.
SUPFAM; SSF46626; SSF46626; 3.
TIGRFAMs; TIGR00782; ccoP; 1.
PROSITE; PS51007; CYTC; 2.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome;
Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron;
Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat;
Respiratory chain; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 290 Cbb3-type cytochrome c oxidase subunit
CcoP.
/FTId=PRO_0000412293.
TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255,
ECO:0000303|PubMed:9711295}.
TRANSMEM 38 58 Helical. {ECO:0000255}.
TOPO_DOM 59 290 Periplasmic. {ECO:0000255,
ECO:0000303|PubMed:9711295}.
DOMAIN 109 199 Cytochrome c 1. {ECO:0000255|PROSITE-
ProRule:PRU00433}.
DOMAIN 206 287 Cytochrome c 2. {ECO:0000255|PROSITE-
ProRule:PRU00433}.
METAL 126 126 Iron (heme C 1 axial ligand).
{ECO:0000250|UniProtKB:D9IA45}.
METAL 174 174 Iron (heme C 2 axial ligand).
{ECO:0000250|UniProtKB:D9IA45}.
METAL 223 223 Iron (heme C 2 axial ligand).
{ECO:0000250|UniProtKB:D9IA45}.
METAL 264 264 Iron (heme C 1 axial ligand).
{ECO:0000250|UniProtKB:D9IA45}.
BINDING 122 122 Heme C 1 (covalent).
{ECO:0000250|UniProtKB:D9IA45}.
BINDING 125 125 Heme C 1 (covalent).
{ECO:0000250|UniProtKB:D9IA45}.
BINDING 219 219 Heme C 2 (covalent).
{ECO:0000250|UniProtKB:D9IA45}.
BINDING 222 222 Heme C 2 (covalent).
{ECO:0000250|UniProtKB:D9IA45}.
CONFLICT 166 166 D -> E (in Ref. 3; AAC44983).
{ECO:0000305}.
SEQUENCE 290 AA; 31362 MW; 69815B0408599881 CRC64;
MSVKPTKQKP GEPPTTGHSW DGIEEFDNPM PRWWLWTFYV TIVWAIGYSI LYPAWPLING
ATNGLIGHST RADVQRDIEA FAEANATIRQ QLVNTDLTAI AADPNLLQYA TNAGAAVFRT
NCVQCHGSGA AGNVGYPNLL DDDWLWGGDI ESIHTTVTHG IRNTTDDEAR YSEMPRFGAD
GLLDSTQISQ VVEYVLQISG QDHDAALSAE GATIFADNCA ACHGEDGTGS RDVGAPNLTD
AIWLYGGDRA TVTETVTYAR FGVMPNWNAR LTEADIRSVA VYVHGLGGGE


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