CCOP_CERS4
ID CCOP_CERS4 Reviewed; 290 AA.
AC Q3J015; P72340; Q53114;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000312|EMBL:ABA79869.1};
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:0000312|EMBL:ABA79869.1}; OrderedLocusNames=RHOS4_23010;
GN ORFNames=RSP_0693;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB02559.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY OF THE
RP CYTOCHROME C OXIDASE COMPLEX, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000312|EMBL:AAB02559.1};
RX PubMed=9711295; DOI=10.1016/s0005-2728(98)00095-4;
RA Toledo-Cuevas M., Barquera B., Gennis R.B., Wikstrom M.,
RA Garcia-Horsman J.A.;
RT "The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-
RT pumping heme-copper oxidase.";
RL Biochim. Biophys. Acta 1365:421-434(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000312|EMBL:ABA79869.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAC44983.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-290, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000312|EMBL:AAC44983.1};
RX PubMed=9068641; DOI=10.1128/jb.179.6.1951-1961.1997;
RA O'Gara J.P., Kaplan S.;
RT "Evidence for the role of redox carriers in photosynthesis gene expression
RT and carotenoid biosynthesis in Rhodobacter sphaeroides 2.4.1.";
RL J. Bacteriol. 179:1951-1961(1997).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAC44983.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-290, AND CATALYTIC ACTIVITY OF THE
RP CYTOCHROME C OXIDASE COMPLEX.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000312|EMBL:AAC44983.1};
RX PubMed=10852880; DOI=10.1128/jb.182.12.3475-3481.2000;
RA Roh J.H., Kaplan S.;
RT "Genetic and phenotypic analyses of the rdx locus of Rhodobacter
RT sphaeroides 2.4.1.";
RL J. Bacteriol. 182:3475-3481(2000).
RN [5] {ECO:0000305}
RP CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000269|PubMed:10052939};
RX PubMed=10052939; DOI=10.1021/bi9825100;
RA Oh J.I., Kaplan S.;
RT "The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and
RT functional implications for the regulation of spectral complex formation.";
RL Biochemistry 38:2688-2696(1999).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000269|PubMed:11864982};
RX PubMed=11864982; DOI=10.1074/jbc.m200198200;
RA Oh J.I., Kaplan S.;
RT "Oxygen adaptation. The role of the CcoQ subunit of the cbb3 cytochrome c
RT oxidase of Rhodobacter sphaeroides 2.4.1.";
RL J. Biol. Chem. 277:16220-16228(2002).
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:D9IA45,
CC ECO:0000269|PubMed:11864982, ECO:0000269|PubMed:9711295}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:11864982};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:11864982};
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 ECO:0000269|PubMed:11864982}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9711295};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8KS19,
CC ECO:0000255, ECO:0000269|PubMed:9711295}.
CC -!- DISRUPTION PHENOTYPE: Single ccoP mutant as well as ccoP rdxB double
CC mutant give rise to colonies with very deep red pigmentation compared
CC to wild-type when grown on SIS agar plates in the presence of O(2). The
CC same mutants don't have cytochrome c oxidase activity and they
CC accumulate high levels of a yellow carotenoid spheroidenone (SO) during
CC anoxygenic photosynthetic and diazotrophic growth. Expression of crtA
CC in the ccoP rdxB double mutant is approximately 60% higher than that
CC observed for wild-type. Disruption of crtA together with ccoP and rdxB
CC mutants prevent the accumulation of SO. CcoP and rdxB mutants, either
CC singly or in combination, are found to synthesize photosynthetic
CC complexes compared with wild-type when grown in the presence of 30%
CC oxygen. They show a greater than 10-fold increase in levels of
CC transcription of genes encoding photosynthetic light-harvesting
CC complexes compared to the levels with wild-type. CcoP single mutant
CC shows increased levels of photopigments bacteriochlorophyll and
CC carotenoid under aerobic conditions. It produces more light-harvesting
CC complexes and photopigments under photosynthetic conditions than under
CC anaerobic dark conditions. It has no cytochrome c oxidase activity
CC under anaerobic dark conditions. Addition of dimethyl sulfoxide (DMSO)
CC to photosynthetic cultures of the ccoP mutant leads to decreased levels
CC of photosynthetic light-harvesting complexes.
CC {ECO:0000269|PubMed:10052939, ECO:0000269|PubMed:9068641}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR EMBL; U58092; AAB02559.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79869.1; -; Genomic_DNA.
DR EMBL; AF202779; AAC44983.1; -; Genomic_DNA.
DR RefSeq; WP_011338422.1; NZ_CP030271.1.
DR RefSeq; YP_353770.1; NC_007493.2.
DR AlphaFoldDB; Q3J015; -.
DR SMR; Q3J015; -.
DR STRING; 272943.RSP_0693; -.
DR EnsemblBacteria; ABA79869; ABA79869; RSP_0693.
DR KEGG; rsp:RSP_0693; -.
DR PATRIC; fig|272943.9.peg.2645; -.
DR eggNOG; COG2010; Bacteria.
DR OMA; DWLYGGE; -.
DR PhylomeDB; Q3J015; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002703; Chromosome 1.
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; Reference proteome; Repeat; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP"
FT /id="PRO_0000412293"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9711295"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..290
FT /note="Periplasmic"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9711295"
FT DOMAIN 109..199
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 206..287
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122
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 /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 126
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"
FT CONFLICT 166
FT /note="D -> E (in Ref. 3; AAC44983)"
FT /evidence="ECO:0000305"
SQ 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
