Cbb3-type cytochrome c oxidase subunit CcoP - Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

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Q3J015 (CCOP_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cbb3-type cytochrome c oxidase subunit CcoP
Short name=Cbb3-Cox subunit CcoP

Alternative name(s):
C-type cytochrome CcoP
Short name=Cyt c(P)
Cytochrome c oxidase subunit III

Gene names

Name:	ccoP
Ordered Locus Names:	RHOS4_23010
ORF Names:	RSP_0693

Organism

Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]

Taxonomic identifier

272943 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter ›

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6
Cofactor	Binds 2 heme C groups per subunit. Ref.6
Pathway	Energy metabolism; oxidative phosphorylation.
Subunit structure	Component of the cbb3-type cytochrome c oxidase at least composed of CcoN, CcoO, CcoQ and CcoP. Ref.6
Subcellular location	Cell inner membrane; Single-pass membrane protein Ref.1.
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 presense of O₂. 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. Ref.3 Ref.5
Sequence similarities	Belongs to the CcoP / FixP family. Contains 2 cytochrome c domains.

Ontologies

Keywords
Biological process	Electron transport Hydrogen ion transport Ion transport Respiratory chain Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway proton transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 290

290

Cbb3-type cytochrome c oxidase subunit CcoP

PRO_0000412293

Regions

Topological domain

1 – 37

Cytoplasmic Potential

Transmembrane

38 – 58

Helical; Potential

Topological domain

59 – 290

232

Periplasmic Potential

Domain

109 – 199

Cytochrome c 1

Domain

206 – 287

Cytochrome c 2

Sites

Metal binding

126

Iron (heme C 1 axial ligand) By similarity

Metal binding

174

Iron (heme C 2 axial ligand) By similarity

Metal binding

223

Iron (heme C 2 axial ligand) By similarity

Metal binding

264

Iron (heme C 1 axial ligand) By similarity

Binding site

122

Heme C 1 (covalent) By similarity

Binding site

125

Heme C 1 (covalent) By similarity

Binding site

219

Heme C 2 (covalent) By similarity

Binding site

222

Heme C 2 (covalent) By similarity

Experimental info

Sequence conflict

166

D → E in AAC44983. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q3J015 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 69815B0408599881
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FASTA

290

31,362

        10         20         30         40         50         60 
MSVKPTKQKP GEPPTTGHSW DGIEEFDNPM PRWWLWTFYV TIVWAIGYSI LYPAWPLING 

        70         80         90        100        110        120 
ATNGLIGHST RADVQRDIEA FAEANATIRQ QLVNTDLTAI AADPNLLQYA TNAGAAVFRT 

       130        140        150        160        170        180 
NCVQCHGSGA AGNVGYPNLL DDDWLWGGDI ESIHTTVTHG IRNTTDDEAR YSEMPRFGAD 

       190        200        210        220        230        240 
GLLDSTQISQ VVEYVLQISG QDHDAALSAE GATIFADNCA ACHGEDGTGS RDVGAPNLTD 

       250        260        270        280        290 
AIWLYGGDRA TVTETVTYAR FGVMPNWNAR LTEADIRSVA VYVHGLGGGE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase." Toledo-Cuevas M., Barquera B., Gennis R.B., Wikstrom M., Garcia-Horsman J.A. Biochim. Biophys. Acta 1365:421-434(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, SUBCELLULAR LOCATION. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[2]	"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1." 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. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[3]	"Evidence for the role of redox carriers in photosynthesis gene expression and carotenoid biosynthesis in Rhodobacter sphaeroides 2.4.1." O'Gara J.P., Kaplan S. J. Bacteriol. 179:1951-1961(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-290, DISRUPTION PHENOTYPE. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[4]	"Genetic and phenotypic analyses of the rdx locus of Rhodobacter sphaeroides 2.4.1." Roh J.H., Kaplan S. J. Bacteriol. 182:3475-3481(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-290, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[5]	"The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and functional implications for the regulation of spectral complex formation." Oh J.I., Kaplan S. Biochemistry 38:2688-2696(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, DISRUPTION PHENOTYPE. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[6]	"Oxygen adaptation. The role of the CcoQ subunit of the cbb3 cytochrome c oxidase of Rhodobacter sphaeroides 2.4.1." Oh J.I., Kaplan S. J. Biol. Chem. 277:16220-16228(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, COFACTOR, SUBUNIT. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U58092 Genomic DNA. Translation: AAB02559.1. CP000143 Genomic DNA. Translation: ABA79869.1. AF202779 Genomic DNA. Translation: AAC44983.1.
RefSeq	YP_353770.1. NC_007493.1.
3D structure databases
ProteinModelPortal	Q3J015.
ModBase	Search...
Protein-protein interaction databases
STRING	272943.RSP_0693.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3718343.
KEGG	rsp:RSP_0693.
PATRIC	23154549. VBIRhoSph57909_2645.
Phylogenomic databases
eggNOG	COG2010.
HOGENOM	HOG000277941.
KO	K00406.
OMA	SNTSHAQ.
ProtClustDB	CLSK841338.
Enzyme and pathway databases
BioCyc	RSPH272943:GJAS-2359-MONOMER.
UniPathway	UPA00705.
Family and domain databases
InterPro	IPR009056. Cyt_c_dom. IPR003088. Cyt_c_I. IPR008168. Cyt_C_IC. IPR004678. Cyt_c_oxidase_cbb3_su3. [Graphical view]
Pfam	PF00034. Cytochrom_C. 1 hit. [Graphical view]
PIRSF	PIRSF000006. Cbb3-Cox_fixP. 1 hit.
PRINTS	PR00605. CYTCHROMECIC.
SUPFAM	SSF46626. Cytochrome_c. 2 hits.
TIGRFAMs	TIGR00782. ccoP. 1 hit.
PROSITE	PS51007. CYTC. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCOP_RHOS4

Accession

Primary (citable) accession number: Q3J015
Secondary accession number(s): P72340, Q53114

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents