Cbb3-type cytochrome c oxidase subunit FixP - Bradyrhizobium japonicum (strain USDA 110)

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Q03075 (FIXP_BRAJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 99. 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 FixP
Short name=Cbb3-Cox subunit FixP

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

Gene names

Name:	fixP
Ordered Locus Names:	blr2766

Organism

Bradyrhizobium japonicum (strain USDA 110) [Reference proteome] [HAMAP]

Taxonomic identifier

224911 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium ›

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. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subunit where oxygen reduction takes place. The complex also functions as a proton pump. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Cofactor	Binds 2 heme C groups per subunit. Ref.4 Ref.6 Ref.7
Pathway	Energy metabolism; oxidative phosphorylation.
Subunit structure	Component of the cbb3-type cytochrome c oxidase at least composed of FixN, FixO, FixQ and FixP. Ref.4 Ref.5 Ref.6
Subcellular location	Cell inner membrane; Single-pass membrane protein Ref.1 Ref.7.
Disruption phenotype	Microaerobically grown cells show 38% decrease in cytochrome c oxadase complex activity. Between 0-5% nitrogen fixing activity of the nitrogenase in root nodules when in symbiosis with soybean. Ref.5
Sequence similarities	Belongs to the CcoP / FixP family. Contains 2 cytochrome c domains.
Mass spectrometry	Molecular mass is 32130 Da from positions 1 - 290. Determined by ESI. Ref.6

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 Direct protein sequencing 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 FixP

PRO_0000412296

Regions

Topological domain

1 – 32

Cytoplasmic Potential

Transmembrane

33 – 53

Helical; Potential

Topological domain

54 – 290

237

Periplasmic Potential

Domain

109 – 198

Cytochrome c 1

Domain

206 – 287

Cytochrome c 2

Sites

Metal binding

126

Iron (heme C 1 axial ligand) By similarity

Metal binding

173

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

Mutagenesis

122

C → S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-125 or with S-125, S-219 and S-222. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex. Ref.6

Mutagenesis

125

C → S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-122 or with S-122, S-219 and S-222. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex. Ref.6

Mutagenesis

219

C → S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-222 or with S-222, S-122 and S-125. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex. Ref.6

Mutagenesis

222

C → S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-219 or with S-219, S-122 and S-125. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

Q03075 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 983F1B606D507BAC
Show »

FASTA

290

31,024

        10         20         30         40         50         60 
MTDHSEFDSV SGKTTTGHEW DGIKELNTPL PRWWVICFYL TIVWAIGYWI VYPAWPLISS 

        70         80         90        100        110        120 
NTTGLFGYSS RADVAVELAN LEKIRGDKMA ALGAASLADV EKDPALLALA RAKGKTVFGD 

       130        140        150        160        170        180 
NCAPCHGSGG AGAKGFPNLN DDDWLWGGTL DQIMQTIQFG ARSGHAKTHE GQMLAFGKDG 

       190        200        210        220        230        240 
VLKGDEIVTV ANYVRSLSGL PTRKGYDAAK GEKIFVENCV ACHGDGGKGN QEMGAPNLTD 

       250        260        270        280        290 
KIWLYGSDEA ALIETISQGR AGVMPAWEGR LDPSTIKAMA VYVHSLGGGK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis." Preisig O., Anthamatten D., Hennecke H. Proc. Natl. Acad. Sci. U.S.A. 90:3309-3313(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
[2]	"Bradyrhizobium japonicum FixK2, a crucial distributor in the FixLJ-dependent regulatory cascade for control of genes inducible by low oxygen levels." Nellen-Anthamatten D., Rossi P., Preisig O., Kullik I., Babst M., Fischer H.M., Hennecke H. J. Bacteriol. 180:5251-5255(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: USDA 110spc4.
[3]	"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.
[4]	"A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum." Preisig O., Zufferey R., Thony-Meyer L., Appleby C.A., Hennecke H. J. Bacteriol. 178:1532-1538(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7, FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, COFACTOR, SUBUNIT.
[5]	"Assembly and function of the cytochrome cbb3 oxidase subunits in Bradyrhizobium japonicum." Zufferey R., Preisig O., Hennecke H., Thony-Meyer L. J. Biol. Chem. 271:9114-9119(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, SUBUNIT, DISRUPTION PHENOTYPE.
[6]	"Heme C incorporation into the c-type cytochromes FixO and FixP is essential for assembly of the Bradyrhizobium japonicum cbb3-type oxidase." Zufferey R., Hennecke H., Thony-Meyer L. FEBS Lett. 412:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, COFACTOR, SUBUNIT, MASS SPECTROMETRY, MUTAGENESIS OF CYS-122; CYS-125; CYS-219 AND CYS-222.
[7]	"Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli." Arslan E., Schulz H., Zufferey R., Kunzler P., Thony-Meyer L. Biochem. Biophys. Res. Commun. 251:744-747(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, SUBCELLULAR LOCATION.
[8]	"The symbiotically essential cbb(3)-type oxidase of Bradyrhizobium japonicum is a proton pump." Arslan E., Kannt A., Thony-Meyer L., Hennecke H. FEBS Lett. 470:7-10(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07487 Genomic DNA. Translation: AAA26206.1. AJ005001 Genomic DNA. Translation: CAA06282.1. BA000040 Genomic DNA. Translation: BAC48031.1.
PIR	D47468.
RefSeq	NP_769406.1. NC_004463.1.
3D structure databases
ProteinModelPortal	Q03075.
ModBase	Search...
Protein-protein interaction databases
STRING	224911.blr2766.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC48031; BAC48031; BAC48031.
GeneID	1054100.
KEGG	bja:blr2766.
PATRIC	21188980. VBIBraJap65052_2748.
Phylogenomic databases
HOGENOM	HOG000277941.
KO	K00406.
OMA	KEMDKAD.
ProtClustDB	CLSK910878.
Enzyme and pathway databases
BioCyc	BJAP224911:GJEJ-2790-MONOMER.
UniPathway	UPA00705.
Family and domain databases
InterPro	IPR009056. Cyt_c_dom. IPR008168. Cyt_C_IC. IPR004678. Cyt_c_oxidase_cbb3_su3. [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

FIXP_BRAJA

Accession

Primary (citable) accession number: Q03075
Secondary accession number(s): D4AER5

Q89RK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 99 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