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Protein

Cytochrome c551 peroxidase

Gene

ccpA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.

Catalytic activityi

2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O.

Cofactori

hemeNote: Binds 2 heme groups. Heme 1 is low-potential (-330 mV) with 2 His axial ligands and functions in the peroxidase reaction, while heme 2 is high potential (+320 mV) with His and Met axial ligands and functions to feed electrons from electron-shuttle proteins such as cytochrome c and azurin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741Heme 1 (covalent)
Binding sitei77 – 771Heme 1 (covalent)
Metal bindingi78 – 781Iron (heme 1 axial ligand)
Binding sitei220 – 2201Heme 2 (covalent)
Binding sitei223 – 2231Heme 2 (covalent)
Metal bindingi224 – 2241Iron (heme 2 axial ligand)
Metal bindingi284 – 2841Iron (heme 1 axial ligand)
Metal bindingi298 – 2981Iron (heme 2 axial ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17891.
BRENDAi1.11.1.5. 5087.

Protein family/group databases

PeroxiBasei3543. PaerDiHCcP.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c551 peroxidase (EC:1.11.1.5)
Short name:
CCP
Short name:
Cytochrome c peroxidase
Gene namesi
Name:ccpA
Ordered Locus Names:PA4587
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4587.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 346323Cytochrome c551 peroxidase1 PublicationPRO_0000006598Add
BLAST

Post-translational modificationi

Binds 2 heme groups per subunit.

Proteomic databases

PaxDbiP14532.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA4587.

Structurei

Secondary structure

1
346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 339Combined sources
Helixi51 – 6111Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 704Combined sources
Helixi74 – 774Combined sources
Helixi80 – 823Combined sources
Beta strandi88 – 903Combined sources
Helixi94 – 963Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi121 – 1233Combined sources
Helixi124 – 1274Combined sources
Helixi129 – 1335Combined sources
Turni135 – 1384Combined sources
Helixi142 – 1509Combined sources
Helixi153 – 16210Combined sources
Beta strandi167 – 1715Combined sources
Helixi172 – 18312Combined sources
Helixi192 – 1976Combined sources
Helixi201 – 2033Combined sources
Helixi206 – 21712Combined sources
Helixi220 – 2223Combined sources
Turni227 – 2293Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi239 – 2413Combined sources
Turni245 – 2473Combined sources
Turni253 – 2553Combined sources
Helixi256 – 2594Combined sources
Helixi262 – 2643Combined sources
Beta strandi267 – 2693Combined sources
Helixi276 – 2783Combined sources
Turni283 – 2864Combined sources
Helixi291 – 30313Combined sources
Helixi309 – 32012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EB7X-ray2.40A24-346[»]
2VHDX-ray2.30A/B24-346[»]
ProteinModelPortaliP14532.
SMRiP14532. Positions 24-346.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14532.

Family & Domainsi

Domaini

Organized into two domains, each containing a covalent c-heme in a structure reminiscent of class 1 cytochromes c. The domains are related by a quasi-twofold axis. The domain interface contains a calcium-binding site with an unusual set of ligands.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CA0. Bacteria.
COG1858. LUCA.
HOGENOMiHOG000173945.
InParanoidiP14532.
KOiK00428.
OMAiYKFANVG.
OrthoDBiEOG6VF30V.
PhylomeDBiP14532.

Family and domain databases

Gene3Di1.10.760.10. 2 hits.
InterProiIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
IPR026259. MauG/Cytc_peroxidase.
[Graphical view]
PfamiPF03150. CCP_MauG. 1 hit.
PF00034. Cytochrom_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000294. Cytochrome-c_peroxidase. 1 hit.
SUPFAMiSSF46626. SSF46626. 2 hits.
PROSITEiPS51007. CYTC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14532-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSSQLLPLG SLLLSFATPL AQADALHDQA SALFKPIPEQ VTELRGQPIS
60 70 80 90 100
EQQRELGKKL FFDPRLSRSH VLSCNTCHNV GTGGADNVPT SVGHGWQKGP
110 120 130 140 150
RNSPTVFNAV FNAAQFWDGR AKDLGEQAKG PIQNSVEMHS TPQLVEQTLG
160 170 180 190 200
SIPEYVDAFR KAFPKAGKPV SFDNMALAIE AYEATLVTPD SPFDLYLKGD
210 220 230 240 250
DKALDAQQKK GLKAFMDSGC SACHNGINLG GQAYFPFGLV KKPDASVLPS
260 270 280 290 300
GDKGRFAVTK TQSDEYVFRA APLRNVALTA PYFHSGQVWE LKDAVAIMGN
310 320 330 340
AQLGKQLAPD DVENIVAFLH SLSGKQPRVE YPLLPASTET TPRPAE
Length:346
Mass (Da):37,403
Last modified:November 1, 1997 - v2
Checksum:i8B402E5BA149EA44
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861D → G (PubMed:8543038).Curated
Sequence conflicti93 – 931Missing (PubMed:8543038).Curated
Sequence conflicti96 – 961W → G (PubMed:8543038).Curated
Sequence conflicti102 – 12019Missing (PubMed:8543038).CuratedAdd
BLAST
Sequence conflicti137 – 1371E → Q (PubMed:8543038).Curated
Sequence conflicti175 – 1751M → V (PubMed:10984043).Curated
Sequence conflicti228 – 2281Missing (PubMed:8543038).Curated
Sequence conflicti286 – 2872GQ → QG (PubMed:8543038).Curated
Sequence conflicti290 – 2901E → Q (PubMed:8543038).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811G → D.
Natural varianti83 – 831G → D.
Natural varianti152 – 1521I → V.
Natural varianti164 – 1641P → A.
Natural varianti198 – 1981K → I.
Natural varianti334 – 3341L → W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23766 Genomic DNA. Translation: AAC43378.1.
AE004091 Genomic DNA. Translation: AAG07975.1.
PIRiI53515.
RefSeqiNP_253277.1. NC_002516.2.
WP_003094815.1. NZ_ASJY01000737.1.

Genome annotation databases

EnsemblBacteriaiAAG07975; AAG07975; PA4587.
GeneIDi881021.
KEGGipae:PA4587.
PATRICi19843919. VBIPseAer58763_4801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23766 Genomic DNA. Translation: AAC43378.1.
AE004091 Genomic DNA. Translation: AAG07975.1.
PIRiI53515.
RefSeqiNP_253277.1. NC_002516.2.
WP_003094815.1. NZ_ASJY01000737.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EB7X-ray2.40A24-346[»]
2VHDX-ray2.30A/B24-346[»]
ProteinModelPortaliP14532.
SMRiP14532. Positions 24-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4587.

Protein family/group databases

PeroxiBasei3543. PaerDiHCcP.

Proteomic databases

PaxDbiP14532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07975; AAG07975; PA4587.
GeneIDi881021.
KEGGipae:PA4587.
PATRICi19843919. VBIPseAer58763_4801.

Organism-specific databases

PseudoCAPiPA4587.

Phylogenomic databases

eggNOGiENOG4105CA0. Bacteria.
COG1858. LUCA.
HOGENOMiHOG000173945.
InParanoidiP14532.
KOiK00428.
OMAiYKFANVG.
OrthoDBiEOG6VF30V.
PhylomeDBiP14532.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17891.
BRENDAi1.11.1.5. 5087.

Miscellaneous databases

EvolutionaryTraceiP14532.

Family and domain databases

Gene3Di1.10.760.10. 2 hits.
InterProiIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
IPR026259. MauG/Cytc_peroxidase.
[Graphical view]
PfamiPF03150. CCP_MauG. 1 hit.
PF00034. Cytochrom_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000294. Cytochrome-c_peroxidase. 1 hit.
SUPFAMiSSF46626. SSF46626. 2 hits.
PROSITEiPS51007. CYTC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence encoding the di-haem cytochrome c551 peroxidase from Pseudomonas aeruginosa."
    Ridout C.J., James R., Greenwood C.
    FEBS Lett. 365:152-154(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NTCC 6750.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. "A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase."
    Samyn B., van Craenenbroeck K., de Smet L., Vandenberghe I., Pettigrew G., van Beeumen J.
    FEBS Lett. 377:145-149(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-346.
  4. "The primary structure of Pseudomonas cytochrome c peroxidase."
    Roennberg M., Kalkkinen N., Ellfolk N.
    FEBS Lett. 250:175-178(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-346.
  5. "Amino acid sequences of the two heme c-binding sites of Pseudomonas cytochrome-c peroxidase."
    Roennberg M.
    Biochim. Biophys. Acta 912:82-86(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  6. "Structural and functional features of Pseudomonas cytochrome c peroxidase."
    Ellfolk N., Roennberg M., Oesterlund K.
    Biochim. Biophys. Acta 1080:68-77(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa."
    Fueloep V., Ridout C.J., Greenwood C., Hajdu J.
    Structure 3:1225-1233(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiCCPR_PSEAE
AccessioniPrimary (citable) accession number: P14532
Secondary accession number(s): Q51369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.