Reviewed, UniProtKB/Swiss-Prot P14532 (CCPR_PSEAE)

Names and origin

Protein names

Recommended name:
    Cytochrome c551 peroxidase
      Short name=Cytochrome c peroxidase
      Short name=CCP
    EC=1.11.1.5

Gene names

Name:	ccpA
Ordered Locus Names:	PA4587

Organism

Pseudomonas aeruginosa [Complete proteome] [HAMAP]

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.
Catalytic activity	2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O.
Cofactor	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.
Subcellular location	Periplasm.
Domain	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.
Post-translational modification	Binds 2 heme groups per subunit.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-c peroxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.4

Chain

24 – 346

323

Cytochrome c551 peroxidase Ref.1

PRO_0000006598

Sites

Metal binding

78

1

Iron (heme 1 axial ligand)

Metal binding

224

1

Iron (heme 2 axial ligand)

Metal binding

284

1

Iron (heme 1 axial ligand)

Metal binding

298

1

Iron (heme 2 axial ligand)

Binding site

74

1

Heme 1 (covalent)

Binding site

77

1

Heme 1 (covalent)

Binding site

220

1

Heme 2 (covalent)

Binding site

223

1

Heme 2 (covalent)

Natural variations

Natural variant

81

1

G → D

Natural variant

83

1

G → D

Natural variant

152

1

I → V

Natural variant

164

1

P → A

Natural variant

198

1

K → I

Natural variant

334

1

L → W

Experimental info

Sequence conflict

86

1

D → G Ref.3

Sequence conflict

93

1

Missing Ref.3

Sequence conflict

96

1

W → G Ref.3

Sequence conflict

102 – 120

19

Missing Ref.3

Sequence conflict

137

1

E → Q Ref.3

Sequence conflict

175

1

M → V Ref.2

Sequence conflict

228

1

Missing Ref.3

Sequence conflict

286 – 287

2

GQ → QG Ref.3

Sequence conflict

290

1

E → Q Ref.3

Secondary structure

1

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346

Helix Strand Turn

Details...

Helix

25 – 33

9

Helix

51 – 62

12

Helix

64 – 66

3

Helix

74 – 77

4

Turn

80 – 84

5

Helix

109 – 111

3

Beta strand

116 – 120

5

Helix

123 – 125

3

Helix

131 – 139

9

Helix

142 – 150

9

Helix

153 – 162

10

Beta strand

167 – 171

5

Helix

172 – 185

14

Helix

192 – 197

6

Helix

206 – 217

12

Helix

220 – 222

3

Turn

227 – 229

3

Beta strand

234 – 241

8

Turn

253 – 255

3

Beta strand

256 – 260

5

Beta strand

266 – 269

4

Helix

276 – 278

3

Turn

283 – 286

4

Helix

291 – 298

8

Beta strand

301 – 305

5

Helix

309 – 320

12

Sequences

	Sequence		Length	Mass (Da)
	P14532-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 8B402E5BA149EA44	FASTA	346	37,403
	10 20 30 40 50 60 MQSSQLLPLG SLLLSFATPL AQADALHDQA SALFKPIPEQ VTELRGQPIS EQQRELGKKL 70 80 90 100 110 120 FFDPRLSRSH VLSCNTCHNV GTGGADNVPT SVGHGWQKGP RNSPTVFNAV FNAAQFWDGR 130 140 150 160 170 180 AKDLGEQAKG PIQNSVEMHS TPQLVEQTLG SIPEYVDAFR KAFPKAGKPV SFDNMALAIE 190 200 210 220 230 240 AYEATLVTPD SPFDLYLKGD DKALDAQQKK GLKAFMDSGC SACHNGINLG GQAYFPFGLV 250 260 270 280 290 300 KKPDASVLPS GDKGRFAVTK TQSDEYVFRA APLRNVALTA PYFHSGQVWE LKDAVAIMGN 310 320 330 340 AQLGKQLAPD DVENIVAFLH SLSGKQPRVE YPLLPASTET TPRPAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7781769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NTCC 6750.
[2]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] 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: 8543038] [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: 2546794] [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: 3030432] [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: 1657179] [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: 8591033] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U23766 Genomic DNA. Translation: AAC43378.1.
AE004091 Genomic DNA. Translation: AAG07975.1.

PIR

I53515.

RefSeq

NP_253277.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EB7	X-ray	2.40	A	24-346	[»]
2VHD	X-ray	2.30	A/B	24-346	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

3543. PaerDiHCcP.

Genome annotation databases

GeneID

881021.

GenomeReviews

Gene locus PA4587 in contig AE004091_GR.

KEGG

pae:PA4587.

Organism-specific databases

PseudoCAP

PA4587.

CMR

Search...

Phylogenomic databases

HOGENOM

P14532.

OMA

P14532. QAQGPIQ.

Enzyme and pathway databases

BioCyc

PAER208964:PA4587-MON.

BRENDA

1.11.1.5. 354.

Family and domain databases

InterPro

IPR009056. Cyt_c_monohaem.
IPR004852. Di-haem_cyt_c_peroxidsae.
[Graphical view]

Gene3D

G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit.

Pfam

PF03150. CCP_MauG. 1 hit.
[Graphical view]

PROSITE

PS51007. CYTC. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CCPR_PSEAE

Accession

Primary (citable) accession number: P14532
Secondary accession number(s): Q51369

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)