Reviewed, UniProtKB/Swiss-Prot P55929 (CCPR_NITEU)

Names and origin

Protein names

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

Gene names

Name:	ccp
Ordered Locus Names:	NE1315

Organism

Nitrosomonas europaea [Complete proteome] [HAMAP]

Taxonomic identifier

915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas

Protein attributes

Sequence length	334 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)

Catalytic activity	2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.
Subcellular location	PeriplasmProbable.
Post-translational modification	Binds 2 heme groups per subunit.
Biophysicochemical properties	Redox potential: E0 are +450 mV (low spin) and -260 mV (high spin).

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Repeat 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-KW
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 iron ion 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 – 26

26

Chain

27 – 334

308

Cytochrome c551 peroxidase

PRO_0000006599

Sites

Metal binding

69

1

Iron (heme 1 axial ligand) By similarity

Metal binding

213

1

Iron (heme 2 axial ligand) By similarity

Metal binding

270

1

Iron (heme 1 axial ligand) By similarity

Metal binding

284

1

Iron (heme 2 axial ligand) By similarity

Binding site

65

1

Heme 1 (covalent) By similarity

Binding site

68

1

Heme 1 (covalent) By similarity

Binding site

209

1

Heme 2 (covalent) By similarity

Binding site

212

1

Heme 2 (covalent) By similarity

Experimental info

Sequence conflict

77

1

D → C AA sequence Ref.2

Secondary structure

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334

Helix Strand Turn

Details...

Helix

42 – 52

11

Helix

55 – 57

3

Beta strand

58 – 61

4

Helix

65 – 68

4

Turn

71 – 74

4

Beta strand

79 – 81

3

Helix

85 – 87

3

Helix

100 – 102

3

Beta strand

104 – 107

4

Beta strand

112 – 114

3

Helix

115 – 124

10

Turn

126 – 129

4

Helix

133 – 141

9

Helix

144 – 154

11

Helix

161 – 173

13

Helix

181 – 186

6

Helix

195 – 207

13

Helix

209 – 211

3

Turn

215 – 218

4

Beta strand

221 – 226

6

Beta strand

228 – 230

3

Helix

242 – 245

4

Helix

248 – 250

3

Beta strand

253 – 255

3

Helix

262 – 264

3

Beta strand

267 – 269

3

Helix

277 – 289

13

Helix

295 – 306

12

Sequences

	Sequence		Length	Mass (Da)
	P55929-1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 44E67A23550A862C	FASTA	334	36,633
	10 20 30 40 50 60 MIKRTLTVSL LSLSLGAMFA SAGVMAANEP IQPIKAVTPE NADMAELGKM LFFDPRLSKS 70 80 90 100 110 120 GFISCNSCHN LSMGGTDNIT TSIGHKWQQG PINAPTVLNS SMNLAQFWDG RAKDLKEQAA 130 140 150 160 170 180 GPIANPKEMA STHEIAEKVV ASMPQYRERF KKVFGSDEVT IDRITTAIAQ FEETLVTPGS 190 200 210 220 230 240 KFDKWLEGDK NALNQDELEG YNLFKGSGCV QCHNGPAVGG SSYQKMGVFK PYETKNPAAG 250 260 270 280 290 300 RMDVTGNEAD RNVFKVPTLR NIELTYPYFH DGGAATLEQA VETMGRIQLN REFNKDEVSK 310 320 330 IVAFLKTLTG DQPDFKLPIL PPSNNDTPRS QPYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea." Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J. J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19718 / IFO 14298.
[2]	"A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states." Arciero D.M., Hooper A.B. J. Biol. Chem. 269:11878-11886(1994) [PubMed: 8163487] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-55; 60-86 AND 206-225. Strain: ATCC 19718 / IFO 14298.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL954747 Genomic DNA. Translation: CAD85226.1.

PIR

A53573.

RefSeq

NP_841364.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IQC	X-ray	1.80	A/B/C/D	27-334	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

5004. NeDiHCcP.

Genome annotation databases

GeneID

1082261.

GenomeReviews

Gene locus NE1315 in contig AL954747_GR.

KEGG

neu:NE1315.

NMPDR

fig|228410.1.peg.1263.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P55929.

Enzyme and pathway databases

BioCyc

NEUR228410:NE1315-MON.

Family and domain databases

InterPro

IPR009056. Cyt_c_monohaem.
IPR004852. CytCP_MauG.
[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_NITEU

Accession

Primary (citable) accession number: P55929

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 16, 2003
Last modified:	November 25, 2008
This is version 65 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)