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UniProtKB/Swiss-Prot entry P55929

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCPR_NITEU
Primary accession number P55929
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 16, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Cytochrome c551 peroxidase [Precursor]
Synonyms Cytochrome c peroxidase
EC 1.11.1.5
Gene name
Name: ccp
OrderedLocusNames: NE1315
From
Nitrosomonas europaea [TaxID: 915] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 19718 / IFO 14298;
DOI=10.1128/JB.185.9.2759-2773.2003; PubMed=12700255 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea.";
J. Bacteriol. 185:2759-2773(2003).
[2]
 PROTEIN SEQUENCE OF 27-55; 60-86 AND 206-225.
STRAIN=ATCC 19718 / IFO 14298;
PubMed=8163487 [NCBI, ExPASy, EBI, Israel, Japan]
Arciero D.M., Hooper A.B.;
"A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states.";
J. Biol. Chem. 269:11878-11886(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL954747; CAD85226.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A53573; A53573.
RefSeq NP_841364.1; -.
3D structure databases
PDB
1IQC; X-ray; 1.80 A; A/B/C/D=27-334.[ExPASy / RCSB / EBI]
PDBsum 1IQC; -.
ModBase P55929.
Protein family/group databases
PeroxiBase 5004; NeDiHCcP.
Enzyme and pathway databases
BioCyc NEUR228410:NE1315-MON; -.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0004130; Molecular function: cytochrome-c peroxidase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR009056; Cyt_c_monohaem.
IPR004852; CytCP_MauG.
Graphical view of domain structure.
Gene3D G3DSA:1.10.760.10; Cytochrome_c_R; 1.
Pfam PF03150; CCP_MauG; 1.
Pfam graphical view of domain structure.
PROSITE PS51007; CYTC; 2.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1082261; -.
GenomeReviews AL954747_GR; NE1315.
KEGG neu:NE1315; -.
NMPDR fig|228410.1.peg.1263; -.
Phylogenomic databases
HOGENOM P55929; -.
Genome annotation databases
CMR P55929; NE1315.
Other
ProtoNet P55929.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Peroxidase; Repeat; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    26  26      
CHAIN   27   334  308     Cytochrome c551 peroxidase. PRO_0000006599
METAL   69    69        Iron (heme 1 axial ligand) (By similarity). 
METAL   213   213        Iron (heme 2 axial ligand) (By similarity). 
METAL   270   270        Iron (heme 1 axial ligand) (By similarity). 
METAL   284   284        Iron (heme 2 axial ligand) (By similarity). 
BINDING   65    65        Heme 1 (covalent) (By similarity). 
BINDING   68    68        Heme 1 (covalent) (By similarity). 
BINDING   209   209        Heme 2 (covalent) (By similarity). 
BINDING   212   212        Heme 2 (covalent) (By similarity). 
CONFLICT   77    77        D -> C (in Ref. 2; AA sequence). 
HELIX   42    52  11      
HELIX   55    57  3      
STRAND   58    61  4      
HELIX   65    68  4      
TURN   71    74  4      
STRAND   79    81  3      
HELIX   85    87  3      
HELIX   100   102  3      
STRAND   104   107  4      
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      
STRAND   221   226  6      
STRAND   228   230  3      
HELIX   242   245  4      
HELIX   248   250  3      
STRAND   253   255  3      
HELIX   262   264  3      
STRAND   267   269  3      
HELIX   277   289  13      
HELIX   295   306  12      
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 36633 Da [This is the MW of the unprocessed precursor] CRC64: 44E67A23550A862C [This is a checksum on the sequence] 
        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
P55929 in FASTA format

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