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UniProtKB/Swiss-Prot entry P55979


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

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Entry information
Entry name BCP_HELPY
Primary accession number P55979
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 46)
Name and origin of the protein
Protein name Putative peroxiredoxin bcp
Synonyms EC 1.11.1.15
Thioredoxin reductase
Bacterioferritin comigratory protein homolog
Gene name
Name: bcp
OrderedLocusNames: HP_0136
From
Helicobacter pylori (Campylobacter pylori) [TaxID: 210] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Helicobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700392 / 26695;
DOI=10.1038/41483; PubMed=9252185 [NCBI, ExPASy, EBI, Israel, Japan]
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
"The complete genome sequence of the gastric pathogen Helicobacter pylori.";
Nature 388:539-547(1997).
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
AE000511; AAD07205.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64536; H64536.
RefSeq NP_206936.1; -.
3D structure databases
HSSP Q63716; 1QQ2. [HSSP ENTRY / PDB]
ModBase P55979.
Protein-protein interaction databases
DIP DIP:3201N; -.
Ontologies
GO
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P55979.
ProtoNet P55979.
Genome annotation databases
GeneID 900152; -.
GenomeReviews AE000511_GR; HP_0136.
KEGG hpy:HP0136; -.
NMPDR fig|85962.1.peg.134; -.
TIGR HP_0136; -.
Phylogenomic databases
HOGENOM P55979; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   152  152     Putative peroxiredoxin bcp. PRO_0000135138
DOMAIN   4   152  149     Thioredoxin. 
ACT_SITE   46    46        By similarity. 
Sequence information
Length: 152 AA [This is the length of the unprocessed precursor] Molecular weight: 17116 Da [This is the MW of the unprocessed precursor] CRC64: 40D71F05CC19D671 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEKLEVGQLA PDFRLKNSDG VEISLKDLLH KKVVLYFYPK DNTPGCTLEA KDFSALFSEF 

        70         80         90        100        110        120 
EKKNAVVVGI SPDNAQSHQK FISQCSLNVI LLCDEDKKAA NLYKAYGKRM LYGKEHLGII 

       130        140        150 
RSTFIINTQG VLEKCFYNVK AKGHAQKVLE SL 

P55979 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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