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P15879 (ARC3_CBDP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mono-ADP-ribosyltransferase C3

EC=2.4.2.-
Alternative name(s):
Exoenzyme C3
Gene names
Name:C3
OrganismClostridium botulinum D phage (Clostridium botulinum D bacteriophage)
Taxonomic identifier29342 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridae
Virus hostClostridium botulinum [TaxID: 1491]

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue.

Subunit structure

Monomer. Interacts with human RALA. Ref.5

Subcellular location

Secreted.

Sequence similarities

To exoenzymes 3 of C.limosum and C.botulinum C phage, and to S.aureus ediN.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentSecreted
   DomainSignal
   LigandNAD
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: InterPro

protein ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontransferase activity, transferring pentosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Ref.1
Chain41 – 251211Mono-ADP-ribosyltransferase C3
PRO_0000020755

Regions

Nucleotide binding128 – 1314NAD
Nucleotide binding167 – 1693NAD
Nucleotide binding183 – 1864NAD
Nucleotide binding212 – 2143NAD

Sites

Binding site801NAD
Binding site871NAD
Binding site911NAD
Site2141Transition state stabilizer

Experimental info

Mutagenesis991G → D: Reduces interaction with human RALA. Ref.7
Mutagenesis1091E → A: Loss of interaction with human RALA. Ref.7
Mutagenesis1741S → A: No effect on enzyme activity. Ref.5
Mutagenesis1821Q → A: No effect on NAD binding. No effect on enzyme activity. Ref.5
Mutagenesis1861R → E: Loss of NAD binding and loss of activity. Ref.5
Mutagenesis2121Q → A: Reduces affinity for NAD 2-fold. No effect on enzyme activity. Ref.5

Secondary structure

..................................... 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15879 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 03D6C8A16FACA46C

FASTA25127,841
        10         20         30         40         50         60 
MKGLRKSILC LVLSAGVIAP VTSGMIQSPQ KCYAYSINQK AYSNTYQEFT NIDQAKAWGN 

        70         80         90        100        110        120 
AQYKKYGLSK SEKEAIVSYT KSASEINGKL RQNKGVINGF PSNLIKQVEL LDKSFNKMKT 

       130        140        150        160        170        180 
PENIMLFRGD DPAYLGTEFQ NTLLNSNGTI NKTAFEKAKA KFLNKDRLEY GYISTSLMNV 

       190        200        210        220        230        240 
SQFAGRPIIT KFKVAKGSKA GYIDPISAFA GQLEMLLPRH STYHIDDMRL SSDGKQIIIT 

       250 
ATMMGTAINP K 

« Hide

References

[1]"DNA sequence of exoenzyme C3, an ADP-ribosyltransferase encoded by Clostridium botulinum C and D phages."
Popoff M.R., Boquet P., Gill D.M., Eklund M.W.
Nucleic Acids Res. 18:1291-1291(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-251, PROTEIN SEQUENCE OF 41-66.
Strain: 1873.
[2]"Characterization of the C3 gene of Clostridium botulinum types C and D and its expression in Escherichia coli."
Popoff M.R., Hauser D., Boquet P., Eklund M.W., Gill D.M.
Infect. Immun. 59:3673-3679(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
Strain: 1873.
[3]"Purification and characterization of ADP-ribosyltransferases (exoenzyme C3) of Clostridium botulinum type C and D strains."
Moriishi K., Syuto B., Yokosawa N., Oguma K., Saito M.
J. Bacteriol. 173:6025-6029(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-60.
Strain: 1873.
[4]"Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis."
Han S., Arvai A.S., Clancy S.B., Tainer J.A.
J. Mol. Biol. 305:95-107(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 41-251.
[5]"NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme."
Menetrey J., Flatau G., Stura E.A., Charbonnier J.-B., Gas F., Teulon J.-M., Le Du M.-H., Boquet P., Menez A.
J. Biol. Chem. 277:30950-30957(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 41-251 IN COMPLEX WITH NAD, SUBUNIT, MUTAGENESIS OF SER-174; GLN-182; ARG-186 AND GLN-212.
[6]"C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal form and a reassessment of NAD-induced flexure."
Evans H.R., Holloway D.E., Sutton J.M., Ayriss J., Shone C.C., Acharya K.R.
Acta Crystallogr. D 60:1502-1505(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 41-251.
[7]"Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme."
Pautsch A., Vogelsgesang M., Traenkle J., Herrmann C., Aktories K.
EMBO J. 24:3670-3680(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 41-251 IN COMPLEX WITH NAD AND HUMAN RALA, MUTAGENESIS OF GLY-99 AND GLU-109.
[8]"Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase."
Holbourn K.P., Sutton J.M., Evans H.R., Shone C.C., Acharya K.R.
Proc. Natl. Acad. Sci. U.S.A. 102:5357-5362(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 41-251 IN COMPLEX WITH HUMAN RALA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59040 Genomic DNA. Translation: CAA41768.1.
X51464 Genomic DNA. Translation: CAA35828.1.
X59039 Genomic DNA. Translation: CAA41767.1.
RefSeqYP_398578.1. NC_007581.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G24X-ray1.70A/B/C/D41-251[»]
1GZEX-ray2.70A/B/C/D41-251[»]
1GZFX-ray1.95A/B/C/D41-251[»]
1UZIX-ray1.89A/B41-251[»]
2A78X-ray1.81B41-251[»]
2A9KX-ray1.73B41-251[»]
2BOVX-ray2.66B1-251[»]
2C89X-ray1.85A/B/C/D41-251[»]
2C8AX-ray1.70A/B/C/D41-251[»]
2C8BX-ray1.70X41-251[»]
2C8CX-ray2.70A/B/C/D41-251[»]
2C8DX-ray2.20A/B/C/D41-251[»]
2C8EX-ray1.60E/F/G41-251[»]
2C8FX-ray2.50E/F/G41-251[»]
2C8GX-ray2.00A/B/C/D41-251[»]
2C8HX-ray1.65A/B/C/D41-251[»]
ProteinModelPortalP15879.
SMRP15879. Positions 41-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15879. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3773098.

Family and domain databases

InterProIPR003540. ADP-ribosyltransferase.
IPR016678. Mono-ADP_RibTrfase_Edin.
[Graphical view]
PfamPF03496. ADPrib_exo_Tox. 1 hit.
[Graphical view]
PIRSFPIRSF016951. MADP_ribosyltransf_Edin. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP15879.

Entry information

Entry nameARC3_CBDP
AccessionPrimary (citable) accession number: P15879
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references