Mono-ADP-ribosyltransferase C3
Details
- Name
- Mono-ADP-ribosyltransferase C3
- Synonyms
- 2.4.2.-
- Exoenzyme C3
- Gene Name
- C3
- Organism
- Clostridium botulinum D phage
- Amino acid sequence
>lcl|BSEQ0016441|Mono-ADP-ribosyltransferase C3 MKGLRKSILCLVLSAGVIAPVTSGMIQSPQKCYAYSINQKAYSNTYQEFTNIDQAKAWGN AQYKKYGLSKSEKEAIVSYTKSASEINGKLRQNKGVINGFPSNLIKQVELLDKSFNKMKT PENIMLFRGDDPAYLGTEFQNTLLNSNGTINKTAFEKAKAKFLNKDRLEYGYISTSLMNV SQFAGRPIITKFKVAKGSKAGYIDPISAFAGQLEMLLPRHSTYHIDDMRLSSDGKQIIIT ATMMGTAINPK
- Number of residues
- 251
- Molecular Weight
- 27840.92
- Theoretical pI
- 10.2
- GO Classification
- Functionstransferase activity, transferring pentosyl groupsProcessespathogenesis / protein ADP-ribosylation / viral processComponentsextracellular region
- General Function
- Transferase activity, transferring pentosyl groups
- Specific Function
- ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue.
- Pfam Domain Function
- ADPrib_exo_Tox (PF03496)
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0016442|Mono-ADP-ribosyltransferase C3 (C3) ATGAAAGGTTTAAGAAAATCAATTTTATGTTTAGTTTTGTCAGCAGGAGTAATAGCTCCA GTAACATCTGGGATGATTCAAAGTCCTCAAAAATGTTATGCTTATTCCATTAATCAAAAG GCTTATTCAAATACTTACCAGGAGTTTACTAATATTGATCAAGCAAAAGCTTGGGGTAAT GCTCAGTATAAAAAGTATGGACTAAGCAAATCAGAAAAAGAAGCTATAGTATCATATACT AAAAGCGCTAGTGAAATAAATGGAAAGCTAAGACAAAATAAGGGAGTTATCAATGGATTT CCTTCAAATTTAATAAAACAAGTTGAACTTTTAGATAAATCTTTTAATAAAATGAAGACC CCTGAAAATATTATGTTATTTAGAGGCGACGACCCTGCTTATTTAGGAACAGAATTTCAA AACACTCTTCTTAATTCAAATGGTACAATTAATAAAACGGCTTTTGAAAAGGCTAAAGCT AAGTTTTTAAATAAAGATAGACTTGAATATGGATATATTAGTACTTCATTAATGAATGTT TCTCAATTTGCAGGAAGACCAATTATTACAAAATTTAAAGTAGCAAAAGGCTCAAAGGCA GGATATATTGACCCTATTAGTGCTTTTGCAGGACAACTTGAAATGTTGCTTCCTAGACAT AGTACTTATCATATAGACGATATGAGATTGTCTTCTGATGGTAAACAAATAATAATTACA GCAACAATGATGGGCACAGCTATCAATCCTAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P15879 UniProtKB Entry Name ARC3_CBDP GenBank Protein ID 505281 GenBank Gene ID X59040 - General References
- Popoff M, Boquet P, Gill DM, Eklund MW: DNA sequence of exoenzyme C3, an ADP-ribosyltransferase encoded by Clostridium botulinum C and D phages. Nucleic Acids Res. 1990 Mar 11;18(5):1291. [Article]
- Popoff MR, Hauser D, Boquet P, Eklund MW, Gill DM: Characterization of the C3 gene of Clostridium botulinum types C and D and its expression in Escherichia coli. Infect Immun. 1991 Oct;59(10):3673-9. [Article]
- Moriishi K, Syuto B, Yokosawa N, Oguma K, Saito M: Purification and characterization of ADP-ribosyltransferases (exoenzyme C3) of Clostridium botulinum type C and D strains. J Bacteriol. 1991 Oct;173(19):6025-9. [Article]
- Han S, Arvai AS, Clancy SB, Tainer JA: Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. J Mol Biol. 2001 Jan 5;305(1):95-107. [Article]
- Menetrey J, Flatau G, Stura EA, Charbonnier JB, Gas F, Teulon JM, Le Du MH, Boquet P, Menez A: NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme. J Biol Chem. 2002 Aug 23;277(34):30950-7. Epub 2002 May 23. [Article]
- Evans HR, Holloway DE, Sutton JM, Ayriss J, Shone CC, Acharya KR: C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal form and a reassessment of NAD-induced flexure. Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1502-5. Epub 2004 Jul 21. [Article]
- Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K: Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme. EMBO J. 2005 Oct 19;24(20):3670-80. Epub 2005 Sep 22. [Article]
- Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR: Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase. Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. [Article]