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P15879

- ARC3_CBDP

UniProt

P15879 - ARC3_CBDP

Protein

Mono-ADP-ribosyltransferase C3

Gene

C3

Organism
Clostridium botulinum D phage (Clostridium botulinum D bacteriophage)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei80 – 801NAD2 Publications
    Binding sitei87 – 871NAD2 Publications
    Binding sitei91 – 911NAD2 Publications
    Sitei214 – 2141Transition state stabilizer

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi128 – 1314NAD2 Publications
    Nucleotide bindingi167 – 1693NAD2 Publications
    Nucleotide bindingi183 – 1864NAD2 Publications
    Nucleotide bindingi212 – 2143NAD2 Publications

    GO - Molecular functioni

    1. transferase activity, transferring pentosyl groups Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: InterPro
    2. protein ADP-ribosylation Source: InterPro
    3. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mono-ADP-ribosyltransferase C3 (EC:2.4.2.-)
    Alternative name(s):
    Exoenzyme C3
    Gene namesi
    Name:C3
    OrganismiClostridium botulinum D phage (Clostridium botulinum D bacteriophage)
    Taxonomic identifieri29342 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridae
    Virus hostiClostridium botulinum [TaxID: 1491]

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991G → D: Reduces interaction with human RALA. 1 Publication
    Mutagenesisi109 – 1091E → A: Loss of interaction with human RALA. 1 Publication
    Mutagenesisi174 – 1741S → A: No effect on enzyme activity. 1 Publication
    Mutagenesisi182 – 1821Q → A: No effect on NAD binding. No effect on enzyme activity. 1 Publication
    Mutagenesisi186 – 1861R → E: Loss of NAD binding and loss of activity. 1 Publication
    Mutagenesisi212 – 2121Q → A: Reduces affinity for NAD 2-fold. No effect on enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 40401 PublicationAdd
    BLAST
    Chaini41 – 251211Mono-ADP-ribosyltransferase C3PRO_0000020755Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer. Interacts with human RALA.3 Publications

    Protein-protein interaction databases

    IntActiP15879. 1 interaction.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi52 – 6615
    Helixi70 – 9223
    Turni93 – 953
    Helixi102 – 11413
    Helixi115 – 1173
    Beta strandi124 – 1307
    Helixi132 – 1354
    Turni137 – 1426
    Beta strandi148 – 1503
    Helixi152 – 16211
    Beta strandi166 – 1716
    Beta strandi173 – 1786
    Beta strandi183 – 19412
    Turni204 – 2063
    Turni208 – 2114
    Beta strandi214 – 2174
    Beta strandi219 – 23012
    Turni232 – 2343
    Beta strandi237 – 24711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP15879.
    SMRiP15879. Positions 41-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15879.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR003540. ADP-ribosyltransferase.
    IPR016678. Mono-ADP_RibTrfase_Edin.
    [Graphical view]
    PfamiPF03496. ADPrib_exo_Tox. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016951. MADP_ribosyltransf_Edin. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15879-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGLRKSILC LVLSAGVIAP VTSGMIQSPQ KCYAYSINQK AYSNTYQEFT    50
    NIDQAKAWGN AQYKKYGLSK SEKEAIVSYT KSASEINGKL RQNKGVINGF 100
    PSNLIKQVEL LDKSFNKMKT PENIMLFRGD DPAYLGTEFQ NTLLNSNGTI 150
    NKTAFEKAKA KFLNKDRLEY GYISTSLMNV SQFAGRPIIT KFKVAKGSKA 200
    GYIDPISAFA GQLEMLLPRH STYHIDDMRL SSDGKQIIIT ATMMGTAINP 250
    K 251
    Length:251
    Mass (Da):27,841
    Last modified:July 1, 1993 - v2
    Checksum:i03D6C8A16FACA46C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59040 Genomic DNA. Translation: CAA41768.1.
    X51464 Genomic DNA. Translation: CAA35828.1.
    X59039 Genomic DNA. Translation: CAA41767.1.
    RefSeqiYP_398578.1. NC_007581.1.

    Genome annotation databases

    GeneIDi3773098.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59040 Genomic DNA. Translation: CAA41768.1 .
    X51464 Genomic DNA. Translation: CAA35828.1 .
    X59039 Genomic DNA. Translation: CAA41767.1 .
    RefSeqi YP_398578.1. NC_007581.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G24 X-ray 1.70 A/B/C/D 41-251 [» ]
    1GZE X-ray 2.70 A/B/C/D 41-251 [» ]
    1GZF X-ray 1.95 A/B/C/D 41-251 [» ]
    1UZI X-ray 1.89 A/B 41-251 [» ]
    2A78 X-ray 1.81 B 41-251 [» ]
    2A9K X-ray 1.73 B 41-251 [» ]
    2BOV X-ray 2.66 B 1-251 [» ]
    2C89 X-ray 1.85 A/B/C/D 41-251 [» ]
    2C8A X-ray 1.70 A/B/C/D 41-251 [» ]
    2C8B X-ray 1.70 X 41-251 [» ]
    2C8C X-ray 2.70 A/B/C/D 41-251 [» ]
    2C8D X-ray 2.20 A/B/C/D 41-251 [» ]
    2C8E X-ray 1.60 E/F/G 41-251 [» ]
    2C8F X-ray 2.50 E/F/G 41-251 [» ]
    2C8G X-ray 2.00 A/B/C/D 41-251 [» ]
    2C8H X-ray 1.65 A/B/C/D 41-251 [» ]
    ProteinModelPortali P15879.
    SMRi P15879. Positions 41-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P15879. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3773098.

    Miscellaneous databases

    EvolutionaryTracei P15879.

    Family and domain databases

    InterProi IPR003540. ADP-ribosyltransferase.
    IPR016678. Mono-ADP_RibTrfase_Edin.
    [Graphical view ]
    Pfami PF03496. ADPrib_exo_Tox. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016951. MADP_ribosyltransf_Edin. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiARC3_CBDP
    AccessioniPrimary (citable) accession number: P15879
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 77 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3