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P15879

- ARC3_CBDP

UniProt

P15879 - ARC3_CBDP

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

        10         20         30         40         50
MKGLRKSILC LVLSAGVIAP VTSGMIQSPQ KCYAYSINQK AYSNTYQEFT
60 70 80 90 100
NIDQAKAWGN AQYKKYGLSK SEKEAIVSYT KSASEINGKL RQNKGVINGF
110 120 130 140 150
PSNLIKQVEL LDKSFNKMKT PENIMLFRGD DPAYLGTEFQ NTLLNSNGTI
160 170 180 190 200
NKTAFEKAKA KFLNKDRLEY GYISTSLMNV SQFAGRPIIT KFKVAKGSKA
210 220 230 240 250
GYIDPISAFA GQLEMLLPRH STYHIDDMRL SSDGKQIIIT ATMMGTAINP

K
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 29, 2014
This is version 78 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