P15879 (ARC3_CBDP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mono-ADP-ribosyltransferase C3
EC=2.4.2.-

Alternative name(s):
Exoenzyme C3

Gene names

Name:

C3

Organism

Clostridium botulinum D phage (Clostridium botulinum D bacteriophage)

Taxonomic identifier

29342 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › unclassified Myoviridae › Clostridium botulinum C phage

Virus host

Clostridium botulinum [TaxID: 1491]

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Host-virus interaction
Cellular component	Secreted
Domain	Signal
Ligand	NAD
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: InterPro protein ADP-ribosylation Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transferase activity, transferring pentosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 40

40

Ref.1

Chain

41 – 251

211

Mono-ADP-ribosyltransferase C3

PRO_0000020755

Regions

Nucleotide binding

128 – 131

4

NAD

Nucleotide binding

167 – 169

3

NAD

Nucleotide binding

183 – 186

4

NAD

Nucleotide binding

212 – 214

3

NAD

Sites

Binding site

80

1

NAD

Binding site

87

1

NAD

Binding site

91

1

NAD

Site

214

1

Transition state stabilizer

Experimental info

Mutagenesis

99

1

G → D: Reduces interaction with human RALA. Ref.7

Mutagenesis

109

1

E → A: Loss of interaction with human RALA. Ref.7

Mutagenesis

174

1

S → A: No effect on enzyme activity. Ref.5

Mutagenesis

182

1

Q → A: No effect on NAD binding. No effect on enzyme activity. Ref.5

Mutagenesis

186

1

R → E: Loss of NAD binding and loss of activity. Ref.5

Mutagenesis

212

1

Q → A: Reduces affinity for NAD 2-fold. No effect on enzyme activity. Ref.5

Secondary structure

1

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251

Helix Strand Turn

Details...

Helix

52 – 66

15

Helix

70 – 92

23

Turn

93 – 95

3

Helix

102 – 114

13

Helix

115 – 117

3

Beta strand

124 – 130

7

Helix

132 – 135

4

Turn

137 – 142

6

Beta strand

148 – 150

3

Helix

152 – 162

11

Beta strand

166 – 171

6

Beta strand

173 – 178

6

Beta strand

183 – 194

12

Turn

204 – 206

3

Turn

208 – 211

4

Beta strand

214 – 217

4

Beta strand

219 – 230

12

Turn

232 – 234

3

Beta strand

237 – 247

11

Sequences

	Sequence		Length	Mass (Da)
	P15879 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 03D6C8A16FACA46C	FASTA	251	27,841
	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

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.

RefSeq

YP_398578.1. NC_007581.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P15879.

SMR

P15879. Positions 41-251.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15879. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3773098.

Family and domain databases

InterPro

IPR003540. ADP-ribosyltransferase.
IPR016678. Mono-ADP_RibTrfase_Edin.
[Graphical view]

Pfam

PF03496. ADPrib_exo_Tox. 1 hit.
[Graphical view]

PIRSF

PIRSF016951. MADP_ribosyltransf_Edin. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P15879.

Entry information

Entry name

ARC3_CBDP

Accession

Primary (citable) accession number: P15879

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program