ARC3_CBDP
ID ARC3_CBDP Reviewed; 251 AA.
AC P15879;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Mono-ADP-ribosyltransferase C3;
DE EC=2.4.2.- {ECO:0000269|PubMed:12029083};
DE AltName: Full=Exoenzyme C3;
DE Flags: Precursor;
GN Name=C3;
OS Clostridium botulinum D phage (Clostridium botulinum D bacteriophage).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=29342;
OH NCBI_TaxID=1491; Clostridium botulinum.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-251, AND PROTEIN SEQUENCE OF 41-66.
RC STRAIN=1873;
RX PubMed=2108433; DOI=10.1093/nar/18.5.1291;
RA Popoff M.R., Boquet P., Gill D.M., Eklund M.W.;
RT "DNA sequence of exoenzyme C3, an ADP-ribosyltransferase encoded by
RT Clostridium botulinum C and D phages.";
RL Nucleic Acids Res. 18:1291-1291(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC STRAIN=1873;
RX PubMed=1910014; DOI=10.1128/iai.59.10.3673-3679.1991;
RA Popoff M.R., Hauser D., Boquet P., Eklund M.W., Gill D.M.;
RT "Characterization of the C3 gene of Clostridium botulinum types C and D and
RT its expression in Escherichia coli.";
RL Infect. Immun. 59:3673-3679(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-60.
RC STRAIN=1873;
RX PubMed=1917836; DOI=10.1128/jb.173.19.6025-6029.1991;
RA Moriishi K., Syuto B., Yokosawa N., Oguma K., Saito M.;
RT "Purification and characterization of ADP-ribosyltransferases (exoenzyme
RT C3) of Clostridium botulinum type C and D strains.";
RL J. Bacteriol. 173:6025-6029(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 41-251, AND FUNCTION.
RX PubMed=11114250; DOI=10.1006/jmbi.2000.4292;
RA Han S., Arvai A.S., Clancy S.B., Tainer J.A.;
RT "Crystal structure and novel recognition motif of rho ADP-ribosylating C3
RT exoenzyme from Clostridium botulinum: structural insights for recognition
RT specificity and catalysis.";
RL J. Mol. Biol. 305:95-107(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 41-251 IN COMPLEX WITH NAD,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF SER-174; GLN-182;
RP ARG-186 AND GLN-212.
RX PubMed=12029083; DOI=10.1074/jbc.m201844200;
RA Menetrey J., Flatau G., Stura E.A., Charbonnier J.-B., Gas F.,
RA Teulon J.-M., Le Du M.-H., Boquet P., Menez A.;
RT "NAD binding induces conformational changes in Rho ADP-ribosylating
RT clostridium botulinum C3 exoenzyme.";
RL J. Biol. Chem. 277:30950-30957(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 41-251, AND FUNCTION.
RX PubMed=15272191; DOI=10.1107/s0907444904011680;
RA Evans H.R., Holloway D.E., Sutton J.M., Ayriss J., Shone C.C.,
RA Acharya K.R.;
RT "C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal
RT form and a reassessment of NAD-induced flexure.";
RL Acta Crystallogr. D 60:1502-1505(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 41-251 IN COMPLEX WITH NAD AND
RP HUMAN RALA, FUNCTION, AND MUTAGENESIS OF GLY-99 AND GLU-109.
RX PubMed=16177825; DOI=10.1038/sj.emboj.7600813;
RA Pautsch A., Vogelsgesang M., Traenkle J., Herrmann C., Aktories K.;
RT "Crystal structure of the C3bot-RalA complex reveals a novel type of action
RT of a bacterial exoenzyme.";
RL EMBO J. 24:3670-3680(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 41-251 IN COMPLEX WITH HUMAN
RP RALA.
RX PubMed=15809419; DOI=10.1073/pnas.0501525102;
RA Holbourn K.P., Sutton J.M., Evans H.R., Shone C.C., Acharya K.R.;
RT "Molecular recognition of an ADP-ribosylating Clostridium botulinum C3
RT exoenzyme by RalA GTPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5357-5362(2005).
CC -!- FUNCTION: ADP-ribosylates eukaryotic Rho and Rac proteins on an
CC asparagine residue. {ECO:0000269|PubMed:11114250,
CC ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:15272191,
CC ECO:0000269|PubMed:16177825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparaginyl-[protein] + NAD(+) = H(+) + N(4)-(ADP-D-
CC ribosyl)-L-asparaginyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:58228, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:15090,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:50347,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:142555;
CC Evidence={ECO:0000269|PubMed:12029083};
CC -!- SUBUNIT: Monomer (PubMed:12029083). Interacts with human RALA
CC (PubMed:15809419, PubMed:16177825). {ECO:0000269|PubMed:12029083,
CC ECO:0000269|PubMed:15809419, ECO:0000269|PubMed:16177825}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2108433}.
CC -!- SIMILARITY: To exoenzymes 3 of C.limosum and C.botulinum C phage, and
CC to S.aureus ediN. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59040; CAA41768.1; -; Genomic_DNA.
DR EMBL; X51464; CAA35828.1; -; Genomic_DNA.
DR EMBL; X59039; CAA41767.1; -; Genomic_DNA.
DR PDB; 1G24; X-ray; 1.70 A; A/B/C/D=41-251.
DR PDB; 1GZE; X-ray; 2.70 A; A/B/C/D=41-251.
DR PDB; 1GZF; X-ray; 1.95 A; A/B/C/D=41-251.
DR PDB; 1UZI; X-ray; 1.89 A; A/B=41-251.
DR PDB; 2A78; X-ray; 1.81 A; B=41-251.
DR PDB; 2A9K; X-ray; 1.73 A; B=41-251.
DR PDB; 2BOV; X-ray; 2.66 A; B=1-251.
DR PDB; 2C89; X-ray; 1.85 A; A/B/C/D=41-251.
DR PDB; 2C8A; X-ray; 1.70 A; A/B/C/D=41-251.
DR PDB; 2C8B; X-ray; 1.70 A; X=41-251.
DR PDB; 2C8C; X-ray; 2.70 A; A/B/C/D=41-251.
DR PDB; 2C8D; X-ray; 2.20 A; A/B/C/D=41-251.
DR PDB; 2C8E; X-ray; 1.60 A; E/F/G=41-251.
DR PDB; 2C8F; X-ray; 2.50 A; E/F/G=41-251.
DR PDB; 2C8G; X-ray; 2.00 A; A/B/C/D=41-251.
DR PDB; 2C8H; X-ray; 1.65 A; A/B/C/D=41-251.
DR PDBsum; 1G24; -.
DR PDBsum; 1GZE; -.
DR PDBsum; 1GZF; -.
DR PDBsum; 1UZI; -.
DR PDBsum; 2A78; -.
DR PDBsum; 2A9K; -.
DR PDBsum; 2BOV; -.
DR PDBsum; 2C89; -.
DR PDBsum; 2C8A; -.
DR PDBsum; 2C8B; -.
DR PDBsum; 2C8C; -.
DR PDBsum; 2C8D; -.
DR PDBsum; 2C8E; -.
DR PDBsum; 2C8F; -.
DR PDBsum; 2C8G; -.
DR PDBsum; 2C8H; -.
DR SMR; P15879; -.
DR IntAct; P15879; 1.
DR DrugBank; DB02147; Cyclo-Tetrametavanadate.
DR EvolutionaryTrace; P15879; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR InterPro; IPR003540; ADP-ribosyltransferase.
DR InterPro; IPR016678; Mono-ADP_RibTrfase_C3/Edin.
DR Pfam; PF03496; ADPrib_exo_Tox; 1.
DR PIRSF; PIRSF016951; MADP_ribosyltransf_Edin; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase;
KW Host-virus interaction; NAD; Nucleotidyltransferase; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:2108433"
FT CHAIN 41..251
FT /note="Mono-ADP-ribosyltransferase C3"
FT /id="PRO_0000020755"
FT DOMAIN 47..246
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT BINDING 128..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT BINDING 167..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT BINDING 183..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT BINDING 212..214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12029083,
FT ECO:0000269|PubMed:16177825"
FT SITE 214
FT /note="Transition state stabilizer"
FT MUTAGEN 99
FT /note="G->D: Reduces interaction with human RALA."
FT /evidence="ECO:0000269|PubMed:16177825"
FT MUTAGEN 109
FT /note="E->A: Loss of interaction with human RALA."
FT /evidence="ECO:0000269|PubMed:16177825"
FT MUTAGEN 174
FT /note="S->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:12029083"
FT MUTAGEN 182
FT /note="Q->A: No effect on NAD binding. No effect on enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:12029083"
FT MUTAGEN 186
FT /note="R->E: Loss of NAD binding and loss of activity."
FT /evidence="ECO:0000269|PubMed:12029083"
FT MUTAGEN 212
FT /note="Q->A: Reduces affinity for NAD 2-fold. No effect on
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:12029083"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:1G24"
FT HELIX 70..92
FT /evidence="ECO:0007829|PDB:1G24"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1G24"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:1G24"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2C8B"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1G24"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1G24"
FT TURN 137..142
FT /evidence="ECO:0007829|PDB:1G24"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2C8B"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:1G24"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1G24"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1G24"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:1G24"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1G24"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:2A9K"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1G24"
FT STRAND 219..230
FT /evidence="ECO:0007829|PDB:1G24"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1G24"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:1G24"
SQ SEQUENCE 251 AA; 27841 MW; 03D6C8A16FACA46C CRC64;
MKGLRKSILC LVLSAGVIAP VTSGMIQSPQ KCYAYSINQK AYSNTYQEFT NIDQAKAWGN
AQYKKYGLSK SEKEAIVSYT KSASEINGKL RQNKGVINGF PSNLIKQVEL LDKSFNKMKT
PENIMLFRGD DPAYLGTEFQ NTLLNSNGTI NKTAFEKAKA KFLNKDRLEY GYISTSLMNV
SQFAGRPIIT KFKVAKGSKA GYIDPISAFA GQLEMLLPRH STYHIDDMRL SSDGKQIIIT
ATMMGTAINP K
