ARC3_CBCP
ID ARC3_CBCP Reviewed; 244 AA.
AC Q00901;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Mono-ADP-ribosyltransferase C3;
DE EC=2.4.2.-;
DE AltName: Full=Exoenzyme C3;
DE Flags: Precursor;
OS Clostridium botulinum C phage (Clostridium botulinum C bacteriophage).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=12336;
OH NCBI_TaxID=36828; Clostridium botulinum C.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 41-232.
RC STRAIN=003-9;
RX PubMed=1918048; DOI=10.1016/s0021-9258(18)54999-1;
RA Nemoto Y., Namba T., Kozaki S., Narumiya S.;
RT "Clostridium botulinum C3 ADP-ribosyltransferase gene. Cloning, sequencing,
RT and expression of a functional protein in Escherichia coli.";
RL J. Biol. Chem. 266:19312-19319(1991).
RN [2]
RP PROTEIN SEQUENCE OF 41-59.
RC STRAIN=6813;
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).
CC -!- FUNCTION: ADP-ribosylates eukaryotic Rho and Rac proteins on an
CC asparagine residue. {ECO:0000250|UniProtKB:P15879}.
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:0000250|UniProtKB:P15879};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P15879}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1917836,
CC ECO:0000269|PubMed:1918048}.
CC -!- SIMILARITY: To exoenzymes 3 of C.limosum and C.botulinum D phage, and
CC to S.aureus ediN. {ECO:0000305}.
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DR EMBL; M74038; AAA23212.1; -; Genomic_DNA.
DR PIR; A41021; A41021.
DR PDB; 1R45; X-ray; 1.57 A; A/B/C/D=41-244.
DR PDB; 1R4B; X-ray; 1.85 A; A/B=41-244.
DR PDBsum; 1R45; -.
DR PDBsum; 1R4B; -.
DR SMR; Q00901; -.
DR EvolutionaryTrace; Q00901; -.
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; NAD;
KW Nucleotidyltransferase; Secreted; Signal; Transferase.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:1917836,
FT ECO:0000269|PubMed:1918048"
FT CHAIN 41..244
FT /note="Mono-ADP-ribosyltransferase C3"
FT /id="PRO_0000020754"
FT DOMAIN 44..244
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 213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 128..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 167..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 182..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT BINDING 211..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT SITE 213
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15879"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:1R45"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:1R45"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:1R45"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:1R45"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1R45"
SQ SEQUENCE 244 AA; 27359 MW; B78E5B1B9C16DF23 CRC64;
MKGIRKSILC LVLSAGVIAP VTTSIVQSPQ KCYACTVDKG SYADTFTEFT NVEEAKKWGN
AQYKKYGLSK PEQEAIKFYT RDASKINGPL RANQGNENGL PADILQKVKL IDQSFSKMKM
PQNIILFRGD DPAYLGPEFQ DKILNKDGTI NKTVFEQVKA KFLKKDRTEY GYISTSLMSA
QFGGRPIVTK FKVTNGSKGG YIDPISYFPG QLEVLLPRNN SYYISDMQIS PNNRQIMITA
MIFK
