VIS_VIBS1
ID VIS_VIBS1 Reviewed; 249 AA.
AC A3UNN4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Putative NAD(+)--arginine ADP-ribosyltransferase Vis;
DE EC=2.4.2.31;
DE AltName: Full=Putative mono(ADP-ribosyl)transferase;
DE Short=mADPRT;
DE Short=mART;
DE AltName: Full=Toxin Vis;
DE Flags: Precursor;
GN ORFNames=V12B01_18061;
OS Vibrio splendidus (strain 12B01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314291;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12B01;
RA Polz M., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS A TOXIN, EXPRESSION IN YEAST, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-189 AND GLU-191.
RC STRAIN=12B01;
RX PubMed=21170356; DOI=10.1371/journal.pcbi.1001029;
RA Fieldhouse R.J., Turgeon Z., White D., Merrill A.R.;
RT "Cholera- and anthrax-like toxins are among several new ADP-
RT ribosyltransferases.";
RL PLoS Comput. Biol. 6:E1001029-E1001029(2010).
CC -!- FUNCTION: A probable mono(ADP-ribosyl)transferase, it may ADP-
CC ribosylate Arg in target protein(s). Upon expression in yeast cells
CC causes cell death. {ECO:0000269|PubMed:21170356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AAMR01000004; EAP95748.1; -; Genomic_DNA.
DR RefSeq; WP_004732479.1; NZ_CH724170.1.
DR PDB; 4XZJ; X-ray; 1.80 A; A=20-240.
DR PDB; 4XZK; X-ray; 1.80 A; A=20-240.
DR PDB; 4Y1W; X-ray; 1.40 A; A=20-240.
DR PDB; 4YC0; X-ray; 1.50 A; A=20-240.
DR PDBsum; 4XZJ; -.
DR PDBsum; 4XZK; -.
DR PDBsum; 4Y1W; -.
DR PDBsum; 4YC0; -.
DR AlphaFoldDB; A3UNN4; -.
DR SMR; A3UNN4; -.
DR HOGENOM; CLU_1115401_0_0_6; -.
DR Proteomes; UP000005350; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR003540; ADP-ribosyltransferase.
DR Pfam; PF03496; ADPrib_exo_Tox; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; NAD; NADP; Nucleotide-binding;
KW Nucleotidyltransferase; Secreted; Signal; Toxin; Transferase; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..249
FT /note="Putative NAD(+)--arginine ADP-ribosyltransferase
FT Vis"
FT /id="PRO_0000410947"
FT DOMAIN 31..223
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 68..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 117..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 189..191
FT /note="EAE->AAA: Restores 60% growth in yeast."
FT MUTAGEN 189
FT /note="E->A: Restores 20% growth in yeast."
FT /evidence="ECO:0000269|PubMed:21170356"
FT MUTAGEN 191
FT /note="E->A: Restores 40% growth in yeast."
FT /evidence="ECO:0000269|PubMed:21170356"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:4Y1W"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:4YC0"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 164..176
FT /evidence="ECO:0007829|PDB:4Y1W"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:4Y1W"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4Y1W"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4Y1W"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:4Y1W"
SQ SEQUENCE 249 AA; 28087 MW; 5215E7F00F1F4FB3 CRC64;
MNTRFLLLLC CLSFTTFSQP FDAIKQPNRS EEEVTQLAED FKDWSKASNG WRYSFITANE
KEAVEDFSIS GYQTANDYLR ATDTSTWGVA GADARQYIRT VKSALNKLPK YKGTAYRGTW
VKLSLLNKLE EGDVLVEPAF TSTSTLPEVA KRFSVVHPNS PQRLKRVLFE VKINQGGHTI
AGLSEYSKEA EVLFAPNAHF RITQIERTSN HTYIGVETVK ASAVKNTQKY NLYSGEEVEA
SFWHSLVCT
