ID   CHELT_VIBCL             Reviewed;         601 AA.
AC   A2PU44;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=NAD(+)--arginine ADP-ribosyltransferase Chelt;
DE            EC=2.4.2.31;
DE   AltName: Full=Putative mono(ADP-ribosyl)transferase;
DE            Short=mADPRT;
DE            Short=mART;
DE   AltName: Full=Toxin Chelt;
DE   Flags: Precursor;
GN   ORFNames=A51_B1772;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MZO-3;
RA   Heidelberg J., Sebastian Y.;
RT   "Annotation of Vibrio cholerae MZO-3.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION AS A TOXIN, EXPRESSION IN YEAST, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF GLU-128 AND GLU-130.
RC   STRAIN=MZO-3;
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   -!- MISCELLANEOUS: Toxins are often highly strain specific; not encoded in
CC       strain ATCC 39315 / El Tor Inabe N16961.
CC   -!- SIMILARITY: Belongs to the enterotoxin A family. {ECO:0000305}.
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DR   EMBL; AAUU01000054; EAY40854.1; -; Genomic_DNA.
DR   RefSeq; WP_001897790.1; NZ_VTWR01000001.1.
DR   AlphaFoldDB; A2PU44; -.
DR   SMR; A2PU44; -.
DR   PATRIC; fig|666.2183.peg.780; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; IPR001144; Enterotoxin_A.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   Pfam; PF01375; Enterotoxin_a; 1.
DR   PRINTS; PR00771; ENTEROTOXINA.
DR   SUPFAM; SSF69318; SSF69318; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Enterotoxin; Glycosyltransferase; NAD; NADP;
KW   Nucleotide-binding; Nucleotidyltransferase; Secreted; Signal; Toxin;
KW   Transferase; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..601
FT                   /note="NAD(+)--arginine ADP-ribosyltransferase Chelt"
FT                   /id="PRO_0000410945"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000305"
FT   BINDING         26..43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   DISULFID        205..220
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         128..130
FT                   /note="ENE->ANA: Fully restores growth in yeast."
FT   MUTAGEN         128
FT                   /note="E->A: Restores 10% growth in yeast."
FT                   /evidence="ECO:0000269|PubMed:21170356"
FT   MUTAGEN         130
FT                   /note="E->A: Restores 20% growth in yeast."
FT                   /evidence="ECO:0000269|PubMed:21170356"
SQ   SEQUENCE   601 AA;  68790 MW;  C427AEC7578DBC7D CRC64;
     MKTIISLIFI MFPLFVSAHN GNFYRADSRS PNEIKDLGGL YPRGYYDFFE RGTPMSISLY
     DHARGAPSGN TRYDDGFVST TTDIDSAHEI GQNILSGYTE YYIYLIAPAP NLLDVNAVLG
     RYSPHPQENE YSALGGIPWT QVIGWYVVNN GVLDRNIHRN RQFRADLFNN LSPALPSESY
     QFAGFEPEHP AWRQEPWINF APPGCGRNVR LTKHINQQDC SNSQEELVYK KLQDLRTQFK
     VDKKLKLVNK TSSNNIIFPN HDFIREWVDL DGNGDLSYCG FTVDSDGSRK RIVCAHNNGN
     FTYSSINISL SDYGWPKGQR FIDANGDGLV DYCRVQYVWT HLYCSLSLPG QYFSLDKDAG
     YLDAGYNNSR AWAKVIGTNK YSFCRLTSNG YICTDIDSYS TAFKDDDQGW ADSRYWMDID
     GNGGDDYCRL VYNWTHLRCN LQGKDGLWKR VESKYLDGGY PSLRFKIKMT SNKDNYCRIV
     RNHRVMECAY VSDNGEFHNY SLNMPFSLYN KNDIQFIDID GDNRDDICRY NSAPNTMECY
     LNQDKSFSQN KLVLYLSAKP ISSLGSGSSK IIRTFNSEKN SSAYCYNAGY GTLRCDEFVI
     Y