ID   SPVB_SALEN              Reviewed;         591 AA.
AC   P55220;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Mono(ADP-ribosyl)transferase SpvB;
DE            Short=mADPRT;
DE            Short=mART;
DE            EC=2.4.2.31;
DE   AltName: Full=65 kDa virulence protein;
DE   AltName: Full=NAD(+)--arginine ADP-ribosyltransferase;
DE   AltName: Full=Toxin SpvB;
GN   Name=spvB;
OS   Salmonella enteritidis.
OG   Plasmid pNL2001.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=149539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AL1190;
RX   PubMed=8081495; DOI=10.1099/00221287-140-6-1307;
RA   Suzuki S., Komase K., Matsui H., Abe A., Kawahara K., Tamura Y., Kijima M.,
RA   Danbara H., Nakamura M., Sato S.;
RT   "Virulence region of plasmid pNL2001 of Salmonella enteritidis.";
RL   Microbiology 140:1307-1318(1994).
CC   -!- FUNCTION: Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin
CC       on 'Arg-177'. ADP-ribosylation prevents the polymerization of G-actin
CC       to F-actin, causing actin filament depolymerization, destruction of the
CC       cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase
CC       activity, unlike most mART enzymes (By similarity). {ECO:0000250}.
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. Note=Secreted via the type III
CC       secretion system 1 (SPI-2 TTSS). {ECO:0000250}.
CC   -!- MISCELLANEOUS: In Salmonella spp. the spv gene cluster is encoded on a
CC       highly transmissible plasmid.
CC   -!- SIMILARITY: Belongs to the SpvB family. {ECO:0000305}.
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DR   EMBL; D14490; BAA03383.1; -; Genomic_DNA.
DR   AlphaFoldDB; P55220; -.
DR   SMR; P55220; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   InterPro; IPR003284; Sal_SpvB.
DR   Pfam; PF03496; ADPrib_exo_Tox; 1.
DR   Pfam; PF03534; SpvB; 1.
DR   PRINTS; PR01341; SALSPVBPROT.
DR   PROSITE; PS51996; TR_MART; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; NAD; NADP; Nucleotide-binding; Nucleotidyltransferase;
KW   Plasmid; Secreted; Toxin; Transferase; Virulence.
FT   CHAIN           1..591
FT                   /note="Mono(ADP-ribosyl)transferase SpvB"
FT                   /id="PRO_0000221665"
FT   DOMAIN          373..576
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        471
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        501
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        538
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
SQ   SEQUENCE   591 AA;  65350 MW;  F83F33E02915D58F CRC64;
     MLILNGFSSA TLALITPPFL PKGGKALSQS GPDGLASITL PLPISAERGF APALALHYSS
     GGGNGPFGVG WSCATMSIAR STSHGVPQYN DSDEFLGPDG EVLVQTLSTG DAPNPVTCFA
     YGDVSFPQSY TVTRYQPRTE SSFYRLEYWV GNSNGDDFWL LHDSNGILHL LGKTAAARLS
     DPQAASHTAQ WLVEESVTPA GEHIYYSYLA ENGDNVDLNG NEAGRDRSAM RYLSKVQYGN
     ATPAADLYLW TSATPAVQWL FTLVFDYGER GVDPQVPPAF TAQNSWLARQ DPFSLYNYGF
     EIRLHRLCRQ VLMFHHFPDE LGEADTLVSR LLLEYDENPI LTQLCAARTL AYEGDGYRRA
     PVNNMMPPPP PPPMMGGNSS RPKSKWAIVE ESKQIQALRY YSAQGYSVIN KYLRGDDYPE
     TQAKETLLSR DYLSTNEPSD EEFKNAMSVY INDIAEGLSS LPETDHRVVY RGLKLDKPAL
     SDVLKEYTTI GNIIIDKAFM STSPDKAWIN DTILNIYLEK GHKGRILGDV AHFKGEAEML
     FPPNTKLKIE SIVNCGSQDF ASQLSKLRLS DDATADTNRI KRIINMRVLN S