ID   SPVB_SALT1              Reviewed;         591 AA.
AC   D0ZHS9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Mono(ADP-ribosyl)transferase SpvB;
DE            Short=mADPRT;
DE            Short=mART;
DE            EC=2.4.2.31;
DE   AltName: Full=NAD(+)--arginine ADP-ribosyltransferase;
DE   AltName: Full=Toxin SpvB;
GN   Name=spvB; OrderedLocusNames=STM14_5562;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OG   Plasmid unnamed.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
RP   SUBCELLULAR LOCATION UPON INFECTION OF HUMAN MACROPHAGES.
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=12438395; DOI=10.1128/iai.70.12.7126-7135.2002;
RA   Browne S.H., Lesnick M.L., Guiney D.G.;
RT   "Genetic requirements for Salmonella-induced cytopathology in human
RT   monocyte-derived macrophages.";
RL   Infect. Immun. 70:7126-7135(2002).
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 {ECO:0000269|PubMed:12438395}.
CC       Note=Secreted via the type III secretion system 1 (SPI-2 TTSS).
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}.
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; CP001362; ACY86472.1; -; Genomic_DNA.
DR   RefSeq; WP_001676648.1; NC_016855.1.
DR   AlphaFoldDB; D0ZHS9; -.
DR   SMR; D0ZHS9; -.
DR   EnsemblBacteria; ACY86472; ACY86472; STM14_5562.
DR   KEGG; seo:STM14_5562; -.
DR   PATRIC; fig|588858.6.peg.50; -.
DR   HOGENOM; CLU_458478_0_0_6; -.
DR   OMA; RAPVNNI; -.
DR   BioCyc; SENT588858:STM14_RS00195-MON; -.
DR   PHI-base; PHI:3760; -.
DR   Proteomes; UP000002695; Plasmid.
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_0000410492"
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;  65420 MW;  A38F33E02915D5F4 CRC64;
     MLILNGFSSA TLALITPPFL PKGGKALSQS GPDGLASITL PLPISAERGF APALALHYSS
     GGGNGPFGVG WSCATMSIAR RTSHGVPQYN 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