SPVB_SALDU
ID SPVB_SALDU Reviewed; 593 AA.
AC P24419;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 90.
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; Synonyms=vsdC;
OS Salmonella dublin.
OG Plasmid pSDL2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=98360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lane;
RX PubMed=2041471; DOI=10.1111/j.1365-2958.1991.tb02111.x;
RA Krause M., Roudier C., Fierer J., Harwood J., Guiney D.;
RT "Molecular analysis of the virulence locus of the Salmonella dublin plasmid
RT pSDL2.";
RL Mol. Microbiol. 5:307-316(1991).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=Lane;
RX PubMed=1400193; DOI=10.1128/jb.174.20.6418-6423.1992;
RA Roudier C., Fierer J., Guiney D.G.;
RT "Characterization of translation termination mutations in the spv operon of
RT the Salmonella virulence plasmid pSDL2.";
RL J. Bacteriol. 174:6418-6423(1992).
RN [3]
RP FUNCTION AS AN ADP-RIBOSYLTRANSFERASE, FUNCTION IN MOUSE VIRULENCE, AND
RP MUTAGENESIS OF 538-GLU--GLU-540.
RC STRAIN=Lane;
RX PubMed=11260464; DOI=10.1046/j.1365-2958.2001.02360.x;
RA Lesnick M.L., Reiner N.E., Fierer J., Guiney D.G.;
RT "The Salmonella spvB virulence gene encodes an enzyme that ADP-ribosylates
RT actin and destabilizes the cytoskeleton of eukaryotic cells.";
RL Mol. Microbiol. 39:1464-1470(2001).
RN [4]
RP FUNCTION IN INFECTION OF HUMAN MACROPHAGES, MUTAGENESIS OF
RP 538-GLU--GLU-540, AND SECRETION VIA SPI-2 TYPE III SECRETION SYSTEM.
RC STRAIN=Lane;
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 muscle and non-muscle actin. ADP-
CC ribosylates Chinese hamster ovary and HeLa cell actin as well as rabbit
CC muscle, porcine heart actin and non-muscle beta- and gamma-actin. ADP-
CC ribosylation of actin prevents the polymerization of G actin to F
CC actin, causing actin filament depolymerization, destruction of the
CC cytoskeleton and cytotoxicity; this requires only the C-terminal 120
CC residues. Does not possess NAD(+)-glycohydrolase activity, unlike most
CC mART enzymes. {ECO:0000269|PubMed:11260464,
CC ECO:0000269|PubMed:12438395}.
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).
CC -!- DISRUPTION PHENOTYPE: A non-polar disruption of this gene is no longer
CC virulent in mouse infection. {ECO:0000269|PubMed:1400193}.
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; X56727; CAA40049.1; -; Genomic_DNA.
DR PIR; S15215; S15215.
DR RefSeq; WP_001675599.1; NZ_VDCP01000013.1.
DR RefSeq; YP_001716113.1; NC_010422.1.
DR RefSeq; YP_006954901.1; NC_019106.1.
DR AlphaFoldDB; P24419; -.
DR SMR; P24419; -.
DR PHI-base; PHI:4516; -.
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 1: Evidence at protein level;
KW Glycosyltransferase; NAD; NADP; Nucleotide-binding; Nucleotidyltransferase;
KW Plasmid; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..593
FT /note="Mono(ADP-ribosyl)transferase SpvB"
FT /id="PRO_0000221664"
FT DOMAIN 375..578
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT REGION 361..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT MUTAGEN 538..540
FT /note="EAE->DAD: No ADP-ribosylation of actin, 100- to
FT 1000-fold reduction of virulence in mice."
FT /evidence="ECO:0000269|PubMed:11260464,
FT ECO:0000269|PubMed:12438395"
SQ SEQUENCE 593 AA; 65614 MW; ECDC218FC41D6567 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 PPPPPMMGGN SSRPKSKWAI VEESKQIQAL RYYSAQGYSV INKYLRGDDY
PETQAKETLL SRDYLSTNEP SDEEFKNAMS VYINDIAEGL SSLPETDHRV VYRGLKLDKP
ALSDVLKEYT TIGNIIIDKA FMSTSPDKAW INDTILNIYL EKGHKGRILG DVAHFKGEAE
MLFPPNTKLK IESIVNCGSQ DFASQLSKLR LSDDATADTN RIKRIINMRV LNS
