SPVB_SALCH
ID SPVB_SALCH Reviewed; 591 AA.
AC P17450; Q5J4C8; Q7DIJ8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=Protein M2 in mba region;
DE AltName: Full=Toxin SpvB;
GN Name=spvB; OrderedLocusNames=SCH_V04;
OS Salmonella choleraesuis (strain SC-B67).
OG Plasmid pKDSc50, and Plasmid pSCV50.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RF-1; PLASMID=pKDSc50;
RX PubMed=2336400; DOI=10.1093/nar/18.8.2181;
RA Matsui H.;
RT "Nucleotide sequences of genes encoding 32 kDa and 70 kDa polypeptides in
RT mba region of the virulence plasmid, pKDSc50, of Salmonella choleraesuis.";
RL Nucleic Acids Res. 18:2181-2181(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RF-1; PLASMID=pKDSc50;
RX PubMed=11254626; DOI=10.1128/iai.69.4.2612-2620.2001;
RA Haneda T., Okada N., Nakazawa N., Kawakami T., Danbara H.;
RT "Complete DNA sequence and comparative analysis of the 50-kilobase
RT virulence plasmid of Salmonella enterica serovar Choleraesuis.";
RL Infect. Immun. 69:2612-2620(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67; PLASMID=pSCV50;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; X52035; CAA36278.1; -; Genomic_DNA.
DR EMBL; AB040415; BAB20511.1; -; Genomic_DNA.
DR EMBL; AY509003; AAS58877.1; -; Genomic_DNA.
DR PIR; S09498; S09498.
DR RefSeq; WP_001541538.1; NC_006855.1.
DR AlphaFoldDB; P17450; -.
DR SMR; P17450; -.
DR EnsemblBacteria; AAS58877; AAS58877; SCH_V04.
DR KEGG; sec:SCH_V04; -.
DR HOGENOM; CLU_458478_0_0_6; -.
DR OMA; RAPVNNI; -.
DR Proteomes; UP000000538; Plasmid pSCV50.
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_0000221663"
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"
FT CONFLICT 118
FT /note="C -> S (in Ref. 1; CAA36278 and 2; BAB20511)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="A -> R (in Ref. 1; CAA36278 and 2; BAB20511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 65272 MW; 16030F6BAA21F813 CRC64;
MLILNGFSSA TLALITPPSL 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
PVNNIMPPPP PPPMMGGNSS RPKSKWAIVE ESKQIQALRY YSAQGYSVIN KYLRGDDYPE
TQAKETLLSR DYLSTNEPSD EEFKNAMSVY INDIAEGLSS LPETDHRVVY RGLKLDKPAL
SDVLKEYTTI GNIIIDKAFM STSPDKAWIN DTILNIYLEK GHKGRILGDV AHFKGEAEML
FPPNTKLKIE SIVNCGSQDF ASQLSKLRLS DDATADTNRI KRIINMRVLN S
