SPVB_SALTM
ID SPVB_SALTM Reviewed; 591 AA.
AC P21454;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=mkaA;
OS Salmonella typhimurium.
OG Plasmid pEX102.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TML R66;
RX PubMed=2693884; DOI=10.1016/0882-4010(89)90052-1;
RA Taira S., Rhen M.;
RT "Identification and genetic analysis of mkaA -- a gene of the Salmonella
RT typhimurium virulence plasmid necessary for intracellular growth.";
RL Microb. Pathog. 7:165-173(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-10.
RC PLASMID=pEX102;
RX PubMed=2037236; DOI=10.1016/0378-1097(91)90573-s;
RA Taira S., Baumann M., Riikonen P., Sukupolvi S., Rhen M.;
RT "Amino-terminal sequence analysis of four plasmid-encoded virulence-
RT associated proteins of Salmonella typhimurium.";
RL FEMS Microbiol. Lett. 77:319-323(1991).
RN [3]
RP FUNCTION AS AN ADP-RIBOSYLTRANSFERASE, ACTIVITY REGULATION, AND LACK OF
RP NAD(+)-GLYCOHYDROLASE ACTIVITY.
RX PubMed=10972829; DOI=10.1046/j.1365-2958.2000.02064.x;
RA Otto H., Tezcan-Merdol D., Girisch R., Haag F., Rhen M., Koch-Nolte F.;
RT "The spvB gene-product of the Salmonella enterica virulence plasmid is a
RT mono(ADP-ribosyl)transferase.";
RL Mol. Microbiol. 37:1106-1115(2000).
RN [4]
RP ACTIN AS SUBSTRATE, AND ACTIVITY REGULATION.
RX PubMed=11169102; DOI=10.1046/j.1365-2958.2001.02258.x;
RA Tezcan-Merdol D., Nyman T., Lindberg U., Haag F., Koch-Nolte F., Rhen M.;
RT "Actin is ADP-ribosylated by the Salmonella enterica virulence-associated
RT protein SpvB.";
RL Mol. Microbiol. 39:606-619(2001).
RN [5]
RP FUNCTION AS AN ADP-RIBOSYLTRANSFERASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIN
RP SUBSTRATES, AND LACK OF NAD(+)-GLYCOHYDROLASE ACTIVITY.
RX PubMed=16430223; DOI=10.1021/bi051810w;
RA Hochmann H., Pust S., von Figura G., Aktories K., Barth H.;
RT "Salmonella enterica SpvB ADP-ribosylates actin at position arginine-177-
RT characterization of the catalytic domain within the SpvB protein and a
RT comparison to binary clostridial actin-ADP-ribosylating toxins.";
RL Biochemistry 45:1271-1277(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 391-590 IN COMPLEX WITH NAD, AND
RP FUNCTION AS A MONO-ADP-RIBOSYLTRANSFERASE.
RX PubMed=16905096; DOI=10.1016/j.str.2006.05.022;
RA Margarit S.M., Davidson W., Frego L., Stebbins C.E.;
RT "A steric antagonism of actin polymerization by a Salmonella virulence
RT protein.";
RL Structure 14:1219-1229(2006).
CC -!- FUNCTION: Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin
CC on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on
CC nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers
CC monomeric G-actin but can weakly ADP-ribosylate F-actin. ADP-
CC ribosylation prevents the polymerization of G-actin to F-actin, causing
CC actin filament depolymerization, destruction of the cytoskeleton and
CC cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike
CC most mART enzymes. {ECO:0000269|PubMed:10972829,
CC ECO:0000269|PubMed:16430223, ECO:0000269|PubMed:16905096}.
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 -!- ACTIVITY REGULATION: Inhibited by novobiocin.
CC {ECO:0000269|PubMed:10972829, ECO:0000269|PubMed:11169102}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for NAD {ECO:0000269|PubMed:16430223};
CC Note=For a catalytic domain encompassing residues 375-591, measured
CC on Drosophila melanogaster Act88F indirect flight muscle actin.;
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:16430223};
CC -!- INTERACTION:
CC P21454; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-15595598, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via the type III
CC secretion system 1 (SPI-2 TTSS). {ECO:0000305}.
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; Z15042; CAA78760.1; -; Genomic_DNA.
DR PIR; S15215; S15215.
DR PDB; 2GWL; X-ray; 1.90 A; A=392-591.
DR PDB; 2GWM; X-ray; 1.50 A; A=391-590.
DR PDBsum; 2GWL; -.
DR PDBsum; 2GWM; -.
DR AlphaFoldDB; P21454; -.
DR SMR; P21454; -.
DR DIP; DIP-29142N; -.
DR IntAct; P21454; 1.
DR EvolutionaryTrace; P21454; -.
DR PHI-base; PHI:2628; -.
DR PHI-base; PHI:5438; -.
DR PHI-base; PHI:5569; -.
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 3D-structure; Direct protein sequencing; Glycosyltransferase; NAD; NADP;
KW Nucleotide-binding; Nucleotidyltransferase; Plasmid; Secreted; Toxin;
KW Transferase; Virulence.
FT CHAIN 1..591
FT /note="Mono(ADP-ribosyl)transferase SpvB"
FT /id="PRO_0000221666"
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 BINDING 414
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16905096"
FT BINDING 471..477
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16905096"
FT BINDING 538
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16905096"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 440..459
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 545..557
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:2GWM"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:2GWM"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:2GWM"
SQ SEQUENCE 591 AA; 65441 MW; 2B933EAA4C8075E3 CRC64;
MLILNGFSSA TLALITPPFL PKGGKALSQS GPDGLASITL PLPISAERGF APALALPYSS
GGGNGPFGVG WSCATMSIAR RTSHGVPQYN DSDEFLGPDG EVLVQTLSTG DAPNPVTCFA
YGDVSFPQSY TVTRYQPRTE SSFYRLEYWV GNSNGDDFWL LHDSNGILHL LGKTAAARLS
DPQAASHTAQ WLVEESVTPA GEHIYYSYLA ENGDNVDLNG NEAGRDRSAM RYLSKVQYGN
ATPAADLYLW TSATPAVQWL FTLVFDYGER GVDPQVPPAF TAQNSWLARQ DPFSLYNYGF
EIRLLRLCRQ VLMFHHFPDE LGEADTLVSR LLLEYDENPI RTQLCAARTL AYEGDGYRRA
PVNNMMPPPP PPPMMGGNSS RPKSKWAIVE ESKQIQALRY YSAQGYSVIN KYLRGDDYPE
TQAKETLLSR DYLSTNEPSD EEFKNAMSVY INDIAEGLSS LPETDHRVVY RGLKLDKPAL
SDVLKEYTTI VNIIIDKAFM STSPDKAWIN DTILNIYLEK GHKGRILGDV AHFKGEAEML
FPPNTKLKIE SIVNCGSQDF ASQLSKLRLS DDATADTNRI KRIINMRVLN S
