VGRG1_AERHY
ID VGRG1_AERHY Reviewed; 681 AA.
AC K7WKL8;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Type VI secretion system spike protein VgrG1 {ECO:0000303|PubMed:19880608};
DE AltName: Full=Actin ADP-ribosyltransferase {ECO:0000303|PubMed:19880608};
DE EC=2.4.2.31 {ECO:0000269|PubMed:19880608};
GN Name=vgrG1;
OS Aeromonas hydrophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=644;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SSU;
RX PubMed=23519162; DOI=10.1099/mic.0.063495-0;
RA Sha J., Rosenzweig J.A., Kozlova E.V., Wang S., Erova T.E., Kirtley M.L.,
RA van Lier C.J., Chopra A.K.;
RT "Evaluation of the roles played by Hcp and VgrG type 6 secretion system
RT effectors in Aeromonas hydrophila SSU pathogenesis.";
RL Microbiology 159:1120-1135(2013).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=19880608; DOI=10.1128/jb.01260-09;
RA Suarez G., Sierra J.C., Erova T.E., Sha J., Horneman A.J., Chopra A.K.;
RT "A type VI secretion system effector protein, VgrG1, from Aeromonas
RT hydrophila that induces host cell toxicity by ADP ribosylation of actin.";
RL J. Bacteriol. 192:155-168(2010).
CC -!- FUNCTION: Part of the type VI secretion system specialized secretion
CC system, which delivers several virulence factors in both prokaryotic
CC and eukaryotic cells during infection. Acts directly as an secreted
CC effector with an actin ADP-ribosyltransferase activity that disrupts
CC the host actin cytoskeleton, leading to a decrease in host cell
CC viability and an increase in apoptosis. {ECO:0000269|PubMed:19880608}.
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 Evidence={ECO:0000269|PubMed:19880608};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19880608}.
CC -!- SIMILARITY: Belongs to the VgrG protein family. {ECO:0000305}.
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DR EMBL; JX646703; AFX59895.1; -; Genomic_DNA.
DR AlphaFoldDB; K7WKL8; -.
DR SMR; K7WKL8; -.
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 Gene3D; 2.40.50.230; -; 1.
DR InterPro; IPR006531; Gp5/Vgr_OB.
DR InterPro; IPR017847; T6SS_RhsGE_Vgr_subset.
DR InterPro; IPR006533; T6SS_Vgr_RhsGE.
DR InterPro; IPR037026; Vgr_OB-fold_dom_sf.
DR Pfam; PF04717; Phage_base_V; 1.
DR TIGRFAMs; TIGR01646; vgr_GE; 1.
DR TIGRFAMs; TIGR03361; VI_Rhs_Vgr; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Nucleotidyltransferase; Secreted; Transferase.
FT CHAIN 1..681
FT /note="Type VI secretion system spike protein VgrG1"
FT /id="PRO_0000448968"
FT REGION 621..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 75614 MW; 6DA37BCA1F88451F CRC64;
MADSTGLQFT VKVGALPENT FVVAEFALDE ALNRPFNLRL ELASAQPDID FGAVLDQPCE
LLVWYNGELQ RRVCGVVSDF AQGDSGFRRT RYQLRVLPAL WRLSLRQNSR IFQAQKPDEI
LSILLQEHGI TDYAFALKNE HAKREYCVQY RESDLDFVNR LAAEEGMFYF HEFEAGKHRI
VFADDAAALT QGPELFFNLG NRSLEQGPYV RQFHYREAVR PSDVELKDYS FKTPAYGLSH
KKVGAELTHQ RDTYQHFDFP GRYKEDPSGK AFAQHRLDAL RNDAVAGQAK SNCAALLPGQ
SFSLTEHPNG SLNTDWQIVR IQHTGLQPQA LEEEGGSGPT VYHNEFGVVK ASTTWRARIG
SPEAPHKPMV DGPQIAIVVG PDGEEIYCDE HGRVKLQFPW DRYGSSNDQS SCWVRVSQGW
AGGQYGMMAI PRIGHEVIVS FLEGDPDQPI VTGRTYHATN RPPYELPANK TRTVLRTETH
QGEGFNELRF EDQVGQEEIY IHGQKDLNVL IENDAAWHIK HDEHTDVDNE RVTRIKANDH
LTVEGEKRDQ IKADYSLTVD TSMHQKLGDS WLTQAGQEVH VKAGAKVVLE AGSEITVKVG
GCFIKVDGGG VTLVGPTIKM NSGGSPSSGS GWGGKSPVDP LGVSVPPKPK VPLTPAQLAT
MKSAAPFCEE CEKCKEGGCE I