ID   VGRG1_AERHH             Reviewed;         743 AA.
AC   A0KJB0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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; OrderedLocusNames=AHA_1827;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39429.1; -; Genomic_DNA.
DR   RefSeq; WP_011705707.1; NC_008570.1.
DR   RefSeq; YP_856361.1; NC_008570.1.
DR   AlphaFoldDB; A0KJB0; -.
DR   SMR; A0KJB0; -.
DR   STRING; 380703.AHA_1827; -.
DR   EnsemblBacteria; ABK39429; ABK39429; AHA_1827.
DR   KEGG; aha:AHA_1827; -.
DR   PATRIC; fig|380703.7.peg.1842; -.
DR   eggNOG; COG3501; Bacteria.
DR   HOGENOM; CLU_004121_8_2_6; -.
DR   OMA; HSHRTIG; -.
DR   Proteomes; UP000000756; Chromosome.
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; Reference proteome; Secreted;
KW   Transferase.
FT   CHAIN           1..743
FT                   /note="Type VI secretion system spike protein VgrG1"
FT                   /id="PRO_0000448969"
SQ   SEQUENCE   743 AA;  82412 MW;  F8AE17B09C77B08D CRC64;
     MADSTGLQFT VKVGALPEST FVVAEFALDE ALNRPFNLRL ELASAQPDID FGAVLDQPCE
     LLVWYNGELQ RRVCGVVSDF AQGDSGFRRT RYQLMVQPAL WRLSLRQNCR IFQAQKPDEI
     LSILLQEHGI TDYAFALKNE HAKREYCVQY RETDLDFVNR LAAEEGMFYF HEFEAGKHRI
     VFADDAAALT AGPELFFNLG NRSLEQGPYV RQFHYREAVR PSDVELKDYS CKTPAYGLSH
     KKQGSELEHQ RDTYQHFDYP GRYKQDPSGK AFAQHRLDAL RNDAVAGQVK SNCAALLPGQ
     TFSLTEHPNG SLNTDWQIVR IRHTGEQPQA LEEEGGSGPT VYHNEFGVVK ASTTWRARIG
     SPEAPHKPMV DGPQIAMVVG PDGEEIYCDE HGRVKLQFPW DRYGSSNDQS SCWVRVSQGW
     AGGQYGMMAI PRIGHEVIVS FLEGDPDQPI VTGRTYHATN RPPYELPANK TRTVLRTETH
     QGEGFNELRF EDQAGQEEIY IHGQKDLNVL IENDAAWHIK HDQHTDIDNE RVTRVRKVPG
     EEGAPPSLGN DHLTVEGEKR DHIKADYSLT VDTSMHQKLG QSWLTQAGQE VHVKAGAKVV
     LEAGSEITVK VGGCFIKVDG GGVTLVGPTI KMNSGGNAGS GSGWAGKVPK SMEGMLDSPH
     TRWMKFYHLD SELMPLAGTP YKAVLSDGSV REGTLDGEGM ALLEDVPAGT ASVTYDLQDT
     FADLPRESIS ALTGHLDSLS DEG