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There are several matches for 'vgrG1'.
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organism
protein
Erwinia amylovora
vgrG1
- Putative type VI secretion system, effector protein vgrG COG3501: Uncharacterized protein conserved in bacteria Protein of unknown function, DUF586 Rhs element Vgr protein
Erwinia pyrifoliae
vgrG1
- Rhs element Vgr protein; silverDB:cEP00641
Pseudomonas aeruginosa
vgrG1
-
VgrG1
; vgr_GE: Rhs element Vgr family protein
Pseudomonas fluorescens Q287
vgrG1
- Type VI secretion protein
VgrG1
; Identified by similarity to GB:AAG03481.1; match to protein family HMM PF04524; match to protein family HMM TIGR01646; match to protein family HMM TIGR03361
Pseudomonas sp. UW4
vgrG1
- Type VI secretion system Vgr family protein; [S] COG3501 Uncharacterized protein conserved in bacteria
Vibrio anguillarum
vgrG1
- VgrG protein; User locus_tag: VANGcII0085; BlastN-similarity/overlapping fragments vs VgrGnuc_gi|15600771 Vibrio cholerae O1 biovar El Tor str. N16961 chrII (80-100% nt)
Vibrio cholerae O1
vgrG1
- Actin cross-linking toxin
VgrG1
; Actin-directed toxin that catalyzes the covalent cross- linking of host cytoplasmic monomeric actin. Mediates the cross- link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding. The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both pr [...]
Vibrio cholerae O395
vgrG-1 - Actin cross-linking toxin
VgrG1
; Actin-directed toxin that catalyzes the covalent cross- linking of host cytoplasmic monomeric actin. Mediates the cross- link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding. The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both pr [...]
[a.k.a. VC0395_A1026,
vgrG1
, ACP09541.1]