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Protein

Actin cross-linking toxin VgrG1

Gene

vgrG1

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (PubMed:17873062, PubMed:20150509). 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 profilin-dependent and independent manners (By similarity). Acts as an acid--amino-acid ligase that transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin residue, resulting in the formation of an activated acyl phosphate intermediate. This intermediate is further hydrolyzed and the energy of hydrolysis is utilized for the formation of the amide bond between actin subunits (By similarity).By similarity2 Publications

Cofactori

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit. Can also use Mn2+ ions instead of Mg2+.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi743 – 7431Magnesium 1; catalytic; for actin cross-linking activityBy similarity
Metal bindingi743 – 7431Magnesium 2; catalytic; for actin cross-linking activityBy similarity
Metal bindingi805 – 8051Magnesium 2; catalytic; for actin cross-linking activityBy similarity
Binding sitei808 – 8081ATP; via carbonyl oxygenCombined sources
Metal bindingi889 – 8891Magnesium 1; catalytic; for actin cross-linking activityBy similarity
Binding sitei995 – 9951ATP; via carbonyl oxygenBy similarity
Metal bindingi1066 – 10661Magnesium 1; catalytic; for actin cross-linking activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi739 – 7435ATPCombined sources

GO - Molecular functioni

GO - Biological processi

  • actin filament depolymerization Source: UniProtKB
  • actin filament reorganization Source: InterPro
  • isopeptide cross-linking Source: UniProtKB
  • isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Source: UniProtKB
  • pathogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciVCHO:VC1416-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin cross-linking toxin VgrG1 (EC:6.3.2.-By similarity)
Gene namesi
Name:vgrG11 Publication
Synonyms:vgrG-11 Publication
Ordered Locus Names:VC_1416Imported
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • host cell cytoplasm Source: UniProtKB
  • host cell cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11631163Actin cross-linking toxin VgrG1PRO_0000434120Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243277.VC1416.

Structurei

Secondary structure

1
1163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi734 – 7374Combined sources
Beta strandi739 – 75315Combined sources
Beta strandi759 – 7668Combined sources
Beta strandi771 – 78313Combined sources
Helixi788 – 7903Combined sources
Beta strandi800 – 8089Combined sources
Helixi816 – 83924Combined sources
Beta strandi853 – 8608Combined sources
Beta strandi865 – 8684Combined sources
Beta strandi873 – 8753Combined sources
Beta strandi882 – 89514Combined sources
Helixi896 – 8983Combined sources
Turni899 – 9013Combined sources
Helixi905 – 9117Combined sources
Helixi920 – 9278Combined sources
Beta strandi929 – 9313Combined sources
Helixi936 – 96025Combined sources
Helixi969 – 9724Combined sources
Beta strandi978 – 9803Combined sources
Helixi984 – 9907Combined sources
Beta strandi991 – 9944Combined sources
Helixi998 – 10047Combined sources
Helixi1007 – 10159Combined sources
Helixi1017 – 10226Combined sources
Helixi1027 – 103812Combined sources
Beta strandi1043 – 10464Combined sources
Beta strandi1052 – 10543Combined sources
Beta strandi1056 – 106914Combined sources
Helixi1072 – 10776Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQKX-ray2.36A717-1111[»]
ProteinModelPortaliQ9KS45.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini728 – 1163436ACDPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi692 – 73645Pro-richPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACD (actin cross-linking) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CS6. Bacteria.
COG3501. LUCA.
KOiK11904.
OMAiLIENDQF.
OrthoDBiEOG69SK6H.

Family and domain databases

Gene3Di2.40.50.230. 1 hit.
InterProiIPR032074. ACD_dom.
IPR006531. Gp5_N-like_dom.
IPR017847. T6SS_RhsGE_Vgr_subset.
IPR006533. T6SS_Vgr_RhsGE.
[Graphical view]
PfamiPF16671. ACD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01646. vgr_GE. 1 hit.
TIGR03361. VI_Rhs_Vgr. 1 hit.
PROSITEiPS51772. ACD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KS45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLAYSIEV EGLEDETLVV RGFHGQESLS NSVFLGQACY GFRYEVQLAS
60 70 80 90 100
RVSNLTAEQM VDKRAELKLY RNSQLVQRVH GIVRAFSQGD IGHHHTFYQL
110 120 130 140 150
TLVPALERLS LRHNSRIFQK QTVPEILSIL LQEMGINDYA FALKRDGVQR
160 170 180 190 200
EFCVQYRESD IDFLHRLAAE EGLVYSFVHE AGKHTLYFSD ASDSLSKLPE
210 220 230 240 250
PIPYNALVGG AIDTPYIHGL TYRTQAEVSE VQLKDYSFKK PAYSFLQTVQ
260 270 280 290 300
GTELDYQQTR YQHFDAPGRY KDDVNGAAFS QIRLDYLRRH AHTATGQSNE
310 320 330 340 350
PLLRAGYKFD LQEHLDPAMN RDWVVVSINH QGEQPQALQE DGGSGATTYS
360 370 380 390 400
NQFSLIPGHL HWRAEPQPKP QVDGPMIATV VGPEGEEIFC DEHGRVKIHF
410 420 430 440 450
PWDRYSNGNE QSSCWVRVSQ GWAGSQYGFI AIPRIGHEVI VEFLNGDPDQ
460 470 480 490 500
PIITGRTYHA TNTPPYTLPE HKTKTVLRTE THQGEGFNEL SFEDQAGKEQ
510 520 530 540 550
IYLHAQKDFD GLIENDHTTV IRHDHHLTVE NDQFTQIKHN QHLTVEWESR
560 570 580 590 600
EAVTGEQVLS IEGSLHVKTG KVWVNEAGTE IHVKAGQKVV IEAGSEITVK
610 620 630 640 650
AGGSFVKVDP AGVHLSGALV NLNSGGSAGS GSGFGGAMPA LPGGLEPAVA
660 670 680 690 700
LAPPQTISYQ ALLQAEQANV PAVKVCPLAA QEATPAVNSI TPPPPPPIAP
710 720 730 740 750
PMAPPQPIMN PQPTANAQPN LGRSTKATPD FPTHFPKSSI GIENELAGLV
760 770 780 790 800
VAMPANSAQK FGYVKSAQGD ALFMLTKDMN QGSYQRPPSL QDGKNYQNWQ
810 820 830 840 850
THTVELVSYP CEMDDKAAVE TRKQAMLWLA THFTTHIDQS NHQPLAPIQS
860 870 880 890 900
EDGRFVIEIT NAKHVIAAGN GISAESQGQT ITMTPSGQQA TVGVAAKGFG
910 920 930 940 950
TSATPELRLL ESAPWYQKSL KSQFASLTSA ENLDDKELAA NVFAYLTSIY
960 970 980 990 1000
LKTAELAKKF GIYINEWDPM SEQITPNANG LTDPKVKNAW EILPRTKPSK
1010 1020 1030 1040 1050
IVEILSKSDA KAVMKHIKPQ LQSRYSESLS KNVFQYFQDG GEVAGHGINN
1060 1070 1080 1090 1100
ATVGDKHSPE LAILFEFRTV PNELQSYLPK TESTTKSEVK LLDQFDPMKR
1110 1120 1130 1140 1150
KTVIQQVESL VQNSGDAFDK WYQSYRDSMN QPPVKNAKKI ASANQKAQWV
1160
KEHNPQEWQR IIA
Length:1,163
Mass (Da):128,829
Last modified:October 1, 2000 - v1
Checksum:iFF95DFEC31FE9F15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94573.1.
PIRiD82202.
RefSeqiNP_231059.1. NC_002505.1.
WP_000212116.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF94573; AAF94573; VC_1416.
GeneIDi2614048.
KEGGivch:VC1416.
PATRICi20081892. VBIVibCho83274_1345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94573.1.
PIRiD82202.
RefSeqiNP_231059.1. NC_002505.1.
WP_000212116.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQKX-ray2.36A717-1111[»]
ProteinModelPortaliQ9KS45.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1416.

Protocols and materials databases

DNASUi2614048.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF94573; AAF94573; VC_1416.
GeneIDi2614048.
KEGGivch:VC1416.
PATRICi20081892. VBIVibCho83274_1345.

Phylogenomic databases

eggNOGiENOG4105CS6. Bacteria.
COG3501. LUCA.
KOiK11904.
OMAiLIENDQF.
OrthoDBiEOG69SK6H.

Enzyme and pathway databases

BioCyciVCHO:VC1416-MONOMER.

Family and domain databases

Gene3Di2.40.50.230. 1 hit.
InterProiIPR032074. ACD_dom.
IPR006531. Gp5_N-like_dom.
IPR017847. T6SS_RhsGE_Vgr_subset.
IPR006533. T6SS_Vgr_RhsGE.
[Graphical view]
PfamiPF16671. ACD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01646. vgr_GE. 1 hit.
TIGR03361. VI_Rhs_Vgr. 1 hit.
PROSITEiPS51772. ACD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.
  2. "Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin."
    Pukatzki S., Ma A.T., Revel A.T., Sturtevant D., Mekalanos J.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:15508-15513(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  3. "In vivo actin cross-linking induced by Vibrio cholerae type VI secretion system is associated with intestinal inflammation."
    Ma A.T., Mekalanos J.J.
    Proc. Natl. Acad. Sci. U.S.A. 107:4365-4370(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Structure of Native VgrG1-ACD with ADP (no cations)."
    Nguyen V.S., Spinelli S., Derrez E., Durand E., Cambillau C.
    Submitted (AUG-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 717-1111 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiVGRG1_VIBCH
AccessioniPrimary (citable) accession number: Q9KS45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: October 1, 2000
Last modified: January 20, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.