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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)DescriptionActionsGraphical viewLength
Metal bindingi743Magnesium 1; catalytic; for actin cross-linking activityBy similarity1
Metal bindingi743Magnesium 2; catalytic; for actin cross-linking activityBy similarity1
Metal bindingi805Magnesium 2; catalytic; for actin cross-linking activityBy similarity1
Binding sitei808ATP; via carbonyl oxygenCombined sources1
Metal bindingi889Magnesium 1; catalytic; for actin cross-linking activityBy similarity1
Binding sitei995ATP; via carbonyl oxygenBy similarity1
Metal bindingi1066Magnesium 1; catalytic; for actin cross-linking activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi739 – 743ATPCombined sources5

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
Proteomesi
  • UP000000584 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)DescriptionActionsGraphical viewLength
ChainiPRO_00004341201 – 1163Actin cross-linking toxin VgrG1Add BLAST1163

Interactioni

Protein-protein interaction databases

STRINGi243277.VC1416.

Structurei

Secondary structure

11163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi734 – 737Combined sources4
Beta strandi739 – 753Combined sources15
Beta strandi759 – 766Combined sources8
Beta strandi771 – 783Combined sources13
Helixi788 – 790Combined sources3
Beta strandi800 – 808Combined sources9
Helixi816 – 839Combined sources24
Beta strandi853 – 860Combined sources8
Beta strandi865 – 868Combined sources4
Beta strandi873 – 875Combined sources3
Beta strandi882 – 895Combined sources14
Helixi896 – 898Combined sources3
Turni899 – 901Combined sources3
Helixi905 – 911Combined sources7
Helixi920 – 927Combined sources8
Beta strandi929 – 931Combined sources3
Helixi936 – 960Combined sources25
Helixi969 – 972Combined sources4
Beta strandi978 – 980Combined sources3
Helixi984 – 990Combined sources7
Beta strandi991 – 994Combined sources4
Helixi998 – 1004Combined sources7
Helixi1007 – 1015Combined sources9
Helixi1017 – 1022Combined sources6
Helixi1027 – 1038Combined sources12
Beta strandi1043 – 1046Combined sources4
Beta strandi1052 – 1054Combined sources3
Beta strandi1056 – 1069Combined sources14
Helixi1072 – 1077Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GQKX-ray2.36A717-1111[»]
ProteinModelPortaliQ9KS45.
SMRiQ9KS45.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini728 – 1163ACDPROSITE-ProRule annotationAdd BLAST436

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi692 – 736Pro-richPROSITE-ProRule annotationAdd BLAST45

Sequence similaritiesi

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

Phylogenomic databases

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

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GQKX-ray2.36A717-1111[»]
ProteinModelPortaliQ9KS45.
SMRiQ9KS45.
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.

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...

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: November 2, 2016
This is version 73 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.