VGRG3_VIBCH
ID VGRG3_VIBCH Reviewed; 1017 AA.
AC Q9KN42;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Type VI secretion system spike protein VgrG3 {ECO:0000303|PubMed:23362380};
DE AltName: Full=Muramidase Vgrg3C {ECO:0000303|PubMed:24699653};
DE EC=3.2.1.- {ECO:0000269|PubMed:23362380, ECO:0000269|PubMed:24699653, ECO:0000269|PubMed:24751834};
GN Name=vgrG3 {ECO:0000303|PubMed:23362380}; OrderedLocusNames=VC_A0123;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH TSEL, MUTAGENESIS OF
RP ASP-842, AND CATALYTIC ACTIVITY.
RC STRAIN=V52;
RX PubMed=23362380; DOI=10.1073/pnas.1222783110;
RA Dong T.G., Ho B.T., Yoder-Himes D.R., Mekalanos J.J.;
RT "Identification of T6SS-dependent effector and immunity proteins by Tn-seq
RT in Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2623-2628(2013).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND INTERACTION WITH
RP TSIV3.
RC STRAIN=V52;
RX PubMed=23341465; DOI=10.1074/jbc.m112.436725;
RA Brooks T.M., Unterweger D., Bachmann V., Kostiuk B., Pukatzki S.;
RT "Lytic activity of the Vibrio cholerae type VI secretion toxin VgrG-3 is
RT inhibited by the antitoxin TsaB.";
RL J. Biol. Chem. 288:7618-7625(2013).
RN [4]
RP FUNCTION.
RX PubMed=31659021; DOI=10.1073/pnas.1914202116;
RA Liang X., Kamal F., Pei T.T., Xu P., Mekalanos J.J., Dong T.G.;
RT "An onboard checking mechanism ensures effector delivery of the type VI
RT secretion system in Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:23292-23298(2019).
RN [5] {ECO:0007744|PDB:4NOO}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 813-1017, FUNCTION, INTERACTION
RP WITH TSIV3, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-827 AND ASP-842.
RX PubMed=24699653; DOI=10.1107/s1399004714001242;
RA Yang X., Xu M., Wang Y., Xia P., Wang S., Ye B., Tong L., Jiang T., Fan Z.;
RT "Molecular mechanism for self-protection against the type VI secretion
RT system in Vibrio cholerae.";
RL Acta Crystallogr. D 70:1094-1103(2014).
RN [6] {ECO:0007744|PDB:4NSO}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 731-1009, AND INTERACTION WITH
RP TSIV3.
RX PubMed=24751834; DOI=10.1016/j.febslet.2014.04.016;
RA Zhang J., Zhang H., Gao Z., Hu H., Dong C., Dong Y.H.;
RT "Structural basis for recognition of the type VI spike protein VgrG3 by a
RT cognate immunity protein.";
RL FEBS Lett. 588:1891-1898(2014).
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 (PubMed:23362380,
CC PubMed:23341465). Forms the spike at the tip of the elongating tube
CC formed by haemolysin co-regulated protein Hcp. Allows the delivery of
CC the TseL antibacterial toxin to target cells where it exerts its
CC toxicity (PubMed:23362380). Additionally, acts directly as an effector
CC and targets the cell wall peptidoglycan layer of prey cells for
CC degradation via its C-terminus (PubMed:23362380, PubMed:23341465).
CC Toxicity is counteracted by a cognate immunity protein TsiV3
CC (PubMed:23362380, PubMed:24699653, PubMed:23341465).
CC {ECO:0000269|PubMed:23341465, ECO:0000269|PubMed:23362380,
CC ECO:0000269|PubMed:24699653}.
CC -!- SUBUNIT: Interacts with TsiV3 (PubMed:24751834, PubMed:24699653,
CC PubMed:23341465). Interacts with TseL (PubMed:23362380).
CC {ECO:0000269|PubMed:23341465, ECO:0000269|PubMed:23362380,
CC ECO:0000269|PubMed:24699653, ECO:0000269|PubMed:24751834}.
CC -!- INTERACTION:
CC Q9KN42; Q9KN41: tsiV3; NbExp=11; IntAct=EBI-9356343, EBI-9356338;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23341465}.
CC -!- DISRUPTION PHENOTYPE: Mutants are unable to secrete TseL.
CC {ECO:0000269|PubMed:23362380}.
CC -!- SIMILARITY: Belongs to the VgrG protein family. {ECO:0000305}.
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DR EMBL; AE003853; AAF96037.1; -; Genomic_DNA.
DR PIR; F82500; F82500.
DR RefSeq; NP_232524.1; NC_002506.1.
DR RefSeq; WP_000113295.1; NZ_LT906615.1.
DR PDB; 4NOO; X-ray; 2.30 A; A/C=813-1017.
DR PDB; 4NSO; X-ray; 2.40 A; A=731-1009.
DR PDBsum; 4NOO; -.
DR PDBsum; 4NSO; -.
DR AlphaFoldDB; Q9KN42; -.
DR SMR; Q9KN42; -.
DR IntAct; Q9KN42; 1.
DR MINT; Q9KN42; -.
DR STRING; 243277.VC_A0123; -.
DR PRIDE; Q9KN42; -.
DR DNASU; 2612828; -.
DR EnsemblBacteria; AAF96037; AAF96037; VC_A0123.
DR GeneID; 57741584; -.
DR KEGG; vch:VC_A0123; -.
DR PATRIC; fig|243277.26.peg.2763; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG3501; Bacteria.
DR HOGENOM; CLU_004121_0_1_6; -.
DR OMA; VWTHRYE; -.
DR BioCyc; VCHO:VCA0123-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.101.10; -; 1.
DR Gene3D; 2.40.50.230; -; 1.
DR InterPro; IPR006531; Gp5/Vgr_OB.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR017847; T6SS_RhsGE_Vgr_subset.
DR InterPro; IPR006533; T6SS_Vgr_RhsGE.
DR InterPro; IPR037026; Vgr_OB-fold_dom_sf.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF04717; Phage_base_V; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR TIGRFAMs; TIGR01646; vgr_GE; 1.
DR TIGRFAMs; TIGR03361; VI_Rhs_Vgr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Secreted.
FT CHAIN 1..1017
FT /note="Type VI secretion system spike protein VgrG3"
FT /id="PRO_0000448967"
FT ACT_SITE 842
FT /evidence="ECO:0000269|PubMed:23362380"
FT MUTAGEN 827
FT /note="E->Q: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24699653"
FT MUTAGEN 842
FT /note="D->N: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:23362380,
FT ECO:0000269|PubMed:24699653"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 824..827
FT /evidence="ECO:0007829|PDB:4NOO"
FT TURN 828..830
FT /evidence="ECO:0007829|PDB:4NOO"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:4NOO"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:4NOO"
FT TURN 849..852
FT /evidence="ECO:0007829|PDB:4NOO"
FT TURN 855..858
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 859..866
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 870..873
FT /evidence="ECO:0007829|PDB:4NOO"
FT STRAND 878..880
FT /evidence="ECO:0007829|PDB:4NSO"
FT HELIX 881..893
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 895..909
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 911..919
FT /evidence="ECO:0007829|PDB:4NOO"
FT TURN 920..922
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 930..943
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 949..953
FT /evidence="ECO:0007829|PDB:4NOO"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:4NOO"
FT STRAND 959..961
FT /evidence="ECO:0007829|PDB:4NSO"
FT HELIX 964..977
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 979..982
FT /evidence="ECO:0007829|PDB:4NOO"
FT TURN 983..985
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 987..989
FT /evidence="ECO:0007829|PDB:4NOO"
FT HELIX 990..1009
FT /evidence="ECO:0007829|PDB:4NOO"
SQ SEQUENCE 1017 AA; 112995 MW; ECFF8C66E0214FE4 CRC64;
MARLQFQLKV DGLEDESLVV RGFEGQESLS DSVWRCEPCY GFRYQVDLAS ALSNLTAEQF
VDQTAHLTIL RDGQVVQQIN GIVRQLSKGD TGHRHTFYSL TLVPALERLS LRSNSRIFQQ
QSVPEIISIL LQEMGIEDYA FALKRECAQR EFCVQYRETD LQFLHRIAAE EGLVYSHLHE
AQKHTLLFTD SSDSQPKLAK PVPYNALAGG EINLPYVVDL QFKTTAQVSH TELKDYSFKK
PAYGFTQRTQ GKDIAYQQPN YEHFDAPGRY KDDANGKAFS QIRLEYLRRD ALLADAKSDE
PLLLAGVRFD LQDHLDHAMN RDWLVVQANH QGTQPQALQE EGGSGATTYS NQLKLIPAHI
TWRARPCAKP QVDGPMIATV VGPQGEEIYC DNFGRVKVHF PWDRYSSSNE KSSCWVRVAQ
EWAGSQYGSM AIPRVGHEVI VSFLNGDPDQ PIITGRTYHA TNTAPYALPD HKTKTVLRTE
THQGQGYNEL SFEDQAGSEQ ILLHAQKDWD ALIEHDHTEV IRHDQHLTVD NDRFTRIQRN
QHLTVEGEVR SKIALDSSHE VGASLQHKVG QRIAVEAGKE ISLKSGAKIV VEAGAELTLK
AGGSFVKVDA GGVHLVGPAI NLNAGGSAGS GSAYGGQLAA APRMLAQAKP VAELVQPDIA
ASMQSGAARV IDVASLPTMM PSSANNTAND EPVAEEKTPE RILKSDLLKP SDELEKLAKR
QASAYRQGNH SDEVKLLQEA LIKLGFDLGK AGADGDFGSK TKTAIEQFQK SYQPSHQTHP
SYSIGAVDGI VGKGTLLALD EALMDGWVYE NNIYQIWPLG KTSEKYESAG RGPGVISTGN
GDYGGASYGC YQMSSNLGVV QKYIQSSKFK EFFSGLNPAT KEFNVVWQDI ASRYPQEFRE
EQHQFIKRTH YDIQIGHLRG KGLLFEHNRA AVHDLIWSTS VQFGGRTNLI FNALNGQNME
SMTDKDIIIL VQDYKLVNTE RLFKSSPSWW SDLKKRAVSE KKALLELEID GLEVDIK
