ID   TSIV3_VIBCH             Reviewed;         122 AA.
AC   Q9KN41;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Antitoxin protein TsiV3 {ECO:0000303|PubMed:24348240};
DE   Flags: Precursor;
GN   Name=tsiV3 {ECO:0000303|PubMed:24348240}; OrderedLocusNames=VC_A0124;
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, AND DISRUPTION PHENOTYPE.
RX   PubMed=24348240; DOI=10.1371/journal.ppat.1003752;
RA   Miyata S.T., Unterweger D., Rudko S.P., Pukatzki S.;
RT   "Dual expression profile of type VI secretion system immunity genes
RT   protects pandemic Vibrio cholerae.";
RL   PLoS Pathog. 9:E1003752-E1003752(2013).
RN   [3] {ECO:0007744|PDB:4NOO}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 25-122, DISULFIDE BONDS,
RP   INTERACTION WITH VGRG3, AND MUTAGENESIS OF GLN-91 AND ARG-92.
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   [4] {ECO:0007744|PDB:4NSO, ECO:0007744|PDB:4NSR}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-122, AND INTERACTION WITH
RP   VGRG3.
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: Immunity protein that plays a role in preventing early
CC       activation of toxin VgrG3. {ECO:0000269|PubMed:24348240}.
CC   -!- SUBUNIT: Homodimer; dimerization is critical for inhibitory activity
CC       (PubMed:24699653). Forms a heterotetramer with VgrG3 composed of one
CC       TsiV3 homodimer and two VgrG3 molecules (PubMed:24699653).
CC       {ECO:0000269|PubMed:24699653}.
CC   -!- INTERACTION:
CC       Q9KN41; Q9KN41: tsiV3; NbExp=4; IntAct=EBI-9356338, EBI-9356338;
CC       Q9KN41; Q9KN42: vgrG3; NbExp=11; IntAct=EBI-9356338, EBI-9356343;
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is susceptible to killing by V52
CC       strain in a VgrG3-dependent manner. {ECO:0000269|PubMed:24348240}.
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DR   EMBL; AE003853; AAF96038.1; -; Genomic_DNA.
DR   PIR; G82500; G82500.
DR   RefSeq; NP_232525.1; NC_002506.1.
DR   RefSeq; WP_001061295.1; NZ_LT906615.1.
DR   PDB; 4NOO; X-ray; 2.30 A; B/D=25-122.
DR   PDB; 4NSO; X-ray; 2.40 A; B=26-122.
DR   PDB; 4NSR; X-ray; 2.79 A; A/B/C/D/E/F=26-122.
DR   PDBsum; 4NOO; -.
DR   PDBsum; 4NSO; -.
DR   PDBsum; 4NSR; -.
DR   AlphaFoldDB; Q9KN41; -.
DR   SMR; Q9KN41; -.
DR   IntAct; Q9KN41; 1.
DR   MINT; Q9KN41; -.
DR   STRING; 243277.VC_A0124; -.
DR   PRIDE; Q9KN41; -.
DR   DNASU; 2612882; -.
DR   EnsemblBacteria; AAF96038; AAF96038; VC_A0124.
DR   GeneID; 57741585; -.
DR   KEGG; vch:VC_A0124; -.
DR   PATRIC; fig|243277.26.peg.2764; -.
DR   HOGENOM; CLU_2025765_0_0_6; -.
DR   BioCyc; VCHO:VCA0124-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..122
FT                   /note="Antitoxin protein TsiV3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004328313"
FT   DISULFID        28..41
FT                   /evidence="ECO:0007744|PDB:4NOO"
FT   DISULFID        82..100
FT                   /evidence="ECO:0007744|PDB:4NOO"
FT   MUTAGEN         91
FT                   /note="Q->A: Greatly reduces VgrG3 binding affinity; when
FT                   associated with A-92."
FT                   /evidence="ECO:0000269|PubMed:24699653"
FT   MUTAGEN         92
FT                   /note="R->A: Greatly reduces VgrG3 binding affinity; when
FT                   associated with A-91."
FT                   /evidence="ECO:0000269|PubMed:24699653"
FT   HELIX           35..58
FT                   /evidence="ECO:0007829|PDB:4NOO"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:4NOO"
FT   HELIX           70..82
FT                   /evidence="ECO:0007829|PDB:4NOO"
FT   HELIX           83..87
FT                   /evidence="ECO:0007829|PDB:4NOO"
FT   HELIX           90..120
FT                   /evidence="ECO:0007829|PDB:4NOO"
SQ   SEQUENCE   122 AA;  13669 MW;  93B79A60BBBEF16F CRC64;
     MNNLLSAYVT MLLILLSISG GAIASENCND TSGVHQKILV CIQNEIAKSE TQIRNNISSK
     SIDYGFPDDF YSKQRLAIHE KCMLYINVGG QRGELLMNQC ELSMLQGLDI YIQQYIEDVD
     NS