TSE2_PSEAE
ID TSE2_PSEAE Reviewed; 158 AA.
AC Q9I0E0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Toxin Tse2 {ECO:0000303|PubMed:20114026};
GN Name=tse2 {ECO:0000303|PubMed:20114026}; OrderedLocusNames=PA2702;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TSI2.
RX PubMed=20114026; DOI=10.1016/j.chom.2009.12.007;
RA Hood R.D., Singh P., Hsu F., Guevener T., Carl M.A., Trinidad R.R.,
RA Silverman J.M., Ohlson B.B., Hicks K.G., Plemel R.L., Li M., Schwarz S.,
RA Wang W.Y., Merz A.J., Goodlett D.R., Mougous J.D.;
RT "A type VI secretion system of Pseudomonas aeruginosa targets a toxin to
RT bacteria.";
RL Cell Host Microbe 7:25-37(2010).
RN [3]
RP FUNCTION, INTERACTION WITH TSI2, AND SUBUNIT.
RX PubMed=22511866; DOI=10.1371/journal.ppat.1002613;
RA Li M., Le Trong I., Carl M.A., Larson E.T., Chou S., De Leon J.A.,
RA Dove S.L., Stenkamp R.E., Mougous J.D.;
RT "Structural basis for type VI secretion effector recognition by a cognate
RT immunity protein.";
RL PLoS Pathog. 8:E1002613-E1002613(2012).
RN [4] {ECO:0007744|PDB:5AKO}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), SUBUNIT, INTERACTION WITH TSI2,
RP MUTAGENESIS OF ARG-14; SER-80 AND HIS-122, AND FUNCTION.
RX PubMed=26749446; DOI=10.1016/j.str.2015.11.012;
RA Robb C.S., Robb M., Nano F.E., Boraston A.B.;
RT "The Structure of the Toxin and Type Six Secretion System Substrate Tse2 in
RT Complex with Its Immunity Protein.";
RL Structure 24:277-284(2016).
CC -!- FUNCTION: Toxin secreted by the H1 type VI (H1-T6SS) secretion system
CC into the cytoplasm of recipient cells (PubMed:20114026). Acts likely as
CC a NAD-dependent cytotoxin towards both prokaryotic and eukaryotic cells
CC (PubMed:26749446). {ECO:0000269|PubMed:20114026,
CC ECO:0000269|PubMed:26749446}.
CC -!- SUBUNIT: Forms an heterotetramer with Tsi2 consisting of two Tse2
CC dimers and two Tsi2 dimers. Formation of the complex inactivates Tse2
CC enzymatic activity. {ECO:0000269|PubMed:20114026,
CC ECO:0000269|PubMed:22511866, ECO:0000269|PubMed:26749446}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20114026}.
CC Note=Delivered to the target cell cytoplasm by the H1 type VI (H1-T6SS)
CC secretion system. {ECO:0000269|PubMed:20114026}.
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DR EMBL; AE004091; AAG06090.1; -; Genomic_DNA.
DR PIR; B83308; B83308.
DR RefSeq; NP_251392.1; NC_002516.2.
DR RefSeq; WP_003101516.1; NZ_QZGE01000011.1.
DR PDB; 5AKO; X-ray; 2.40 A; C/D=1-158.
DR PDBsum; 5AKO; -.
DR AlphaFoldDB; Q9I0E0; -.
DR SMR; Q9I0E0; -.
DR DIP; DIP-61911N; -.
DR IntAct; Q9I0E0; 1.
DR STRING; 287.DR97_5257; -.
DR PaxDb; Q9I0E0; -.
DR PRIDE; Q9I0E0; -.
DR DNASU; 880323; -.
DR EnsemblBacteria; AAG06090; AAG06090; PA2702.
DR GeneID; 880323; -.
DR KEGG; pae:PA2702; -.
DR PATRIC; fig|208964.12.peg.2828; -.
DR PseudoCAP; PA2702; -.
DR HOGENOM; CLU_1720761_0_0_6; -.
DR OMA; ATHYTIM; -.
DR BioCyc; PAER208964:G1FZ6-2742-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR041018; ADPRTs_Tse2.
DR Pfam; PF18648; ADPRTs_Tse2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Secreted.
FT CHAIN 1..158
FT /note="Toxin Tse2"
FT /id="PRO_0000449040"
FT MUTAGEN 14
FT /note="R->A: Complete loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26749446"
FT MUTAGEN 80
FT /note="S->A: Complete loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26749446"
FT MUTAGEN 122
FT /note="H->A: Complete loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26749446"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5AKO"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5AKO"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5AKO"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5AKO"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:5AKO"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:5AKO"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:5AKO"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:5AKO"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:5AKO"
FT HELIX 133..155
FT /evidence="ECO:0007829|PDB:5AKO"
SQ SEQUENCE 158 AA; 17657 MW; 17C223D5FCF2A712 CRC64;
MSYDYEKTSL TLYRAVFKAN YDGDVGRYLH PDKELAEAAE VAPLLHPTFD SPNTPGVPAR
APDIVAGRDG LYAPDTGGTS VFDRAGVLRR ADGDFVIPDG TDIPPDLKVK QDSYNKRLQA
THYTIMPAKP MYREVLMGQL DNFVRNAIRR QWEKARGL
