TSE6_PSEAE
ID TSE6_PSEAE Reviewed; 430 AA.
AC Q9I739;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=NAD(P)(+) glycohydrolase toxin Tse6 {ECO:0000303|PubMed:26456113};
DE EC=3.2.2.5 {ECO:0000269|PubMed:26456113};
GN Name=tse6 {ECO:0000303|PubMed:26456113}; OrderedLocusNames=PA0093;
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] {ECO:0007744|PDB:4ZV0, ECO:0007744|PDB:4ZV4}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 282-430, FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH TSI6; VGRG1; EAGT6 AND EF-TU, AND MUTAGENESIS OF
RP LEU-270 AND ASP-396.
RX PubMed=26456113; DOI=10.1016/j.cell.2015.09.027;
RA Whitney J.C., Quentin D., Sawai S., LeRoux M., Harding B.N., Ledvina H.E.,
RA Tran B.Q., Robinson H., Goo Y.A., Goodlett D.R., Raunser S., Mougous J.D.;
RT "An interbacterial NAD(P)(+) glycohydrolase toxin requires elongation
RT factor Tu for delivery to target cells.";
RL Cell 163:607-619(2015).
RN [3]
RP FUNCTION, AND INTERACTION WITH EAGT6.
RX PubMed=30177742; DOI=10.1038/s41564-018-0238-z;
RA Quentin D., Ahmad S., Shanthamoorthy P., Mougous J.D., Whitney J.C.,
RA Raunser S.;
RT "Mechanism of loading and translocation of type VI secretion system
RT effector Tse6.";
RL Nat. Microbiol. 3:1142-1152(2018).
CC -!- FUNCTION: Type VI secretion exported toxin that acts as a
CC glycohydrolase on bacterial target cells and degrades the essential
CC dinucleotides NAD(+) and NADP(+), thereby inducing bacteriostasis. The
CC activity resides in the C-terminal region that is initially neutralized
CC by the cognate immunity protein Tsi6. {ECO:0000269|PubMed:26456113,
CC ECO:0000269|PubMed:30177742}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5;
CC Evidence={ECO:0000269|PubMed:26456113};
CC -!- SUBUNIT: Interacts with Tsi6, VgrG1a, EagT6 and EF-Tu.
CC {ECO:0000269|PubMed:26456113}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG03483.1; -; Genomic_DNA.
DR PIR; B83633; B83633.
DR RefSeq; NP_248783.1; NC_002516.2.
DR RefSeq; WP_003115074.1; NZ_QZGE01000015.1.
DR PDB; 4ZV0; X-ray; 1.40 A; A=282-430.
DR PDB; 4ZV4; X-ray; 3.50 A; C/D=265-430.
DR PDB; 6OX6; X-ray; 2.17 A; A=22-373.
DR PDB; 6XRF; X-ray; 2.56 A; C/F/I=1-60.
DR PDBsum; 4ZV0; -.
DR PDBsum; 4ZV4; -.
DR PDBsum; 6OX6; -.
DR PDBsum; 6XRF; -.
DR AlphaFoldDB; Q9I739; -.
DR SMR; Q9I739; -.
DR STRING; 287.DR97_3050; -.
DR PaxDb; Q9I739; -.
DR EnsemblBacteria; AAG03483; AAG03483; PA0093.
DR GeneID; 880654; -.
DR KEGG; pae:PA0093; -.
DR PATRIC; fig|208964.12.peg.97; -.
DR PseudoCAP; PA0093; -.
DR HOGENOM; CLU_037199_0_0_6; -.
DR OMA; DHDINYR; -.
DR BioCyc; PAER208964:G1FZ6-95-MON; -.
DR BRENDA; 3.2.2.5; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061810; F:NAD glycohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IDA:PseudoCAP.
DR GO; GO:0097351; F:toxin sequestering activity; IMP:PseudoCAP.
DR GO; GO:0033103; P:protein secretion by the type VI secretion system; IDA:PseudoCAP.
DR InterPro; IPR028238; Ntox46.
DR InterPro; IPR008727; PAAR_motif.
DR Pfam; PF15538; Ntox46; 1.
DR Pfam; PF05488; PAAR_motif; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..430
FT /note="NAD(P)(+) glycohydrolase toxin Tse6"
FT /id="PRO_0000449108"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 270
FT /note="L->E: Complete loss of interaction with EF-Tu."
FT /evidence="ECO:0000269|PubMed:26456113"
FT MUTAGEN 396
FT /note="D->A: Approximately 225-fold loss of NAD(P)+
FT glycohydrolase activity."
FT /evidence="ECO:0000269|PubMed:26456113"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:6XRF"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6XRF"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:6XRF"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:6XRF"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:6OX6"
FT HELIX 284..299
FT /evidence="ECO:0007829|PDB:4ZV0"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:4ZV0"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:4ZV0"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:4ZV0"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4ZV0"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:4ZV0"
SQ SEQUENCE 430 AA; 44738 MW; C722EB84BF4A77BA CRC64;
MDAQAAARLG DEIAHGFGVA AMVAGAVAGA LIGAAVVAAT AATGGLAAVI LAGSIAAGGL
SMFQIVKGLT TIFELPEPTT GVLIRGSFNV YVNSRNAMRA GDDVSATCSG LPLNHPLWPF
PVLIAEGSAT VYINGKPAAR LQSKMVCGAH IKTGSQNTFI GGPTERVAFV LDLEEWLHTG
LEALGLAALA GGLLLAAMAG VAALVGVVAI GGLMMGGMAL LGDLGDRLGP GYRDLFQGVA
GMALLGFGPK LAGRRPAAVT SETAQRRAYL NNKFGRSGNL DHDINYRGNR ETAAKFFKSK
DIDPADAESY MNGLDFNHPV RVETLAPGKN LWQYQSPGAP QGNWYTLSPR VQPTELGINP
MGTNRAANTI EPKVLNSYRT TQKVEVLRST AAPTDDFWSV KGQSYPAKGG AQQLFSNEKG
SFGLLPREGS