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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}.
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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
 
 
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