ID   TRE1_PSEPG              Reviewed;         495 AA.
AC   B0KTG9;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=NAD(+)--protein-arginine ADP-ribosyltransferase Tre1 {ECO:0000305};
DE            EC=2.4.2.31 {ECO:0000305|PubMed:30343895};
DE   AltName: Full=Effector protein Tre1 {ECO:0000303|PubMed:30343895};
DE            Short=Tre1-Pp {ECO:0000303|PubMed:30343895};
DE   AltName: Full=NAD(+)--protein-arginine ADP-ribosyltransferase {ECO:0000305};
GN   Name=tre1 {ECO:0000303|PubMed:30343895}; OrderedLocusNames=PputGB1_2762;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=GB-1;
RX   PubMed=30343895; DOI=10.1016/j.cell.2018.09.037;
RA   Ting S.Y., Bosch D.E., Mangiameli S.M., Radey M.C., Huang S., Park Y.J.,
RA   Kelly K.A., Filip S.K., Goo Y.A., Eng J.K., Allaire M., Veesler D.,
RA   Wiggins P.A., Peterson S.B., Mougous J.D.;
RT   "Bifunctional immunity proteins protect bacteria against FtsZ-targeting
RT   ADP-ribosylating toxins.";
RL   Cell 175:1380-1392(2018).
CC   -!- FUNCTION: Toxic component of a contact-dependent interbacterial
CC       competition system (also called effector-immunity systems). Acts by
CC       ADP-ribosylating a number of target proteins in target cells; E.coli
CC       target proteins include FtsZ, EFTu, RNase E, Fis, YegQ, GuaB and IF2.
CC       {ECO:0000269|PubMed:30343895}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC         ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:142554; EC=2.4.2.31;
CC         Evidence={ECO:0000305|PubMed:30343895};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cytoplasm
CC       {ECO:0000305}. Note=Probably delivered to target cells by a type 6
CC       secretion system (T6SS). {ECO:0000250|UniProtKB:A8GG78}.
CC   -!- DOMAIN: The ART domain is toxic when expressed as a protein fragment.
CC       {ECO:0000269|PubMed:30343895}.
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000926; ABY98656.1; -; Genomic_DNA.
DR   RefSeq; WP_012272395.1; NC_010322.1.
DR   AlphaFoldDB; B0KTG9; -.
DR   SMR; B0KTG9; -.
DR   STRING; 76869.PputGB1_2762; -.
DR   EnsemblBacteria; ABY98656; ABY98656; PputGB1_2762.
DR   KEGG; ppg:PputGB1_2762; -.
DR   eggNOG; COG2369; Bacteria.
DR   HOGENOM; CLU_550787_0_0_6; -.
DR   OMA; GGHRIDN; -.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR000768; ART.
DR   Pfam; PF01129; ART; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Host cytoplasm; Nucleotidyltransferase; Secreted;
KW   Toxin; Transferase; Virulence.
FT   CHAIN           1..495
FT                   /note="NAD(+)--protein-arginine ADP-ribosyltransferase
FT                   Tre1"
FT                   /id="PRO_0000446516"
FT   DOMAIN          315..495
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   REGION          278..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..495
FT                   /note="ART domain"
FT                   /evidence="ECO:0000305|PubMed:30343895"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
SQ   SEQUENCE   495 AA;  52676 MW;  D02EC9BD96E78037 CRC64;
     MDLLANVPSW SDIERSLDQK FSAVNQSIHQ GLQSANDSWH GFSRRVSDGA GQAYGYLGGH
     RIDNVQQALA MSYPIFQEDL KRKWASIGIE QILPVLLQLV KEVSMILGGS IAVGSAAGGA
     IGALAFGVGA APGAVAGAGI GLEVGNLILL ALGLSAIAEY FIKGLPVCLA TLQEGIATAW
     NAEEGVKPAG LDPTGGSVAV IQERTERAAR QLARGQEQLV LLLLMAIVTY LLRGQMKAGI
     MGSMENIATR SAKLQADIAN KQFGAWLAKN EAKLLAHPDL QIKGPTPVKK PEPLQPARQP
     EKASAPKPVA KPAVMSLREA VGNQTADRWI STGRRIADFT DPKRSALLTD DQIGALHGYT
     TNEGYQWINP ALRGQTPLSP QMEAFVTHAN EGLAKLPSYT LGDTFRGTTL PEDVMSRMQV
     GLPTSDAAFL STSADRALAF NGNVKMTLQG VTGKDISFLS GHREAEVLFG PGTRFNVVDR
     VDNGSVTQFI LKEIP