TRE1_SERP5
ID TRE1_SERP5 Reviewed; 444 AA.
AC A8GG78;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=NAD(+)--protein-arginine ADP-ribosyltransferase Tre1 {ECO:0000305};
DE EC=2.4.2.31 {ECO:0000269|PubMed:30343895};
DE AltName: Full=Effector protein Tre1 {ECO:0000303|PubMed:30343895};
DE Short=Tre1-Sp {ECO:0000303|PubMed:30343895};
DE AltName: Full=Type VI secretion ADP-ribosyltransferase effector 1 {ECO:0000303|PubMed:30343895};
GN Name=tre1 {ECO:0000303|PubMed:30343895}; OrderedLocusNames=Spro_3017;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6DRE, ECO:0007744|PDB:6DRH}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 273-442 IN COMPLEX WITH TRI1,
RP FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-415.
RC STRAIN=568;
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, RL9, SucB, and LolD.
CC FtsZ is thought to be the physiologically relevant target as it is ADP-
CC ribosylated on a critical residue. ADP-ribosylation of FtsZ prevents
CC formation of the FtsZ mid-cell ring and inhibits cell division.
CC Overexpression of the whole Tre1 protein or the ART domain in E.coli is
CC toxic; cells elongate dramatically and some undergo lysis. Toxic
CC activity is neutralized by coexpression of the cognate immunity protein
CC Tri1-Sp; Tri1-Sp neutralizes this protein both by binding to and
CC occluding the active site (via Tri1's N-terminal extension) and by
CC hydrolysis of the ADP-ribosyl moiety from the target protein. Tre1 can
CC also be neutralized by non-cognate immunity protein Tri1-Pp from
CC P.putida strain GB-1, with which it does not form a stable complex;
CC DraG of R.palustris does not neutralize the toxic effects of this
CC protein. In interbacterial competition studies Tri1 from P.putida
CC strain B6-2 also neutralizes this protein.
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:0000269|PubMed:30343895};
CC -!- SUBUNIT: Forms a stable complex with cognate immunity protein Tri1-Sp.
CC {ECO:0000269|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:0000305|PubMed:30343895}.
CC -!- DOMAIN: The ART domain is toxic when expressed as a protein fragment.
CC {ECO:0000269|PubMed:30343895}.
CC -!- DISRUPTION PHENOTYPE: A double tre1-tri1 deletion is outcompeted by
CC wild-type cells, but not by wild-type cells missing a type 6 secretion
CC system (T6SS). {ECO:0000269|PubMed:30343895}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CP000826; ABV42118.1; -; Genomic_DNA.
DR RefSeq; WP_012145739.1; NC_009832.1.
DR PDB; 6DRE; X-ray; 1.80 A; B=273-442.
DR PDB; 6DRH; X-ray; 2.30 A; B/D/F/H=273-441.
DR PDBsum; 6DRE; -.
DR PDBsum; 6DRH; -.
DR AlphaFoldDB; A8GG78; -.
DR SMR; A8GG78; -.
DR STRING; 399741.Spro_3017; -.
DR EnsemblBacteria; ABV42118; ABV42118; Spro_3017.
DR KEGG; spe:Spro_3017; -.
DR eggNOG; COG4104; Bacteria.
DR HOGENOM; CLU_616409_0_0_6; -.
DR OrthoDB; 776615at2; -.
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 InterPro; IPR008727; PAAR_motif.
DR Pfam; PF01129; ART; 1.
DR Pfam; PF05488; PAAR_motif; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Host cytoplasm; Nucleotidyltransferase;
KW Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..444
FT /note="NAD(+)--protein-arginine ADP-ribosyltransferase
FT Tre1"
FT /id="PRO_0000446515"
FT DOMAIN 266..444
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT REGION 72..140
FT /note="PAAR domain"
FT /evidence="ECO:0000305|PubMed:30343895"
FT REGION 274..444
FT /note="ART domain"
FT /evidence="ECO:0000305|PubMed:30343895"
FT ACT_SITE 356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340,
FT ECO:0000305|PubMed:30343895"
FT ACT_SITE 381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340,
FT ECO:0000305|PubMed:30343895"
FT ACT_SITE 415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340,
FT ECO:0000305|PubMed:30343895"
FT MUTAGEN 415
FT /note="E->Q: Cells are impaired in interbacterial
FT competetion, no ADP-ribosylation of proteins in target
FT cells, the ART domain is no longer toxic when expressed in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:30343895"
FT HELIX 276..296
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 331..346
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 389..400
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:6DRE"
SQ SEQUENCE 444 AA; 45824 MW; 7585645E3EA2DD9B CRC64;
MSELSAAREL DEIAHTASEG WMIAGLIGGA IVGAALIAVT GGTAAVAVAA VVAGASAGGG
LGEVLGSMSW APRHVTGVLA DGSPNVYING RPAIRAHIST GECSEDGPAK KVVAQGSAKV
YINDFPAARI NDLLACSAEI HTGSPNVIIG GEKEQTDDIE PEIPDWVNWT LLAAGAGAAA
VLATPAIAIL GTLGGLGGGF AGSLIGGAFF GEGSDGQKWS MLAGGFVGGF AGGKGGAKFD
AWRNTKIVEP PPRVTTKVDP ISPPRMTLAE AVGQEQAKVW TQTARANAEK NNAQLSTLLT
DDQIGAIYGY TTNEGYTALN PALRGQTPLT PELEAFTGHV TDGLNKLPAY NGETYRGTTL
PAHILEQNQI GGTVSDGGFM STSAKTPFDG DVSISVRGNS GKQIDFLSKY KNEAEVLYPP
NTRFEVINRI EQNGTTHLLY REIP
