TRI1_SERP5
ID TRI1_SERP5 Reviewed; 366 AA.
AC A8GG79;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ADP-ribosylarginine hydrolase Tri1 {ECO:0000305};
DE EC=3.2.2.19 {ECO:0000305|PubMed:30343895};
DE AltName: Full=Immunity protein Tri1 {ECO:0000303|PubMed:30343895};
DE Short=Tri1-Sp {ECO:0000303|PubMed:30343895};
GN Name=tri1 {ECO:0000303|PubMed:30343895}; OrderedLocusNames=Spro_3018;
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) IN COMPLEX WITH TRE1 AND MG(2+),
RP FUNCTION, COFACTOR, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF ARG-32 AND ASP-161.
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: Immunity component of a contact-dependent interbacterial
CC competition system (also called effector-immunity systems). Acts as an
CC arginine mono-ADP-ribosylhydrolase, mediating the removal of mono-ADP-
CC ribose attached to arginine residues on proteins. De-ADP-ribosylates
CC FtsZ, is able to act on other proteins as well. Neutralizes the toxic
CC activity of cognate toxin Tre1-Sp. Expression of this protein alone in
CC E.coli partially protects the cells against competition by wild-type
CC S.proteamaculans. Neutralizes Tre1-Sp both by occluding its active site
CC via its N-terminal extension and by hydrolyzing the ADP-ribosyl moiety
CC from FtsZ; the 2 activities are dissociable by mutagenesis.
CC {ECO:0000269|PubMed:30343895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-
CC ribose + L-arginyl-[protein]; Xref=Rhea:RHEA:14885, Rhea:RHEA-
CC COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29965, ChEBI:CHEBI:57967, ChEBI:CHEBI:142554;
CC EC=3.2.2.19; Evidence={ECO:0000305|PubMed:30343895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30343895};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:30343895};
CC -!- SUBUNIT: Forms a stable complex with cognate effector protein Tre1-Sp.
CC {ECO:0000269|PubMed:30343895}.
CC -!- DOMAIN: The N-terminal extension forms a projection that reaches into
CC the active site of cognate toxin Tre1-Sp where it occludes the active
CC site. {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 ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; CP000826; ABV42119.1; -; Genomic_DNA.
DR RefSeq; WP_012145740.1; NC_009832.1.
DR PDB; 6DRE; X-ray; 1.80 A; A=1-366.
DR PDB; 6DRH; X-ray; 2.30 A; A/C/E/G=1-366.
DR PDBsum; 6DRE; -.
DR PDBsum; 6DRH; -.
DR AlphaFoldDB; A8GG79; -.
DR SMR; A8GG79; -.
DR STRING; 399741.Spro_3018; -.
DR EnsemblBacteria; ABV42119; ABV42119; Spro_3018.
DR KEGG; spe:Spro_3018; -.
DR eggNOG; COG1397; Bacteria.
DR HOGENOM; CLU_024566_8_4_6; -.
DR OMA; PGTWTDD; -.
DR OrthoDB; 1661477at2; -.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..366
FT /note="ADP-ribosylarginine hydrolase Tri1"
FT /id="PRO_0000446517"
FT REGION 1..65
FT /note="N-terminal extension"
FT /evidence="ECO:0000269|PubMed:30343895"
FT REGION 74..366
FT /note="ADP-ribosyl hydrolase domain"
FT /evidence="ECO:0000305|PubMed:30343895"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30343895"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30343895"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30343895"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30343895"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30343895"
FT MUTAGEN 32
FT /note="R->E: Partially protects E.coli against cognate
FT toxin Tre1. No longer protects E.coli; when associated with
FT N-161."
FT /evidence="ECO:0000269|PubMed:30343895"
FT MUTAGEN 161
FT /note="D->N: Partially protects E.coli against cognate
FT toxin Tre1, no longer de-ADP-ribosylates FtsZ. No longer
FT protects E.coli; when associated with E-32."
FT /evidence="ECO:0000269|PubMed:30343895"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6DRH"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 65..86
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6DRE"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:6DRE"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:6DRE"
FT TURN 268..273
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6DRE"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:6DRE"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:6DRE"
SQ SEQUENCE 366 AA; 40934 MW; A9443B5B3280CC54 CRC64;
MIDLREDTWT LQLYAQRYKG LSPKNSRELQ LRMEYDPLKP NLPTSGEEQN SKPEWLNTPP
CLIPESESLD KAKGALVGLA IGDAIGTTLE FLPRDKLHVN DMVGGGPFRL QPGEWTDDTS
MALCLAESYI SAGRLDITLF REKLVRWYRH GENSSNGRCF DIGNTTRNAL EQYLKHGASW
FGNTEPETAG NAAIIRQAPT SIFRRKSLQR TFADSDSQSM ATHCAPESMA SCQFLGFILN
YLINGSSREK AFSPHVMPLP VRVLLINAGE YKEKKRDEIR SSGYVIDTLE AAMWAVWNTD
NFHDAILLAA NLGDDADSVA ATTGQIAGAL YGYSNIPKPW LDKLVQQERI SNLAEQLFYM
APEEDF
