UniProt functional annotation for A8GG78



	UniProt functional annotation for A8GG78

UniProt code: A8GG78.

Organism: Serratia proteamaculans (strain 568).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Yersiniaceae; Serratia.

Function: Toxic component of a contact-dependent interbacterial competition system (also called effector-immunity systems). Acts by ADP-ribosylating a number of target proteins in target cells; E.coli target proteins include FtsZ, EFTu, RNase E, Fis, RL9, SucB, and LolD. FtsZ is thought to be the physiologically relevant target as it is ADP- ribosylated on a critical residue. ADP-ribosylation of FtsZ prevents formation of the FtsZ mid-cell ring and inhibits cell division. Overexpression of the whole Tre1 protein or the ART domain in E.coli is toxic; cells elongate dramatically and some undergo lysis. Toxic activity is neutralized by coexpression of the cognate immunity protein Tri1-Sp; Tri1-Sp neutralizes this protein both by binding to and occluding the active site (via Tri1's N-terminal extension) and by hydrolysis of the ADP-ribosyl moiety from the target protein. Tre1 can also be neutralized by non-cognate immunity protein Tri1-Pp from P.putida strain GB-1, with which it does not form a stable complex; DraG of R.palustris does not neutralize the toxic effects of this protein. In interbacterial competition studies Tri1 from P.putida strain B6-2 also neutralizes this protein. {ECO:0000269|PubMed:30343895}.

Catalytic activity: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D- ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:0000269|PubMed:30343895};

Subunit: Forms a stable complex with cognate immunity protein Tri1-Sp. {ECO:0000269|PubMed:30343895}.

Subcellular location: Secreted {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Probably delivered to target cells by a type 6 secretion system (T6SS). {ECO:0000305|PubMed:30343895}.

Domain: The ART domain is toxic when expressed as a protein fragment. {ECO:0000269|PubMed:30343895}.

Disruption phenotype: A double tre1-tri1 deletion is outcompeted by wild-type cells, but not by wild-type cells missing a type 6 secretion system (T6SS). {ECO:0000269|PubMed:30343895}.

Similarity: Belongs to the Arg-specific ADP-ribosyltransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Serratia proteamaculans (strain 568).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Yersiniaceae; Serratia.



Function:		Toxic component of a contact-dependent interbacterial competition system (also called effector-immunity systems). Acts by ADP-ribosylating a number of target proteins in target cells; E.coli target proteins include FtsZ, EFTu, RNase E, Fis, RL9, SucB, and LolD. FtsZ is thought to be the physiologically relevant target as it is ADP- ribosylated on a critical residue. ADP-ribosylation of FtsZ prevents formation of the FtsZ mid-cell ring and inhibits cell division. Overexpression of the whole Tre1 protein or the ART domain in E.coli is toxic; cells elongate dramatically and some undergo lysis. Toxic activity is neutralized by coexpression of the cognate immunity protein Tri1-Sp; Tri1-Sp neutralizes this protein both by binding to and occluding the active site (via Tri1's N-terminal extension) and by hydrolysis of the ADP-ribosyl moiety from the target protein. Tre1 can also be neutralized by non-cognate immunity protein Tri1-Pp from P.putida strain GB-1, with which it does not form a stable complex; DraG of R.palustris does not neutralize the toxic effects of this protein. In interbacterial competition studies Tri1 from P.putida strain B6-2 also neutralizes this protein. {ECO:0000269\|PubMed:30343895}.


Catalytic activity:		Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D- ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:0000269\|PubMed:30343895};
Subunit:		Forms a stable complex with cognate immunity protein Tri1-Sp. {ECO:0000269\|PubMed:30343895}.
Subcellular location:		Secreted {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Probably delivered to target cells by a type 6 secretion system (T6SS). {ECO:0000305\|PubMed:30343895}.
Domain:		The ART domain is toxic when expressed as a protein fragment. {ECO:0000269\|PubMed:30343895}.
Disruption phenotype:		A double tre1-tri1 deletion is outcompeted by wild-type cells, but not by wild-type cells missing a type 6 secretion system (T6SS). {ECO:0000269\|PubMed:30343895}.
Similarity:		Belongs to the Arg-specific ADP-ribosyltransferase family. {ECO:0000305}.