UniProt functional annotation for Q5F881



	UniProt functional annotation for Q5F881

UniProt code: Q5F881.

Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).

Taxonomy: Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.

Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. {ECO:0000269|PubMed:10639460}.

Subunit: Homodimer in the absence of FitB; forms a heterodimer with FitB; 4 FitAB heterodimers form a complex that binds to fitAB promoter DNA. The complex is also seen in solution. {ECO:0000269|PubMed:16156663, ECO:0000269|PubMed:16982615}.

Disruption phenotype: Disruption of the fitAB operon leads to faster transepithelial cell trafficking of the bacterium; mutants adhere to and invade cells normally. Mutants grow normally in liquid culture but much faster within human cell lines A431 and T84; these latter 2 phenotypes were observed using MS11A bacteria with a disrupted fitAB locus. {ECO:0000269|PubMed:10639460}.

Annotations taken from UniProtKB at the EBI.


Organism:		Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
Taxonomy:		Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.



Function:		Antitoxin component of a type II toxin-antitoxin (TA) system. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. {ECO:0000269\|PubMed:10639460}.


Subunit:		Homodimer in the absence of FitB; forms a heterodimer with FitB; 4 FitAB heterodimers form a complex that binds to fitAB promoter DNA. The complex is also seen in solution. {ECO:0000269\|PubMed:16156663, ECO:0000269\|PubMed:16982615}.
Disruption phenotype:		Disruption of the fitAB operon leads to faster transepithelial cell trafficking of the bacterium; mutants adhere to and invade cells normally. Mutants grow normally in liquid culture but much faster within human cell lines A431 and T84; these latter 2 phenotypes were observed using MS11A bacteria with a disrupted fitAB locus. {ECO:0000269\|PubMed:10639460}.