); [EMAIL_ADDRESS] (T.M. ); [EMAIL_ADDRESS] (T.M. ); [EMAIL_ADDRESS] (W.P.E.) [PERSON]  
2 Laboratorio de Desenvolvimento de Vacinas, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (L.M.M.-N.); [EMAIL_ADDRESS] (J.C.C.L.) [PERSON]  
1 Laboratorio de Baccteriologia, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (J.C.A.S. ); [EMAIL_ADDRESS] (E.C. ); aledari.fuseny.br (A.M.G.D.C. ); [EMAIL_ADDRESS] (C.H. ); [EMAIL_ADDRESS] (T.M. ); [EMAIL_ADDRESS] (T.M. ); [EMAIL_ADDRESS] (W.P.E.) [PERSON]  
2 Laboratorio de Desenvolvimento de Vacinas, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (L.M.M.-N.); [EMAIL_ADDRESS] (L.M.C.C.L)  
[PERSON]  
1 Laboratorio de Baccteriologia, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (J.C.A.S. ); [EMAIL_ADDRESS] (E.C.L. ); aledari.fuseny.br (A.M.G.D.C. ); [EMAIL_ADDRESS] (C.H. ); [EMAIL_ADDRESS] (T.M. ); [EMAIL_ADDRESS] (W.P.E.) [PERSON]  
2 Laboratorio de Desenvolvimento de Vacinas, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (L.M.M.-N.); [EMAIL_ADDRESS] (L.C.C.L.) [PERSON]  
1 Laboratorio de Desenvolvimento de Vacinas, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (L.M.M.-N.); [EMAIL_ADDRESS] (L.M.C.C.L.) [PERSON]  
1 Laboratorio de Baccteriologia, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [EMAIL_ADDRESS] (L.M.M.-N.); [EMAIL_ADDRESS] (L.C.C.L.) [PERSON]  
1 Laboratorio de Baccteriologia, Instituto Butantan, Avenida Vital Brazil, 1500, Sao Paulo 05503-900, SP, Brazil; [PERSON](J.C.A.S. ); [EMAIL_ADDRESS] (characterized, where the formation of a TA complex occurs through a direct protein-protein interaction between the toxin and antitoxin, effectively inhibiting the toxin activity [5; 6]. These systems were discovered in the 1980s as modules that were present in plasmids, and, after the characterization of R1 and F plasmids, the \"post-segregational killing\" (PSK) model was established, referring to its role in controlling cells that fail to inherit a plasmid copy [7; 8]. Furthermore, different functions were proposed for plasmid-encoded systems, since they affect important bacterial physiological processes such as DNA replication, translation, cell division, and ATP synthesis [9; 10]. DNA sequencing technology and bioinformatic approaches allowed the identification of thousands of TA systems in bacterial chromosomes, and, currently, more than 10,000 TA models are known [11; 12]. Despite the well-established functions of plasmid-encoded systems, the proposed roles for their chromosomal counterparts are still inconsistent, being largely associated with bacterial physiology, including stress-response-promoting fitness, antibiotic persistence, and, therefore, general bacterial pathogenesis [13; 14; 15]. Some studies demonstrated the activation of type II TA systems in stress conditions, like the RelBE system in _Escherichia coli_ K-12 with a robust induction of _relBE_ transcription under nutritional stress, where RelE reduced the overall translation rate during nutrient scarcity favoring bacterial survival [16]. The antitoxin MqsA was described to be part of the stress response in _E. coli_, wherein the antitoxin represses stress response regulators. When this antitoxin is degraded under specific conditions, the regulator genes are derepressed, enabling the proper response, which can induce other activities such as biofilm formation and reduced motility [15]. In an Upopathogenic _E. coli_ (UPEC) strain, one of the main pathogens causing urinary tract infections, the association of the type II TA system PasT-PasI with stress response was demonstrated with an increase in toxin expression, resulting in resistance to nitrosative and oxidative stress, regulating bacterial growth.