UNLABELLED

HolPase is a crucial enzyme catalyzing dephosphorylation of L-histidinol-phosphate (Hol-P) to L-histidinol, usually the last and most difficult enzyme to be identified in histidine biosynthesis due to its complex origin and evolution. We previously reported that PA0335 encode a HolPase belonging to the HAD family and inactivation resulted incomplete L-histidine auxotrophy in , suggesting the presence of alternate HolPase enzymes. In this study, the alternative homologs of PA0335 encoded HolPase were identified and primarily characterized in . PA3255 and PA1143 code phosphatase with side HolPase activity. PA0335 play a key role in histidine biosynthesis, PA3255 respond mainly for the residual growth when PA0335 HolPase is absence. Moreover, all three genes, especially for PA3255, are required for the resistance of PA to ciprofloxacin and meropenem, while PA3255 and PA0335 are required for the full virulence but inactivation of PA1143 increased the pathogens of . PA0335 and PA3255 could be used as targets for infection treatment separately or synergistically due to their participates in histidine auxotrophy, full virulence and obvious antibiotics resistance in . The relation and regulation of the three phosphatases with HolPase or side HolPase activity need further study.

SUPPLEMENTARY INFORMATION

The online version contains supplementary material available at 10.1186/s12866-025-04092-3.