The products of a nonribosomal peptide synthetase gene, <i>holA</i>, from <i>Paraburkholderia rhizoxinica</i> were investigated using our recently established recombineering technique. Fifteen products, including 13 new linear lipopeptides, holrhizins E-Q (<b>2</b>-<b>8</b>, <b>10</b>-<b>15</b>), together with the two known holrhizins A and B (<b>1</b>, <b>9</b>), were detected in the activated mutant, and their structures were identified using HRESIMS, NMR spectroscopy, Marfey's analysis, and feeding experiments with labeled amino acids. The lipohexapeptides <b>1</b>-<b>3</b> and <b>7</b>-<b>14</b> differ in three amino acid residues and the N-terminal fatty acid chains. The diversity of the holrhizins originates from the substrate flexibility of the A<sub>4</sub>, A<sub>5</sub>, and A<sub>6</sub> domains as well as the starter C domain in the biosynthetic pathway.