In this study, bioinformatics methods were applied to analyze the Bacillus subtilis lipase LipA, aiming to lay some theoretical foundation for the subsequent study of LipA. The primary structure, hydrophobicity, basic properties, secondary structure, special crimp helix, motif and PEST sequences rich in proline (p), glutamic acid (E), serine (s) and threonine (T) of LipA were predicted and analyzed by using a series of online websites or software, the homology modeling of the tertiary structure was carried out, and the surface potential, the accessibility distribution and the Ramachandran diagram were analyzed. Bacillus subtilis lipase LipA is a stable liposoluble protein composed of 212 amino acids. The regions with the strongest hydrophilicity and hydrophobicity were predicted to be Lys75~Asn81 and Val9~Leu17, and there is no stable dimer, trimer curling helix and non-PEST sequences. LipA was found to have three motifs that may participate in different biochemical reactions, as well as α/β proteins with five segments α-helix, six-segment β-sheets; LipA is predicted to be weak positive potential; The modeled three-dimensional structure is shown by accessibility and Ramachandran diagram to be reasonable and reliable. The subsequent molecular design and modification of Bacillus subtilis lipase LipA were provided with some theoretical basis in this study.