[Background] Phosphopantetheinyl transferases (PPTases) are known to catalyze the transformation of peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs) from inactive apo-form to active holo-form, so that initiating the synthesis of nonribosomal polypeptides. [Objective] To identify the Sfp-type PPTases Bap from the marine sponge Dysidea avara symbiont Bacillus atrophaeus C89 and to confirm the function of Bap in activating PCPs in NRPSs. [Methods] Sfp-type PPTase Bap from B. atrophaeus C89 was identified by BLAST and amino acid sequences alignment. The bap gene was heterologously expressed in the sfp gene mutant strain Bacillus subtilis 168. The nonribosomal polypeptide surfactin was detected from the metabolites of the recombinant strains B. subtilis 168-bap. [Results] Bap was identified to be Sfp-type PPTases, and the production of surfactin was detected in recombinant strains B. subtilis 168-bap. [Conclusion] Our findings provide basis for heterologous expression of NRPSs gene clusters from marine B. atrophaeus.