PMC

Chemical structures of polyketides of Bacillus and Paenibacillus.
(A) Polyketides from B. amyloliquefaciens FZB42 (a, b, c) and Bacillus sp. AH159-1 (c): (a) difficidins, (b) bacillaenes and (c) macrolactins. Stereochemistry not shown.
(B) Polyketides from Paenibacillus: (a) Paenimacrolidin from Paenibacillus sp. F6-B70. Stereochemistry unknown. (b) Paenilamicin from P. larvae DSM25430.

Chemical structures of lipopeptides from Bacillus and Paenibacillus.
(A) Lipopeptides from B. amyloliquefaciens FZB42 (a,b,c): (a) surfactin, (b) bacillomycin (an iturin member), (c) plipastatin (a fengycin member) and (d) kurstakin from B. thuringiensis kurstaki HD-1.
(B) Lipopeptides from Paenibacillus: (a) polymyxin A from P. polymyxa E681, (b) fusaricidin C from P. polymyxa E681, (c) paenibacterin from Paenibacillus sp. OSY-SE (d) tridecaptin from P. terrae NRRL B-30644.

Organization of the non-ribosomal peptide synthetases (NRPS) encoding lipopeptides in Paenibacillus and Bacillus. Iterative domains: A, adenylation; T, thiolation; E, epimerization; MCT, malonyl-CoA transacylase; ACL, acyl-coA ligase; AMT, aminotransferase; dab, 2,4-diaminobutyric acid; orn, ornithine; KS, keto synthetase; TE, thioesterase. Further details of domains are described in . Modules and recruited amino acids indicated below, gene names indicated above each illustration.
(A) Organization of the known NRPS (a) polymyxin A in P. polymyxa E681, (b) fusaricidin in P. polymyxa E681 and (c) tridecaptin A in P. terrae NRRL B-30644.
(B) Organization of the predicted novel NRPS encoding (a) a heptapeptide in P. polymyxa E681; modular architecture is similar to the known Iturin but predicted amino acid composition is completely different and (b) organization of the known mycosubtilin operon , an iturin member from B. subtilis for comparison.

Architectures of type I polyketide synthases (PKS) showing similarities and dissimilarities in known and predicted PKs. Iterative domains: ACP, acyl carrier protein; PCP, peptidyl carrier protein; A, adenylation; KS, ketosynthase; DH, dehydratase; MT, methyl transferase; KR, ketoreductase; TE, thioesterase. Further details of domains are described in . Modules and recruited amino acids indicated below, gene names indicated above each illustration.
(A) Gene clusters of the three types of well-known PKS from B. amyloliquefaciens FZB42: (a) difficidin, (b) macrolactin, (c) bacillaene.
Modular regions of predicted PKS: (a) bacillaene variant from P. pini 16418; number and order of the domains differ from B.amyloliquefaciens FZB42 bacillaene, (b) novel PKS from P. polymyxa E681; an adenylation domain specifies glycine, (c) paenimacrolidine like PKS from P. durus DSM 1735, (d) novel PKS form Brevibacillus brevis NBRC 100599; adenylation domains specify ala and ser, also contains the methylation domains- oMT and nMT. These predicted PKS machinery in Paenibacillus may work without thioesterase.