Bacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Bacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.

Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family.

Bacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.

Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains.

Bacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.

Surfactin synthetase; Probably activates a leucine.

Bacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.

Putative iron-chelator esterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Promiscuous acetyl xylan esterase-cephalosporin C deacetylase; Esterase that removed acetyl groups from a number of O- acetylated small substrates, such as acetylated xylose, short xylooligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan. Cannot cleave amide linkages. Belongs to the carbohydrate esterase 7 family.

Alpha/beta hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the RBBP9 family.

Promiscuous acetyl xylan esterase-cephalosporin C deacetylase; Esterase that removed acetyl groups from a number of O- acetylated small substrates, such as acetylated xylose, short xylooligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan. Cannot cleave amide linkages. Belongs to the carbohydrate esterase 7 family.

Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the dienelactone hydrolase family.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Bacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Ala/Val as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Ala/Val residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Surfactin synthetase; Probably activates a leucine.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Surfactin synthetase; Probable thioesterase involved in the biosynthesis of surfactin; Belongs to the thioesterase family.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Putative iron-chelator esterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Putative hydrolase/transferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.

Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.

Secreted alkaliphilic lipase; Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups. Belongs to the AB hydrolase superfamily.

Secreted esterase / lipase; An esterase which preferentially hydrolyzes triacylglyceride substrates with short chain fatty acids (less than C10) with the maximum activity towards tricaprylin (C8:0). Active against p- nitrophenylesters with fatty acid chain lengths from C6 to C18.

Secreted alkaliphilic lipase; Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups. Belongs to the AB hydrolase superfamily.

Carboxylesterase NP; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the AB hydrolase superfamily.