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srfAA srfAA srfAB srfAB comS comS srfAC srfAC srfAD srfAD pksB pksB pksC pksC pksD pksD pksE pksE acpK acpK pksF pksF pksG pksG pksH pksH pksI pksI pksJ pksJ pksL pksL pksM pksM pksN pksN pksR pksR pksS pksS ppsE ppsE ppsD ppsD ppsC ppsC ppsB ppsB ppsA ppsA ybdZ ybdZ dhbB dhbB
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
srfAASurfactin 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. (3587 aa)
srfABSurfactin 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. (3583 aa)
comSRegulator of genetic competence; Required for the development of competence. (46 aa)
srfACSurfactin synthetase; Probably activates a leucine. (1275 aa)
srfADSurfactin synthetase; Probable thioesterase involved in the biosynthesis of surfactin; Belongs to the thioesterase family. (242 aa)
pksBPutative hydrolase; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism; Belongs to the metallo-beta-lactamase superfamily. (225 aa)
pksCmalonyl-CoA-acyltransferase involved in polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK); Belongs to the FabD family. (288 aa)
pksDEnzyme involved in polyketide synthesis; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (324 aa)
pksEEnzyme involved in polyketide synthesis; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity; In the N-terminal section; belongs to the FabD family. (767 aa)
acpKAcyl-carrier protein; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (82 aa)
pksFDecarboxylase converting malonyl-S-AcpK to acetyl-S-AcpK for polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It decarboxylates selectively the malonyl group attached on the acyl-carrier-protein AcpK (Mal-AcpK); Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (415 aa)
pksGacetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. (420 aa)
pksHDehydratase for polyketide biosynthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably catalyzes the dehydration of the (S)-3-hydroxy-3- methylglutaryl group attached to PksL. (259 aa)
pksIDecarboxylase involved in polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. May have a role in the decarboxylation of the (S)-3- methylglutaryl group attached to PksL. (249 aa)
pksJPolyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (5043 aa)
pksLPolyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4538 aa)
pksMPolyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4262 aa)
pksNPolyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (5488 aa)
pksRPolyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (2543 aa)
pksSCytochrome P450 of bacillaene metabolism; Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene. (405 aa)
ppsEPlipastatin 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. (1279 aa)
ppsDPlipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr 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. (3603 aa)
ppsCPlipastatin 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. (2555 aa)
ppsBPlipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. (2560 aa)
ppsAPlipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn 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. (2561 aa)
ybdZConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. (69 aa)
dhbBIsochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (312 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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