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pksC pksC bacA bacA bacB bacB bacC bacC bacD bacD bacG bacG bacH bacH albG albG albF albF albE albE albD albD albB albB albA albA sdpB sdpB sdpA sdpA ytpA ytpA sunT sunT sunS sunS ppsA ppsA ppsB ppsB ppsC ppsC ppsD ppsD ppsE ppsE pksS pksS pksM pksM pksL pksL pksJ pksJ pksI pksI pksH pksH pksG pksG pksF pksF acpK acpK pksE pksE pksD pksD pksB pksB ntdA ntdA ntdB ntdB ntdC ntdC yczE yczE srfAD srfAD srfAC srfAC srfAB srfAB srfAA srfAA skfH skfH skfG skfG skfF skfF skfE skfE skfC skfC skfB skfB
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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)
bacABacilysin biosynthesis protein, dehydratase; Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacA is an unusual prephenate decarboxylase that avoids the typical aromatization of the cyclohexadienol ring of prephenate. BacA catalyzes the protonation of prephenate (1-carboxy-4-hydroxy- alpha-oxo-2,5-cyclohexadiene-1-propanoic acid) at C6 position, followed by a decarboxylation [...] (204 aa)
bacBIsomerase component of bacilysin (l-alanine-[2,3-epoxycyclohexano-4]-l-alanine) synthetase; Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacB catalyzes the allylic isomerization of the endocyclic-delta(4),delta(8)-7R-dihydro- hydroxyphenylpyruvate (en-H2HPP) to generate a mixture of 3E,7R- and 3Z, 7R-olefins (E/Z ration of 3/1) of the exocyclic-delta(3),delta(5)- dihydro-h [...] (235 aa)
bacCBacilysin biosynthesis oxidoreductase; Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala). It is not able to oxidize the 4R-H4Tyr diastereomer and the dihydrobacilysin dipeptide (L-Ala-4S-H4Tyr dipeptide). (253 aa)
bacDAlanine-anticapsin ligase; Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. In vivo catalyzes the ligation of L-alanine and L-anticapsin (epoxycyclohexanonyl-Ala) to produce the final bacilysin antibiotic (L- Ala-L-4S-cyclohexenonyl-Ala dipeptide). The substrate specificity is restricted to small amino acids such as L-Ala, for the N-terminal end of the dipeptide, whereas a wide range o [...] (472 aa)
bacGPhenylalanine aminotransferase forming tetrahydrotyrosine in bacilysin synthesis; Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the reductive amination of the C2 ketone of tetrahydro-hydroxyphenylpyruvate (H4HPP), with L-Phe as an amino donor, to yield tetrahydrotyrosine (H4Tyr) diastereomer. D-Phe is not an effective amino donor. BacF associated to BacG converts [...] (399 aa)
bacHCyclohexenol-containing tetrahydro-4-hydroxyphenylpyruvate H(4)HPP in bacilysin synthesis; Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP). Although the [...] (259 aa)
albGPutative integral inner membrane protein involved in subtilosin production and immunity; Involved in the production of the bacteriocin subtilosin. (233 aa)
albFPutative peptidase involved in subtilosin production; Required for production of the bacteriocin subtilosin. Could catalyze some step in the processing of presubtilosin. (426 aa)
albEPutative hydrolase involved in subtilosin production; Involved in the production of the bacteriocin subtilosin. (386 aa)
albDPutative integral inner membrane protein involved in subtilosin production and immunity; Involved in the production of the bacteriocin subtilosin. Required for immunity to subtilosin. (436 aa)
albBPutative membrane component involved in subtilosin production; Involved in the production of the bacteriocin subtilosin. Required for maximal production and for optimal immunity to subtilosin. (53 aa)
albAPutative antilisterial bacteriocin (subtilosin) production enzyme; Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation. In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA. (448 aa)
sdpBExporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. (323 aa)
sdpAExport of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. (158 aa)
ytpAPhospholipase component of bacilysocin synthesis or export; Phospholipase involved in the biosynthesis of the antibiotic bacilysocin. It probably catalyzes the hydrolysis of the 2-sn-acyl moiety of phosphatidylglycerol to produce bacilysocin (lysophosphatidylglycerol). Is also able to catalyze the hydrolysis reaction of one acyl bond in phosphatidylcholine in vitro (actual cleavage point is unknown), resulting in lysophosphatidylcholine. (259 aa)
sunTSublancin 168 lantibiotic transporter; SunT (TC 3.A.1.112.4) is required for production of the lantibiotic sublancin-168, probably by both processing the signal peptide and exporting the resulting mature lantibiotic. (705 aa)
sunSSublancin glycosyltransferase; Transfers a hexose moiety onto 'Cys-41' of bacteriocin sublancin-168 (SunA). Accepts UDP-glucose (UDP-Glc), UDP-N- acetylglucosamine (UDP-GlcNAc), UDP-galactose (UDP-Gal), UDP-xylose (UDP-Xyl) and GDP-mannose as substrate. (422 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)
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)
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)
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)
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)
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)
pksMPolyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4262 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)
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)
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)
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)
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)
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)
acpKAcyl-carrier protein; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (82 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)
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)
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)
ntdA3-oxo-glucose-6-phosphate:glutamate aminotransferase; Involved in the biosynthesis of kanosamine (3-amino-3-deoxy- D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transamination of 3-dehydro- alpha-D-glucose 6-phosphate to form alpha-D-kanosamine-6-phosphate. It can only use alpha-anomer and glutamate is the only amino donor. (441 aa)
ntdBBiosynthesis of neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha, beta-trehalose);hydrolase; Involved in the biosynthesis of kanosamine (3-amino-3-deoxy- D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the dephosphorylation of kanosamine 6-phosphate to yield kanosamine. There is a trace amount of activity using glucosamine-6-phosphate. Belongs to the HAD-like hydrolase superfamily. Cof family. (282 aa)
ntdCBiosynthesis of neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose), dehydrogenase; Involved in the biosynthesis of kanosamine (3-amino-3-deoxy- D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the oxidation of glucose 6-phosphate to 3-oxo-D-glucose 6-phosphate. It can only use NAD. (350 aa)
yczEN-terminal part of 4'-phosphopantetheinyl transferase (Surfactin synthetase-activating enzyme); Evidence 7: Gene remnant; Product type e: enzyme. (215 aa)
srfADSurfactin synthetase; Probable thioesterase involved in the biosynthesis of surfactin; Belongs to the thioesterase family. (242 aa)
srfACSurfactin synthetase; Probably activates a leucine. (1275 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)
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)
skfHSibling killing effect; Required for production of the bacteriocin SkfA. (141 aa)
skfGSporulation killing factor biosynthesis and export; Required for production of the bacteriocin SkfA. (171 aa)
skfFSporulation killing factor biosynthesis and export; Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for the translocation of bacteriocin SkfA across the membrane. (447 aa)
skfESporulation killing factor biosynthesis and export; Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for energy coupling to the transport system. (239 aa)
skfCSporulation killing factor biosynthesis and export; Required for production of the bacteriocin SkfA. (496 aa)
skfBSynthesis of sporulation killing factor A; Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA. Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys. The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this is the first rea [...] (410 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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