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ansA ansA rpsJ rpsJ rpsE rpsE ilvE ilvE ansZ ansZ yhdR yhdR gltB gltB gltA gltA aspB aspB gudB gudB ansB ansB ansR ansR bcd bcd mdh mdh ald ald fumC fumC bacG bacG rocG rocG ilvK ilvK
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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:
ansAExported L-asparaginase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparaginase 1 family. (329 aa)
rpsJRibosomal protein S10 (BS13); Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. (102 aa)
rpsERibosomal protein S5; With S4 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations); Belongs to the universal ribosomal protein uS5 family. (166 aa)
ilvEKetomethiobutyrate-branched-chain/aromatic amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (356 aa)
ansZL-asparaginase 2 (putative lipoprotein); Catalyzes the conversion of L-asparagine to L-aspartate and ammonium. (375 aa)
yhdRPutative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (393 aa)
gltBGlutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (493 aa)
gltAGlutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. (1520 aa)
aspBPutative aspartate aminotransferase; 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 class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa)
gudBCryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] (427 aa)
ansBL-aspartase (aspartate ammonia lyase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II fumarase/aspartase family. Aspartase subfamily. (475 aa)
ansRTranscriptional regulator of ansAB (Xre family); Transcriptional repressor for the ans operon coding for L- asparaginase and L-aspartase. NH4(+) may influence this repression. (116 aa)
bcdBranched-chain amino acid dehydrogenase; Catalyzes the reversible deamination of L-leucine to 4- methyl-2-oxopentanoate. (364 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
aldL-alanine dehydrogenase; Catalyzes the reversible oxidative deamination of L-alanine to pyruvate. This enzyme is a key factor in the assimilation of L- alanine as an energy source through the tricarboxylic acid cycle during sporulation. (378 aa)
fumCFumarate hydratase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (462 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)
rocGGlutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...] (424 aa)
ilvKBranched-chain amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (363 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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