STRINGSTRING
coaD coaD asnH asnH yxiE yxiE tyrZ tyrZ argS argS tagD tagD asnB asnB leuS leuS tyrS tyrS thiI thiI argG argG etfB etfB etfA etfA valS valS mnmA mnmA nadD nadD panC panC ribC ribC sat sat cysH cysH ileS ileS ylbM ylbM queC queC trpS trpS yitB yitB yitA yitA asnO asnO nhaX nhaX guaA guaA nadE nadE cysS cysS gltX gltX tilS tilS metS metS
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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
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textmining
co-expression
protein homology
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coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (161 aa)
asnHAsparagine synthetase (glutamine-hydrolyzing); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparagine synthetase family. (747 aa)
yxiEPhosphate starvation protein (universal stress protein A family); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the universal stress protein A family. (148 aa)
tyrZtyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. (413 aa)
argSarginyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (556 aa)
tagDGlycerol-3-phosphate cytidylyltransferase; Catalyzes the transfer of the cytidylyl group of CTP to sn- glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF. Belongs to the cytidylyltransferase family. (129 aa)
asnBAsparagine synthetase; Main asparagine synthetase in vegetative cells. (632 aa)
leuSleucyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (804 aa)
tyrStyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). (422 aa)
thiIPutative persulfide ATP pyrophosphatase involved in thiamine biosynthesis and tRNA modification; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (401 aa)
argGArgininosuccinate synthase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (403 aa)
etfBElectron transfer flavoprotein (beta subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). (257 aa)
etfAElectron transfer flavoprotein (alpha subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). (325 aa)
valSvalyl-tRNA synthetase; As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (By similarity). Catalyzes the attachment of valine to tRNA(Val); Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (880 aa)
mnmAtRNA 2-thiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. (371 aa)
nadDNicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD); Belongs to the NadD family. (189 aa)
panCPantothenate synthetase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (286 aa)
ribCBifunctional riboflavin kinase FAD synthase; Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD. (316 aa)
satSulfate adenylyltransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (382 aa)
cysH(phospho)adenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. (233 aa)
ileSisoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). (921 aa)
ylbMConserved hypothetical protein; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. (415 aa)
queCPre-queuosine 0 synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Uses ammonia as nitrogen donor. (219 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (330 aa)
yitBPutative phospho-adenylylsulfate sulfotransferase; Reduction of activated sulfate into sulfite; Belongs to the PAPS reductase family. CysH subfamily. (236 aa)
yitAPutative sulfate adenylyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the sulfate adenylyltransferase family. (389 aa)
asnOAsparagine synthetase; Asparagine synthetase involved in sporulation. (614 aa)
nhaXStress response protein, UspA family; Evidence 2b: Function of strongly homologous gene; factor. (166 aa)
guaAGMP synthetase; Catalyzes the synthesis of GMP from XMP. (513 aa)
nadEAmmonium-dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (272 aa)
cysScysteinyl-tRNA synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (466 aa)
gltXglutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (483 aa)
tilStRNAile lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (472 aa)
metSmethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. (664 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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