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coaD coaD nadR nadR nadE nadE argS argS uspC uspC metG metG gltX gltX guaA guaA cysD cysD cysH cysH ygcQ ygcQ ygcR ygcR hldE hldE argG argG trpS trpS uspA uspA tyrS tyrS ydcF ydcF uspF uspF ttcA ttcA mnmA mnmA elyC elyC phr phr glnS glnS asnB asnB leuS leuS nadD nadD citC citC uspG uspG ybdN ybdN cysS cysS queC queC thiI thiI tilS tilS gluQ gluQ panC panC fixB fixB fixA fixA ileS ileS ribF ribF uspD uspD valS valS ydiR ydiR ydiQ ydiQ
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
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textmining
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coaDPantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. CoA is not a substrate for the enzyme ; Belongs to the bacterial CoaD family. (159 aa)
nadRTrifunctional NAD biosynthesis/regulator protein NadR; This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity [...] (410 aa)
nadENAD synthetase, NH3/glutamine-dependent; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (275 aa)
argSArginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (577 aa)
uspCUniversal stress protein; Required for resistance to DNA-damaging agents. (142 aa)
metGmethionyl-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 1 subfamily. (677 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). (471 aa)
guaAGMP synthetase (glutamine aminotransferase); Catalyzes the synthesis of GMP from XMP. (525 aa)
cysDATP:sulfurylase (ATP:sulfate adenylyltransferase), subunit 2; Protein involved in sulfur metabolic process; Belongs to the PAPS reductase family. CysD subfamily. (302 aa)
cysHPhosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. (244 aa)
ygcQPutative flavoprotein; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (286 aa)
ygcRPutative flavoprotein; May play a role in a redox process. (259 aa)
hldEHeptose 7-phosphate kinase and heptose 1-phosphate adenyltransferase; Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate; In the N-terminal section; belongs to the carbohydrate kinase PfkB family. (477 aa)
argGArgininosuccinate synthetase; Protein involved in arginine biosynthetic process; Belongs to the argininosuccinate synthase family. Type 2 subfamily. (447 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Amino acylates tRNA(Trp) with both L- and D-tryptophan, although D-tryptophan is a poor substrate ; Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
uspAUniversal stress global response regulator; Required for resistance to DNA-damaging agents; Belongs to the universal stress protein A family. (144 aa)
tyrStyrosyl-tRNA synthetase; Catalyzes the attachment of L-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). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. (424 aa)
ydcFDUF218 superfamily protein, SAM-binding; Binds S-adenosyl-L-methionine (AdoMet); To S.coelicolor SCO4629. (266 aa)
uspFUniversal stress protein F; Pseudogene, prophage Rac integration site ttcA duplication;Phage or Prophage Related. (144 aa)
ttcAtRNA s(2)C32 thioltransferase, iron sulfur cluster protein; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. Belongs to the TtcA family. (311 aa)
mnmAtRNA(Gln,Lys,Glu) U34 2-thiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs. (368 aa)
elyCEnvelope biogenesis factor; Plays a critical role in the metabolism of the essential lipid carrier used for cell wall synthesis. (259 aa)
phrDeoxyribodipyrimidine photolyase, FAD-binding; Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. (472 aa)
glnSGlutamine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (554 aa)
asnBAsparagine synthetase B; Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity. (554 aa)
leuSLeucine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
nadDNicotinic acid mononucleotide adenylyltransferase, NAD(P)-dependent; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). Belongs to the NadD family. (213 aa)
citCCitrate lyase ligase; Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'- dephosphocoenzyme-A) of the gamma subunit of citrate lyase. (352 aa)
uspGUniversal stress protein UP12; Has intrinsic autoadenylation and autophosphorylation activities, probably on Ser or Thr residues. Belongs to the universal stress protein A family. (142 aa)
ybdNPAPS reductase-like domain protein. (406 aa)
cysSCysteine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
queC7-cyano-7-deazaguanine (preQ0) synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). (231 aa)
thiItRNA s(4)U8 sulfurtransferase; 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. Belongs to the ThiI family. (482 aa)
tilStRNA(Ile)-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. This enzyme is essential for viability. (432 aa)
gluQglutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis. (308 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. (283 aa)
fixBProtein FixB; Required for anaerobic carnitine reduction. May bring reductant to CaiA; Belongs to the ETF alpha-subunit/FixB family. (313 aa)
fixAAnaerobic carnitine reduction putative electron transfer flavoprotein subunit; Required for anaerobic carnitine reduction. May bring reductant to CaiA; Belongs to the ETF beta-subunit/FixA family. (256 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). (938 aa)
ribFBifunctional riboflavin kinase/FAD synthetase; Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD; Belongs to the RibF family. (313 aa)
uspDStress-induced protein; Required for resistance to DNA-damaging agents. (142 aa)
valSvalyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). 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. (951 aa)
ydiRPutative electron transfer flavoprotein, FAD-binding subunit; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (312 aa)
ydiQPutative electron transfer flavoprotein subunit; May play a role in a redox process; Belongs to the ETF beta-subunit/FixA family. (254 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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