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mntR mntR bioD bioD cysS cysS hemB hemB dksA dksA hisI hisI yjiA yjiA basR basR metR metR slyD slyD zntR zntR argK argK queD queD hypB hypB yeiR yeiR thrS thrS yciC yciC
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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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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
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Your Input:
mntRMn(2+)-responsive manganese regulon transcriptional regulator; In the presence of manganese, represses expression of mntH and mntS. Up-regulates expression of mntP. (155 aa)
bioDDethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid; Belongs to the dethiobiotin synthetase family. (225 aa)
cysSCysteine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
hemB5-aminolevulinate dehydratase (porphobilinogen synthase); Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen; Belongs to the ALAD family. (324 aa)
dksATranscriptional regulator of rRNA transcription; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhibits formation of initiation complexes, and amplifies effects of ppGpp and the initiating NTP on rRNA transcription. Inhibits transcript elongation, exonucleolytic RNA cleavage and pyrophosphorolysis, and increases intrinsic terminat [...] (151 aa)
hisIPhosphoribosyl-amp cyclohydrolase; phosphoribosyl-ATP pyrophosphatase; Protein involved in histidine biosynthetic process; In the C-terminal section; belongs to the PRA-PH family. (203 aa)
yjiAMetal-binding GTPase; Binds GTP and has low GTPase activity. May have a GTP- dependent regulatory function; Belongs to the SIMIBI class G3E GTPase family. CobW subfamily. (318 aa)
basRResponse regulator in two-component regulatory system with BasS; Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin (By similarity). (222 aa)
metRMethionine biosynthesis regulon transcriptional regulator; Control of the last step in methionine biosynthesis; MetR is a positive activator of the metA, metE and metH genes. MetR is also a negative regulator of its own expression. Binds homocysteine as an inducer; Belongs to the LysR transcriptional regulatory family. (317 aa)
slyDFKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] (196 aa)
zntRzntA gene transcriptional activator; Zinc-responsive transcriptional regulator of zntA. (141 aa)
argKMembrane ATPase/protein kinase; Binds and hydrolyzes GTP. Likely functions as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) ScpA and reactivation of the enzyme during catalysis; Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB subfamily. (331 aa)
queD6-pyruvoyl tetrahydrobiopterin synthase (PTPS); Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP. (121 aa)
hypBGTP hydrolase involved in nickel liganding into hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion. In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA. Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily. (290 aa)
yeiRZn-stimulated GTPase involved in zinc homeostasis; Involved in metal homeostasis. Has GTPase activity. Binds several Zn(2+) ions in vitro. (328 aa)
thrSthreonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] (642 aa)
yciCUPF0259 family inner membrane protein. (247 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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