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csdA csdA erpA erpA bolA bolA grxD grxD sufE sufE sufS sufS sufD sufD sufC sufC sufB sufB sufA sufA mrp mrp cysM cysM iscX iscX fdx fdx hscA hscA hscB hscB iscA iscA iscU iscU iscS iscS ygfZ ygfZ ibaG ibaG nfuA nfuA cyaY cyaY fpr fpr ytfE ytfE
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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csdACysteine sulfinate desulfinase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, and transiently retains the released sulfur atom on a cysteine residue, in the form of a persulfide. Can also desulfinate L-cysteine sulfinate, which is the best substrate of the enzyme. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Seems to participate in Fe/S biogenesis by recruiting the SufBCD-SufE proteins. Transfers sulfur to CsdE that increases the cys [...] (401 aa)
erpAIron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family. (114 aa)
bolAStationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...] (105 aa)
grxDGlutaredoxin-4; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters; Belongs to the glutaredoxin family. Monothiol subfamily. (115 aa)
sufESulfur acceptor protein; Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L- alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process. Together with the SufBCD complex, it thereby enhances up to 50-fold, the cysteine desulfurase activity of SufS. Component of [...] (138 aa)
sufSCysteine desulfurase, stimulated by SufE; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd [...] (406 aa)
sufDComponent of SufBCD Fe-S cluster assembly scaffold; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein. (423 aa)
sufCSufBCD Fe-S cluster assembly scaffold protein, ATP-binding protein; Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. (248 aa)
sufBComponent of SufBCD Fe-S cluster assembly scaffold; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. (495 aa)
sufAFe-S cluster assembly protein. (122 aa)
mrpAntiporter inner membrane protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (369 aa)
cysMCysteine synthase B (O-acetylserine sulfhydrolase B); Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. (303 aa)
iscXFe(2+) donor and activity modulator for cysteine desulfurase; May function as iron donor in the assembly of iron-sulfur clusters; Belongs to the IscX family. (66 aa)
fdx[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins. (111 aa)
hscADnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU; Belongs to the heat shock protein 70 family. (616 aa)
hscBHscA co-chaperone, J domain-containing protein Hsc56; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. (171 aa)
iscAFeS cluster assembly protein; Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB; Belongs to the HesB/IscA family. (107 aa)
iscUIron-sulfur cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D- state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters; Belongs to the NifU family. (128 aa)
iscSCysteine desulfurase (tRNA sulfurtransferase), PLP-dependent; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to a [...] (404 aa)
ygfZIron-sulfur cluster repair protein, plumbagin resistance; Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication; Belongs to the tRNA-modifying YgfZ family. (326 aa)
ibaGAcid stress protein; Involved in cell resistance against acid stress. (84 aa)
nfuAFe/S biogenesis protein, putative scaffold/chaperone protein; Involved in iron-sulfur cluster biogenesis under severe conditions such as iron starvation or oxidative stress. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. Required for E.coli to sustain oxidative stress and iron starvation. Also necessary for the use of extracellular DNA as the sole source of carbon and energy. Belongs to the NfuA family. (191 aa)
cyaYIron-dependent inhibitor of iron-sulfur cluster formation; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. Can bind both Fe(2+) and Fe(3+) ions. In vivo, has a positive effect on Fe-S cluster biogenesis under iron- rich growth conditions. In vitro, can inhibit IscS cysteine desulfurase activity and the formation of Fe-S clusters on IscU. In vitro, in the presence of IscS and cysteine, Fe(3+)-CyaY can be used as an iron donor during Fe-S cluster assembly on the scaffold protein IscU. (106 aa)
fprferredoxin-NADP reductase; Transports electrons between flavodoxin or ferredoxin and NADPH. Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase. Belongs to the ferredoxin--NADP reductase type 1 family. (248 aa)
ytfEIron-sulfur cluster repair protein RIC; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. (220 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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