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djlA djlA yadR yadR pepD pepD bolA bolA copA copA ybdK ybdK dsbG dsbG ahpC ahpC ahpF ahpF ybgH ybgH ybgI ybgI ybgJ ybgJ ybgK ybgK ybgL ybgL nei nei yliJ yliJ grxA grxA hcr hcr hcp hcp trxB trxB pepN pepN ycbX ycbX grxB grxB dsbB dsbB chaC chaC tpx tpx gst gst sodC sodC ydhD ydhD sodB sodB sufE sufE sufS sufS sufD sufD sufC sufC sufB sufB sufA sufA btuE btuE katE katE yeaQ yeaQ yoaG yoaG yeaR yeaR yeaW yeaW yeaX yeaX mrp mrp yfcF yfcF bcp bcp pepB pepB yfhJ yfhJ fdx fdx hscA hscA hscB hscB iscA iscA iscU iscU iscS iscS iscR iscR hmp hmp trxC trxC gshA gshA norR norR norV norV norW norW ygbA ygbA csdA csdA ygdK ygdK ygdL ygdL dsbC dsbC gshB gshB gss gss yrbA yrbA gntY gntY ggt ggt gor gor grxC grxC yibN yibN trxA trxA cyaY cyaY dsbA-2 dsbA-2 sodA sodA yiiM yiiM katG katG oxyR oxyR dipZ dipZ nsrR nsrR ytfE ytfE pepA pepA
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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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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
Your Input:
djlADnaJ-like protein, membrane anchored; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. (271 aa)
yadRPutative chaperone involved in Fe-S cluster assembly and activation; Required for insertion of 4Fe-4S clusters for at least IspG. (114 aa)
pepDAminoacyl-histidine dipeptidase (peptidase D); Function experimentally demonstrated in the studied species; enzyme. (485 aa)
bolARegulator of penicillin binding proteins and beta lactamase transcription (morphogene); Function experimentally demonstrated in the studied species; regulator; Belongs to the BolA/IbaG family. (105 aa)
copACopper transporter; Function experimentally demonstrated in the studied species; transporter. (834 aa)
ybdKGamma-glutamyl:cysteine ligase; ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. (372 aa)
dsbGPeriplasmic disulfide isomerase/thiol-disulphide oxidase; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (248 aa)
ahpCAlkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
ahpFAlkyl hydroperoxide reductase, F52a subunit, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (521 aa)
ybgHPutative transporter; Probable proton-dependent permease that transports dipeptides; Belongs to the PTR2/POT transporter (TC 2.A.17) family. DtpD subfamily. (493 aa)
ybgIConserved hypothetical protein; Homologs of previously reported genes of unknown function. (247 aa)
ybgJPutative hydrolase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (218 aa)
ybgKPutative hydrolase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (310 aa)
ybgLPutative lactam utilization protein, UPF0271 family; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. (244 aa)
neiEndonuclease VIII; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. (263 aa)
yliJPutative glutathione S-transferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (208 aa)
grxAGlutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); Function experimentally demonstrated in the studied species; carrier. (85 aa)
hcrHCP oxidoreductase, NADH-dependent; Function experimentally demonstrated in the studied species; enzyme. (322 aa)
hcpHybrid-cluster [4Fe-2S-2O] protein in anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. (550 aa)
trxBThioredoxin reductase, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (321 aa)
pepNFunction experimentally demonstrated in the studied species; enzyme. (870 aa)
ycbXPutative 2Fe-2S cluster-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (369 aa)
grxBGlutaredoxin 2 (Grx2); Function experimentally demonstrated in the studied species; carrier. (215 aa)
dsbBOxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (176 aa)
chaCRegulatory protein for cation transport; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides; Belongs to the gamma-glutamylcyclotransferase family. (238 aa)
tpxLipid hydroperoxide peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Tpx subfamily. (168 aa)
gstGlutathionine S-transferase; Function experimentally demonstrated in the studied species; enzyme. (201 aa)
sodCSuperoxide dismutase, Cu, Zn; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family. (173 aa)
ydhDMonothiol glutaredoxin; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glutaredoxin family. Monothiol subfamily. (115 aa)
sodBSuperoxide dismutase, Fe; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (193 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; Belongs to the SufE family. (138 aa)
sufSSelenocysteine lyase, PLP-dependent; 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. (406 aa)
sufDComponent of SufBCD complex; Function experimentally demonstrated in the studied species; factor. (423 aa)
sufCComponent of SufBCD complex, ATP-binding component of ABC superfamily; Function experimentally demonstrated in the studied species; transporter. (248 aa)
sufBComponent of SufBCD complex; Function of strongly homologous gene; putative transporter. (495 aa)
sufAFe-S cluster assembly protein; Function experimentally demonstrated in the studied species; factor; Belongs to the HesB/IscA family. (122 aa)
btuEPutative glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. (183 aa)
katEHydroperoxidase HPII(III) (catalase); Serves to protect cells from the toxic effects of hydrogen peroxide. (753 aa)
yeaQConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative membrane component. (82 aa)
yoaGConserved hypothetical protein; Homologs of previously reported genes of unknown function. (60 aa)
yeaRConserved hypothetical protein; Homologs of previously reported genes of unknown function. (119 aa)
yeaWFragment of putative transporter (partial); Converts carnitine to trimethylamine and malic semialdehyde. (374 aa)
yeaXPutative dioxygenase subunit; Converts carnitine to trimethylamine and malic semialdehyde. (321 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)
yfcFPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (214 aa)
bcpThiol peroxidase, thioredoxin-dependent; Function experimentally demonstrated in the studied species; enzyme. (156 aa)
pepBAminopeptidase B; Probably plays an important role in intracellular peptide degradation. (427 aa)
yfhJConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative factor. (66 aa)
fdx[2Fe-2S] ferredoxin; Function experimentally demonstrated in the studied species; carrier. (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. (616 aa)
hscBDnaJ-like molecular chaperone specific for IscU; 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. (107 aa)
iscUScaffold protein; A scaffold on which IscS assembles Fe-S clusters. 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. (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 and selenium atoms from cysteine and selenocysteine 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. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate; Belongs to the class-V pyr [...] (404 aa)
iscRDNA-binding transcriptional repressor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. (162 aa)
hmpFused nitric oxide dioxygenase; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress; Belongs to the globin family. Two-domain flavohemoproteins subfamily. (396 aa)
trxCThioredoxin 2; Function experimentally demonstrated in the studied species; carrier; Belongs to the thioredoxin family. (139 aa)
gshAGamma-glutamate-cysteine ligase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. (518 aa)
norRDNA-binding transcriptional activator; Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54. (504 aa)
norVFlavorubredoxin oxidoreductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. (479 aa)
norWNADH:flavorubredoxin oxidoreductase; One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase. (377 aa)
ygbAConserved hypothetical protein; Homologs of previously reported genes of unknown function. (114 aa)
csdACysteine sulfinate desulfinase; Function experimentally demonstrated in the studied species; enzyme. (401 aa)
ygdKPutative Fe-S metabolism protein (sufE-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (147 aa)
ygdLConserved hypothetical protein; Homologs of previously reported genes of unknown function. (268 aa)
dsbCProtein disulfide isomerase II; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (236 aa)
gshBGlutathione synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic GSH synthase family. (316 aa)
gssFused glutathionylspermidine amidase; Function experimentally demonstrated in the studied species; enzyme. (619 aa)
yrbAPutative DNA-binding transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator; Belongs to the BolA/IbaG family. (84 aa)
gntYPutative gluconate transport associated protein; Involved in iron-sulfur cluster biogenesis. 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. (191 aa)
ggtGamma-glutamyltranspeptidase; Function experimentally demonstrated in the studied species; enzyme. (580 aa)
gorGlutathione oxidoreductase; Function experimentally demonstrated in the studied species; carrier. (450 aa)
grxCGlutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. (83 aa)
yibNPutative rhodanese-related sulfurtransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (143 aa)
trxAFunction experimentally demonstrated in the studied species; carrier; Belongs to the thioredoxin family. (109 aa)
cyaYFrataxin, iron-binding and oxidizing protein; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. (106 aa)
dsbA-2Periplasmic protein disulfide isomerase I; Function experimentally demonstrated in the studied species; enzyme. (208 aa)
sodASuperoxide dismutase, Mn; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (206 aa)
yiiMConserved hypothetical protein; Homologs of previously reported genes of unknown function. (224 aa)
katGCatalase/hydroperoxidase HPI(I); Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily. (726 aa)
oxyRDNA-binding transcriptional dual regulator; Function experimentally demonstrated in the studied species; regulator; Belongs to the LysR transcriptional regulatory family. (305 aa)
dipZFragment of putative transcriptional regulator (part 1); Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (565 aa)
nsrRDNA-binding transcriptional regulator; Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity. (141 aa)
ytfERegulator of cell morphogenesis and cell wall metabolism; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. (220 aa)
pepAAminopeptidase A, a cyteinylglycinase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. (503 aa)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
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