STRING protein interaction network
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
erpAIron-sulfur cluster insertion protein erpa; 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 (114 aa)    
Predicted Functional Partners:
Nitrogen fixation protein nifu and related proteins; 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
Fe/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
(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using flavodoxin as the reducing agent
Rrf2 family transcriptional regulator, iron-sulfur cluster assembly transcription factor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. Transcriptional repressor of the iscRSUA operon, which is involved in the assembly of Fe-S clusters into Fe-S proteins. In its apoform, under conditions of oxidative stress or iron deprivation, it activates the suf operon, which is a second operon involved in the assembly of Fe-S clusters. Represses its own transcription as well as that of toxin rnlA
Component 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
Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters
Hsca 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
Dnak-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
Iron-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
4-hydroxy-3-methylbut-2-enyl diphosphate reductase, 4Fe-4S protein; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis In vitro, can also hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 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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