STRINGSTRING
STRING protein interaction network
Nodes:
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:
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
Others
textmining
co-expression
protein homology
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[Homology]
Score
iraMInhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during magnesium starvation. May also be involved in the early steps of isoprenoid biosynthesis, possibly through its role as RssB regulator. (107 aa)    
Predicted Functional Partners:
rssB
Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co- degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation. In stationary phase, could also act as an anti-sigma factor and reduce the ability of RpoS to activate gene expression. Is also involved in the regulation of the mRNA polyadenylation pathway during stationary phase, probably by maintaining the association of PcnB with the degradosome. [...]
    
 
 0.987
iraD
Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway
      
 0.927
iraP
Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS especially during phosphate starvation, but also in stationary phase and during nitrogen starvation. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway
      
 0.900
rpoS
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. Controls, positively or negatively, the expression of several hundred genes, which are mainly involved in metabolism, transport, regulation and stress management. ECO:0000269|PubMed:15558318, ECO:0000269|PubMed:15716429, ECO:0000269|PubMed:16511888, ECO:0000269|PubMed:21398637,
      
 0.822
yggT
Uncharacterized protein YggT; Conserved hypothetical integral membrane protein
      
 0.648
appY
Induces the synthesis of acid phosphatase (AppA) and several other polypeptides (such as AppBC) during the deceleration phase of growth. It also acts as a transcriptional repressor for one group of proteins that are synthesized preferentially in exponential growth and for one group synthesized only in the stationary phase. Also involved in the stabilization of the sigma stress factor RpoS during stress conditions
      
 0.616
idi
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)
      
 0.561
elbB
Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate . However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate .
      
 0.560
phoQ
Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP- repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By [...]
      
 0.520
yigA
annotation not available
      
 0.520
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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