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evgS evgS ydeO ydeO hmp hmp safA safA rpoS rpoS rpoH rpoH hdeB hdeB hdeA hdeA hdeD hdeD gadE gadE gadX gadX gadA gadA serC serC arnT arnT
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.
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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:
a 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
Your Input:
evgSHybrid sensory histidine kinase in two-component regulatory system with EvgA; Member of the two-component regulatory system EvgS/EvgA. Phosphorylates EvgA via a four-step phosphorelay in response to environmental signals. (1197 aa)
ydeOUV-inducible global regulator, EvgA-, GadE-dependent; Induces the expression of gadE and mdtEF. Could also regulate the expression of other genes involved in acid resistance. (253 aa)
hmpFused nitric oxide dioxygenase/dihydropteridine reductase 2; 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. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...] (396 aa)
safATwo-component system connector membrane protein, EvgSA to PhoQP; Connects the signal transduction between the two-component systems EvgS/EvgA and PhoQ/PhoP, by directly interacting with PhoQ and thus activating the PhoQ/PhoP system, in response to acid stress conditions; Belongs to the SafA family. (65 aa)
rpoSRNA polymerase, sigma S (sigma 38) factor; 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. (330 aa)
rpoHRNA polymerase, sigma 32 (sigma H) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quic [...] (284 aa)
hdeBAcid-resistance protein; Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. (108 aa)
hdeAStress response protein acid-resistance protein; Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non- specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA. (110 aa)
hdeDAcid-resistance membrane protein. (190 aa)
gadEGad regulon transcriptional activator; Regulates the expression of several genes involved in acid resistance. Required for the expression of gadA and gadBC, among others, regardless of media or growth conditions. Binds directly to the 20 bp GAD box found in the control regions of both loci. (175 aa)
gadXAcid resistance regulon transcriptional activator; Positively regulates the expression of about fifteen genes involved in acid resistance such as gadA, gadB and gadC. Depending on the conditions (growth phase and medium), can repress gadW. (274 aa)
gadAGlutamate decarboxylase A, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. (466 aa)
serC3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa)
arnT4-amino-4-deoxy-L-arabinose transferase; Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. (550 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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