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
lgtCatalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. ECO:0000269|PubMed:26729647, ECO:0000269|PubMed:7896715, (291 aa)    
Predicted Functional Partners:
Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product . This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation .
This protein specifically catalyzes the removal of signal peptides from prolipoproteins
Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation (PubMed:2032623, PubMed:21676878, PubMed:28885614, PubMed:28675161). Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the [...]
Master regulator of 5'-end-dependent mRNA decay . Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage . Preferentially hydrolyzes diadenosine penta-phosphate with ATP as one of the reaction products . Also able to hydrolyze diadenosine hexa- and tetra-phosphate . Has no activity on diadenosine tri-phosphate, ADP-ribose, NADH and UDP-glucose . In an RNase PH (rph) wild-type strain background, RppH is not required for maturation [...]
Specifically catalyzes the dephosphorylation of 2- phosphoglycolate (2P-Gly). Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'- phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress
Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec- independent subunit c of the F(0)ATP synthase, M13 phage procoat and the N-terminus of leader peptidase Lep. Probably in [...]
Component of the phosphoenolpyruvate-dependent nitrogen- metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr) . Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins . Enzyme I-Ntr is specific for NPr .
Signal peptidase I; Enzyme; Protein, peptide secretion; Belongs to the peptidase S26 family
Recycling of diacylglycerol produced during the turnover of membrane phospholipid
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is required to insert newly synthesized SecY [...]
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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