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
ybeDannotation not available (87 aa)    
Predicted Functional Partners:
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalyzes cross-linking of the peptidoglycan cell wall . Responsible for the determination of the rod shape of the cell . Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth .
Peptidoglycan polymerase that is essential for cell wall elongation . Also required for the maintenance of the rod cell shape . Functions probably in conjunction with the penicillin-binding protein 2 (mrdA) (PubMed:2644207, PubMed:27643381)
Belongs to the PhoH family
Specifically methylates the adenine in position 2030 of 23S rRNA. Nascent 23S rRNA seems to be the natural substrate. Appears to be not necessary for ribosome assembly. Required for the utilization of extracellular DNA as the sole source of carbon and energy . ECO:0000269|PubMed:11591672, ECO:0000269|PubMed:16707682,
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit
Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:8662828,
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate
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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