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
ycaLPutative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process (254 aa)    
Predicted Functional Partners:
Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions
Putative heat shock chaperone; Uncharacterized protein YrhB; Factor; Adaptations, atypical conditions
Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors
Hsp70 chaperone family protein; Belongs to the heat shock protein 70 family
Hydrogenase 2-specific chaperone; Hydrogenase-2 operon protein HybE; Member of hyb operon
Redox enzyme maturation protein (remp) chaperone for ycdx; Acts as a chaperone that increases YcdX activity, maybe by facilitating the correct insertion of the zinc ions into the catalytic site of YcdX. Involved in the swarming motility process
Hsp70 family chaperone Hsc62; Probable chaperone. Has ATPase activity. Not stimulated by DnaJ
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate
Hexameric aaa+ moxr family atpase, putative molecular chaperone; Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone
Required for translation of most natural mRNAs except for leaderless mRNA Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated . Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides . Has a preference for polypyrimidine tracts . Negatively autoregulates its own translation . In case of infection by ba [...]
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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