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.
query proteins and first shell of interactors
second shell of interactors
proteins of unknown 3D structure
a 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.
|yncJ||Uncharacterized protein. (76 aa)|| |
Predicted Functional Partners:
DUF533 family inner membrane protein.
| || || || || || ||0.804
Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. May act as a zinc sensor that controls, via c-di-GMP, post-translational events. Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...]
| || || || || || || ||0.683
DUF1471 family periplasmic protein.
| || || || || || ||0.659
Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...]
| || || || || || ||0.539
| || || || || || || ||0.524
mRNA interferase toxin of the HicAB toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-independent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome (after 90 minutes) by subsequent expression of antitoxin HicB. Overexpression causes cleavage of a number of mRNAs and tmRNA, in a translation-independent fashion, suggesting this is an mRNA interferase. mRNA interferases play a role in bacterial persistence to antibiotics ; Belongs t [...]
| || || || || || || ||0.478
L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp.
| || || || || || ||0.460
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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