close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
STRINGSTRING
STRING protein interaction network
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.
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:
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
rnhBRNase HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (197 aa)    
Predicted Functional Partners:
lpxB
lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
 
 
 0.995
SEQ21733.1
DNA polymerase-3 subunit beta; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of re [...]
   
 
 0.950
SEQ50934.1
NAD(P)-dependent nickel-iron dehydrogenase flavin-containing subunit.
   
   0.949
lpxA
acyl-[acyl-carrier-protein]--UDP-N- acetylglucosamine O-acyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
  
  
 0.916
rnhA
RNase HI; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
   
 
 0.890
lpxD
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3- hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
  
  
 0.866
fabZ
3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
  
  
 0.856
SEQ95997.1
Periplasmic chaperone for outer membrane proteins Skp.
       0.820
SEQ95886.1
DNA polymerase-3 subunit alpha.
  
  
 0.818
bamA
Beta-barrel assembly machine subunit BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
  
    0.816
Your Current Organism:
Amphritea atlantica
NCBI taxonomy Id: 355243
Other names: A. atlantica, Amphritea atlantica Gartner et al. 2008 emend. Jang et al. 2015, DSM 18887, LMG 24143, LMG:24143, gamma proteobacterium M41, strain M41
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.