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
apaGCo2+/Mg2+ efflux protein ApaG; Derived by automated computational analysis using gene prediction method: Protein Homology. (125 aa)    
Predicted Functional Partners:
ksgA
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))- dimethyltransferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
  
  
 0.947
apaH
Bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family.
  
  
 0.930
surA
Peptidylprolyl isomerase SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
     
 0.833
pdxA
4-hydroxythreonine-4-phosphate dehydrogenase PdxA; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
  
  
 0.832
HA50_02010
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.659
HA50_16635
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.659
lptD
LPS assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
  
    0.657
djlA
Molecular chaperone DjlA; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.
       0.479
nuoC
NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 
 0.402
Your Current Organism:
Pantoea cypripedii
NCBI taxonomy Id: 55209
Other names: ATCC 29267, Bacillus cypripedii, CFBP 3613, CIP 105195, DSM 3873, Erwinia carotovora var. cypripedii, Erwinia cypripedii, Erwinia cyrpipedii, LMG 2655, LMG 2657, LMG:2655, LMG:2657, NCPPB 3004, P. cypripedii, Pectobacterium cypripedii
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.