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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DR97_1282annotation not available (959 aa)    
Predicted Functional Partners:
DR97_1286
annotation not available
 
 
 0.961
DR97_1287
annotation not available
 
 0.951
DR97_1137
annotation not available
 
 0.889
DR97_1285
annotation not available
 
     0.807
rpoZ
Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).
    
 0.773
polA
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity
  
 0.773
rpoB
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 0.709
aphB
Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine and N-acetylcadaverine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. Shows nearly no activity against N(1)- acetylspermine and N(1)-acetylspermidine. Can also hydrolyze artificial trifluoroacetylated lysine-derivative, and to a lesser extent, acetylated lysine-derivative
   
 0.705
DR97_4095
Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines
   
 0.705
aphA
Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine, N-acetylcadaverine, N(1)-acetylspermine and N(1)- acetylspermidine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. In vitro, can also hydrolyze artificial trifluoroacetylated and acetylated lysine-derivatives.
   
 0.705
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
Server load: low (1%) [HD]