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STRINGSTRING
WL94_35555 protein (Burkholderia cepacia) - STRING interaction network
"WL94_35555" - annotation not available in Burkholderia cepacia
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 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
WL94_35555annotation not available (184 aa)    
Predicted Functional Partners:
mauD
mauD- methylamine dehydrogenase accessory protein MauD (223 aa)
 
      0.980
WL94_35560
annotation not available (385 aa)
 
     
  0.977
aauA
annotation not available (181 aa)
 
     
  0.947
DM42_5690
annotation not available (166 aa)
 
          0.921
DM42_5691
annotation not available (155 aa)
 
          0.912
DM42_5685
annotation not available (320 aa)
 
          0.684
WI67_18995
annotation not available (339 aa)
   
          0.652
WL94_01560
annotation not available (164 aa)
   
          0.651
secY
Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (425 aa)
     
 
  0.649
WL94_11045
annotation not available (465 aa)
   
          0.649
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia, Burkholderia cepacia genomovar I, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
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