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
htpKRegulator of quality control; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type r: regulator. (233 aa)    
Predicted Functional Partners:
htpX
Membrane protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the peptidase M48B family.
     
 0.852
rok
Repressor of comK; Repressor of comK, the master regulator of competence development. Overexpression seems to be lethal. Represses at least 20 genes that specify membrane- localized and secreted proteins, including some that encode products with antibiotic activity. Binds to many AT-rich sites in the chromosome, many of which are known or thought to derive from horizontal gene transfer; helps keep mobile element ICEBs1 quiescent in the genome. Binds to its own promoter and is thus probably autoregulatory.
      
 0.576
sspD
Small acid-soluble spore protein (alpha/beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light.
       0.494
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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