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
yckBL-cystine transport system substrate-binding protein; Probably part of a binding-protein-dependent transport system (287 aa)    
Predicted Functional Partners:
yckA
Amino acid abc transporter permease protein ycka; Part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane (By similarity)
 0.994
tcyC
L-cystine transport system atp-binding protein; Part of the ABC transporter complex TcyABC involved in L- cystine import. Responsible for energy coupling to the transport system (Probable)
 
 0.977
tcyB
L-cystine transport system permease protein tcyb; Part of the ABC transporter complex TcyABC involved in L- cystine import. Probably responsible for the translocation of the substrate across the membrane (Probable)
 0.965
mcpC
Methyl-accepting chemotaxis protein mcpc; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a m [...]
    
 
 0.930
artR
Arginine/lysine/histidine transport system atp-binding protein; Part of a binding-protein-dependent transport system for arginine. Probably responsible for energy coupling to the transport system
 
 
 0.867
glnQ
Aspartate/glutamate/glutamine transport system atp-binding protein; Part of the ABC transporter complex GlnHMPQ involved in glutamine transport. Probably responsible for energy coupling to the transport system (By similarity)
 
 
 0.851
yxeO
Putative s-methylcysteine transport system atp-binding protein; Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine. Responsible for energy coupling to the transport system (Probable)
 
 
 0.844
tcyN
Sulfur-containing amino-acid abc transporter (atp-binding protein); Part of the ABC transporter complex TcyJKLMN involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). Is also involved in cystathionine, djenkolate, and S- methylcysteine transport
 
 
 0.841
tcyA
Cystine abc transporter (substrate-binding lipoprotein); Part of the ABC transporter complex TcyABC involved in L- cystine import
  
  
0.835
artQ
Arginine/lysine/histidine transport system permease protein; Part of a binding-protein-dependent transport system for arginine. Probably responsible for the translocation of the substrate across the membrane
 
 0.730
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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