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
yjkBPutative phosphate ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the ABC transporter superfamily. (250 aa)    
Predicted Functional Partners:
yjkA
Putative ABC transporter (permease); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
    0.944
appD
Oligopeptide ABC transporter (ATP-binding protein); This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for energy coupling to the transport system; Belongs to the ABC transporter superfamily.
 
     
0.896
yheI
Probable multidrug resistance ABC transporter ATP-binding/permease protein YheI; Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily.
 
     
0.895
pstC
Phosphate ABC transporter (permease); Part of the binding-protein-dependent transport system YqgGHIJK. Probably responsible for the translocation of the substrate across the membrane (By similarity); Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
  
 0.881
pstA
Phosphate ABC transporter (permease); Part of the binding-protein-dependent transport system YqgGHIJK. Probably responsible for the translocation of the substrate across the membrane (By similarity); Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
  
 0.877
pstS
Phosphate ABC transporter (binding lipoprotein); Part of the ABC transporter complex PstSACB involved in phosphate import.
  
 0.842
yknZ
Putative permease; Part of an unusual four-component transporter, which is required for protection against the killing factor SdpC (sporulation- delaying protein).
 
    
 0.778
ecsA
ABC transporter (ATP-binding protein); Has a role in exoprotein production, sporulation and competence.
 
   
0.733
yjlA
Putative permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
  
    0.655
ythP
Putative ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the ABC transporter superfamily.
 
   
0.650
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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