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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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mdrMultidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. (512 aa)    
Predicted Functional Partners:
blt
Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family.
  
   
 0.944
bmrA
Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
   
  
 0.907
norM
MatE Na+-driven efflux family protein; Multidrug efflux pump; Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
   
  
 0.761
ebrA
Small multidrug resistance efflux transporter; Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity).
      
 0.717
yfiL
Putative ABC transporter (ATP-binding protein); Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes. Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for energy coupling to the transport system. Also mediates KinC-dependent biofilm morphology.
      
 0.713
yvmA
Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
  
    0.671
ycgE
Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
  
    0.606
ebrB
Small multidrug efflux transporter; Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity).
      
 0.569
fosB
Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
      
 0.566
mapB
Methionine aminopeptidase B; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
      
 0.519
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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