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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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co-expression
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gene co-occurrence
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lmrBEfflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. (479 aa)    
Predicted Functional Partners:
lmrA
Transcriptional repressor of lmrAB and yxaGH operons; Acts as repressor of the lincomycin-resistance (lmrAB) and yxaGH operons.
 
  
 0.988
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.
  
  
 0.825
bmr
Multidrug-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.
  
   
 0.799
ykkD
Efflux transporter; Probably involved in guanidinium transport. In vitro, confers resistance to a broad range of toxic compounds such as cationic dyes, neutral and anionic antimicrobials.
   
  
 0.753
ykkC
Efflux transporter; Probably involved in guanidinium transport. In vitro, confers resistance to a broad range of toxic compounds such as cationic dyes, neutral and anionic antimicrobials.
   
  
 0.751
vmlR
ATP-binding cassette efflux transporter; Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation. Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic [...]
      
 0.714
tmrB
ATP-binding tunicamycin resistance protein; Involved in the resistance to tunicamycin. Binds ATP.
      
 0.713
ywfA
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
qdoR
Transcriptional regulator; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type r: regulator.
 
  
 0.668
mprF
Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...]
   
  
 0.652
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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