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
yxeIPenicillin V acylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase C59 family. (328 aa)    
Predicted Functional Partners:
penP
Beta-lactamase precursor; This protein is a beta-lactamase with a substrate specificity for penicillins.
     
  0.900
yxeJ
Hypothetical protein; Evidence 5: No homology to any previously reported sequences.
  
    0.774
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 [...]
   
  
 0.701
yxeH
Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
    0.481
yxeK
Putative monooxygenase; Probably catalyzes the oxygenation of the 2-position of the succinyl moiety of N-acetyl-S-(2-succino)cysteine, causing a spontaneous elimination reaction of the resulting hemithioketal that generates oxaloacetate and N-acetylcysteine (NAC). Is involved in a S- (2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family.
       0.454
yxeL
Putative acetyltransferase; Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation; Belongs to the acetyltransferase family.
  
    0.451
yxeG
Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
  
    0.440
bmrR
Transcriptional regulator (MerR family); Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer.
 
    0.438
yxeF
Lipocalin-like protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure.
  
    0.409
yxeM
Putative ABC transporter (binding lipoprotein); Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine; Belongs to the bacterial solute-binding protein 3 family.
       0.407
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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