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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
ybaKPutative alkylated deoxynucleotide triphosphohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (147 aa)    
Predicted Functional Partners:
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
      
 0.850
cwlD
N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.
  
  
 0.837
rsmB
RNA-binding Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
      
 0.680
hisZ
histidyl-tRNA synthetase-like component of ATP phophoribosyltransferase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
      
 0.632
coiA
Protein involved in establishment of DNA transport in competence; Required for optimal transformation.
   
  
 0.621
yydA
Conserved hypothetical protein; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family.
      
 0.568
pdaA
Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.
   
  
 0.501
salA
Mrp family regulator; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.
       0.497
rsmE
Methylase of U1498 in 16S rRNA; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
      
 0.487
ybaJ
Putative methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the methyltransferase superfamily.
       0.452
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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