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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ANK63170.1Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (155 aa)    
Predicted Functional Partners:
metE
5-methyltetrahydropteroyltriglutamate-- homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
     
  0.900
ANK62011.1
O-acetylhomoserine aminocarboxypropyltransferase; Catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.900
ANK62522.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
     
  0.900
ANK62636.1
O-acetylhomoserine aminocarboxypropyltransferase; Catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.900
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
     
  0.900
ezrA
Selenide, water dikinase; Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization; Belongs to the EzrA family.
       0.649
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
       0.562
valS
valine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
     
 0.510
leuD
3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
      0.483
thiI
tRNA sulfurtransferase ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
       0.445
Your Current Organism:
Lactobacillus backii
NCBI taxonomy Id: 375175
Other names: DSM 18080, JCM 18665, L. backii, LMG 23555, LMG:23555, Lactobacillus backi, Lactobacillus backii Tohno et al. 2013, strain L1062
Server load: low (22%) [HD]