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
prmARibosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. (314 aa)    
Predicted Functional Partners:
rplK
Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
    
 
 0.840
KRM41214.1
GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
 
     0.820
dtd
D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.
       0.771
KRM41213.1
Hypothetical protein.
       0.703
dnaJ
Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...]
  
  
 0.631
KRM41211.1
Transcriptional regulator; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily.
       0.583
KRM38058.1
NOL1 NOP2 sun family protein.
  
  
 0.581
rsmG
16S rRNA methyltransferase GidB; Specifically methylates the N7 position of a guanine in 16S rRNA; Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.
 
  
 0.577
mutS2
DNA mismatch repair protein MutS; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.
 
     0.532
KRM41010.1
tRNA-dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family.
    
 0.518
Your Current Organism:
Lactobacillus hamsteri
NCBI taxonomy Id: 1423754
Other names: L. hamsteri DSM 5661 = JCM 6256, Lactobacillus hamsteri DSM 5661, Lactobacillus hamsteri DSM 5661 = JCM 6256, Lactobacillus hamsteri JCM 6256, Lactobacillus hamsteri JCM 6256 = DSM 5661
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.