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
EHL97976.1Hydrolase, P-loop family; KEGG: rer:RER_19160 4.9e-17 ATPase K06925; Psort location: Cytoplasmic, score: 9.97. (146 aa)    
Predicted Functional Partners:
tsaD
Putative glycoprotease GCP; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family.
 
 0.979
EHL96656.1
Universal bacterial protein YeaZ; KEGG: sgo:SGO_0221 6.8e-43 glycoprotein endopeptidase K01409.
 
 
 0.977
EHL97975.1
Acetyltransferase, GNAT family; KEGG: tte:TTE0782 2.3e-12 wecD2; histone acetyltransferase HPA2-like acetyltransferase; K00680.
     
 0.851
EHL97828.1
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
 
 
 0.816
trmD
tRNA (guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
 
   
 0.664
glmU
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain.
    
  0.623
smpB
SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...]
 
     0.614
EHL97978.1
Phosphate acetyltransferase; KEGG: lbr:LVIS_0674 1.9e-109 eutD; phosphotransacetylase; K00625 phosphate acetyltransferase; Psort location: Cytoplasmic, score: 9.26.
  
    0.591
EHL97977.1
Hypothetical protein.
       0.536
polA
DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
 
     0.510
Your Current Organism:
Lactobacillus parafarraginis
NCBI taxonomy Id: 797515
Other names: L. parafarraginis F0439, Lactobacillus parafarraginis F0439, Lactobacillus parafarraginis str. F0439, Lactobacillus parafarraginis strain F0439, Lactobacillus sp. oral taxon 418 str. F0439
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.