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
ydiBATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. (149 aa)    
Predicted Functional Partners:
ydiC
Universal bacterial protein YeaZ; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.997
gcp
O-sialoglycoprotein endopeptidase; 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.
 
 
 0.988
rimI
Alanine acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.891
coaD
Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family.
     
 0.538
alrA
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
  
 
  0.532
alr2
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
  
 
  0.532
recR
Recombinase RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
 
     0.500
ald2
Alanine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the AlaDH/PNT family.
    
  0.449
glmU
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.
    
  0.441
dnaN
DNA polymerase III subunit beta; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
  
    0.440
Your Current Organism:
Staphylococcus microti
NCBI taxonomy Id: 569857
Other names: CCM 4903, CCUG 55861, DSM 22147, NCTC 13832, S. microti, Staphylococcus microti Novakova et al. 2010, Staphylococcus sp. CCM 4903, Staphylococcus sp. CCM 4904, strain 4005-LJ(m)
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