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
gatBaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (480 aa)    
Predicted Functional Partners:
gatA
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
 
 0.999
GatC
KEGG: stw:Y1U_C1523 1.9e-47 glutamyl-tRNA Gln amidotransferase subunit C; K02435 aspartyl-tRNA(Asn)/glutamyl-tRNA (Gln) amidotransferase subunit C.
 
 0.999
aspS
aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 0.990
gltX
glutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.989
asnS
asparagine--tRNA ligase; KEGG: stj:SALIVA_1224 7.9e-239 asnS; asparaginyl-tRNA synthetase (Asparagine--tRNA ligase) (AsnRS); Psort location: Cytoplasmic, score: 10.00.
  
 0.988
KXU58537.1
Amidase; KEGG: ssr:SALIVB_1013 6.7e-226 nylA; 6-aminohexanoate-cyclic-dimer hydrolase; Psort location: Cytoplasmic, score: 9.26.
 
 0.987
guaA
GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.833
metG
methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
  
 
 0.740
PheT
KEGG: stf:Ssal_00892 0. pheT; phenylalanyl-tRNA synthetase subunit beta; K01890 phenylalanyl-tRNA synthetase beta chain; Psort location: Cytoplasmic, score: 9.97.
  
  
 0.698
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
  
  
 0.614
Your Current Organism:
Streptococcus salivarius
NCBI taxonomy Id: 1304
Other names: ATCC 7073, CCUG 11878, CCUG 17825, CCUG 50207, CIP 102503, DSM 20560, JCM 5707, LMG 11489, LMG:11489, NCIMB 701779, NCTC 8618, S. salivarius, Streptococcus salivarius subsp. salivarius, Streptococcus sp. FStet12, Streptococcus sp. HSISS4
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