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
pepPPeptidase M24; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M24B family. (356 aa)    
Predicted Functional Partners:
efp
Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
  
 
 0.896
KIX91567.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.816
pepT_2
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.664
accC_2
acetyl-CoA carboxylase biotin carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 
 0.579
KIX91568.1
Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.575
guaB
Inosine-5-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
   
   0.563
guaC
Guanosine 5'-monophosphate oxidoreductase; Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides; Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
    
   0.558
pepT_1
Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family.
  
 
 0.547
ileS
isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
 
 
 0.528
accB_2
acetyl-CoA carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
       0.515
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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