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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
priAPrimosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. (732 aa)    
Predicted Functional Partners:
fmt
Methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
    0.936
AEM78884.1
Phosphopantothenoylcysteine decarboxylase/phosphopantothenate/cysteine ligase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family.
  
    0.870
AEM78878.1
Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
    0.824
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
  
    0.822
AEM78876.1
KEGG: tbo:Thebr_1343 protein phosphatase 2C-like protein; PFAM: Protein phosphatase 2C, N-terminal; SMART: Protein phosphatase 2C-related.
  
    0.816
rlmN
Ribosomal RNA large subunit methyltransferase N; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
  
    0.812
AEM78880.1
PFAM: Protein of unknown function DUF116; KEGG: tbo:Thebr_1347 hypothetical protein.
       0.785
rsgA
Ribosome biogenesis GTPase RsgA; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit; Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.
 
     0.774
AEM78342.1
PFAM: Primosome PriB/single-strand DNA-binding; KEGG: thx:Thet_0747 single-strand-binding protein/primosomal replication protein N.
   
 
 0.760
AEM78879.1
PFAM: Peptidase, membrane zinc metallopeptidase, putative; KEGG: tmt:Tmath_1360 peptidase membrane zinc metallopeptidase putative.
       0.757
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.