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
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. (699 aa)    
Predicted Functional Partners:
Acel_1291
Phosphopantothenate-cysteine ligase / Phosphopantothenoylcysteine decarboxylase; 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.
  
    0.876
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.
    0.790
Acel_2132
TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; KEGG: tfu:Tfu_3094 single-strand binding protein.
    
 
 0.776
whiA
Protein of unknown function DUF199; Involved in cell division and chromosome segregation.
 
     0.768
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
       0.754
rpoZ
DNA-directed RNA polymerase subunit omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
 
     0.753
Acel_1620
TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; KEGG: tfu:Tfu_3094 single-strand binding protein.
    
 
 0.733
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
  
  
 0.715
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: sma:SAV6743 putative phenylalanyl-tRNA synthetase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.656
Acel_1277
PFAM: Fmu (Sun) domain protein; NusB/RsmB/TIM44; KEGG: sma:SAV6878 putative RNA-binding Sun protein; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
 
    0.613
Your Current Organism:
Acidothermus cellulolyticus
NCBI taxonomy Id: 351607
Other names: A. cellulolyticus 11B, Acidothermus cellulolyticus 11B, Acidothermus cellulolyticus str. 11B, Acidothermus cellulolyticus strain 11B
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.