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' (replication factor Y); 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. (734 aa)    
Predicted Functional Partners:
ssb
Single-stranded DNA-binding protein controls activity of RecBCD nuclease; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
 
 
 
 0.930
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.
    0.911
coaBC
Coenzyme A biosynthesis bifunctional protein CoaBC; 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.
  
    0.686
CCG41680.1
Putative single-stranded-DNA-specific exonuclease recJ; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
 
     0.676
CCG41529.1
Conserved hypothetical protein; Homologs of previously reported genes of unknown function.
       0.664
pheT
Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.658
guaB
Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPDH) (IMPD); 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.
  
   0.638
pth
Peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
  
    0.618
CCG40349.1
Putative replicative DNA helicase, dnaB; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily.
   
 0.608
atpH
ATP synthase subunit delta, membrane-bound, F1 sector; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
       0.595
Your Current Organism:
Phaeospirillum molischianum
NCBI taxonomy Id: 1150626
Other names: P. molischianum DSM 120, Phaeospirillum molischianum DSM 120, Phaeospirillum molischianum str. DSM 120, Phaeospirillum molischianum strain DSM 120
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