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
AEM79895.1PFAM: Peptidyl-prolyl cis-trans isomerase, PpiC-type; KEGG: tbo:Thebr_0176 PpiC-type peptidyl-prolyl cis-trans isomerase. (301 aa)    
Predicted Functional Partners:
mfd
Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
     
 0.712
AEM79897.1
KEGG: thx:Thet_2334 hypothetical protein.
       0.678
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.
     
 0.657
AEM79894.1
Stage V sporulation protein T; KEGG: tmt:Tmath_2137 transcriptional regulator, AbrB family; TIGRFAM: Sporulation stage V, protein T; Transcription regulator AbrB; PFAM: Transcription regulator AbrB/SpoV, predicted.
     
 0.647
AEM77965.1
KEGG: tbo:Thebr_1890 pyruvate ferredoxin/flavodoxin oxidoreductase; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
   
 
 0.627
AEM78246.1
PFAM: Outer membrane protein, OmpA/MotB, C-terminal; KEGG: tit:Thit_0659 OmpA/MotB domain protein.
 
   
 0.619
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.
  
 
 0.551
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
 
  
 0.515
tig
Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.
  
  
 0.492
clpP
ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
 
 
 0.485
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.