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
ydjANAD(P) nitroreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (183 aa)    
Predicted Functional Partners:
topB
DNA topoisomerase III; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA su [...]
 
   
 0.752
selD
Selenide,water dikinase SelD; Synthesizes selenophosphate from selenide and ATP.
  
    0.749
birA
biotin--[acetyl-CoA-carboxylase] synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
    0.678
AMG69353.1
Ribosomal protein S12 methylthiotransferase accessory factor YcaO; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.667
AMG70127.1
SppA; catalyzes the degradation of cleaved signal peptides; essential to maintain secretion of mature proteins across the membrane; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.532
AMG68924.1
With YgfM and YgfN forms a selenate reductase, which seems to catalyze the reduction of selenate to selenite; YgfK mutants are unable to reduce selenate; involved in purine salvage process; seems to act as an oxidoreductase, but sequence similarity suggests it is a dihydrothymine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.507
AMG69911.1
Long-chain fatty acid--CoA ligase; Activates fatty acids by binding to coenzyme A; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
   0.484
yadH
ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.445
AMG69243.1
CAAX protease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.443
AMG70813.1
Multidrug ABC transporter ATP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.436
Your Current Organism:
Morganella morganii
NCBI taxonomy Id: 582
Other names: ATCC 25830, ATCC 8076H, Bacillus morgani, CCUG 6328, CIP 103763, CIP A231, DSM 30164, IFO 3848, LMG 7874, LMG:7874, M. morganii, NBRC 3848, NCCB 73065, NCIB 235, NCIB:235, NCTC 235, Organism N 1, Proteus morganii, Salmonella morgani
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