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
DIP2345Hypothetical protein; No significant database matches. (214 aa)    
Predicted Functional Partners:
DIP2160
Modular polyketide synthase; Similar to Streptomyces verticillus polyketide synthase BlmVIII (bleomycin biosynthesis) TR:Q9FB25 (EMBL:AF210249) (1841 aa) fasta scores: E(): 1.3e-72, 27.240% id in 1931 aa, and to Streptomyces noursei nystatin biosynthesis polyketide synthase Nys TR:Q9L4W3 (EMBL:AF263912) (11096 aa) fasta scores: E(): 4e-71, 33.107% id in 882 aa, and to Amycolatopsis mediterranei rifamycin polyketide synthase TR:Q9F847 (EMBL:AF262754) (1265 aa) fasta scores: E(): 7.7e-61, 31.042% id in 902 aa.
  
 
 0.794
glgC
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
   
    0.733
DIP0896
Putative oxydoreductase; Similar to Streptomyces peucetius daunorubicin C-13 ketoreductase DnrU TR:Q9ZAU1 (EMBL:U77891) (287 aa) fasta scores: E(): 1.3e-16, 35.25% id in 278 aa.
   
 
 0.732
DIP2298
Putative oxidoreductase; Similar to Bacillus subtilis hypothetical oxidoreductase YoxD SWALL:YOXD_BACSU (SWALL:P14802) (238 aa) fasta scores: E(): 2.2e-09, 28.57% id in 231 aa, and to Rhizobium sp putative short-chain type dehydrogenase/reductase SWALL:Y4EK_RHISN (SWALL:P55434) (248 aa) fasta scores: E(): 2.3e-09, 30% id in 210 aa.
   
 
 0.732
DIP2344
Conserved hypothetical protein; Weakly similar to many eg. Escherichia coli unknown protein from 2d-page YeaD or B1780 SWALL:UP08_ECOLI (SWALL:P39173) (294 aa) fasta scores: E(): 0.00013, 28.74% id in 247 aa.
       0.578
rpoA
DNA-directed RNA polymerase alpha chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.556
rpoZ
Putative DNA-directed RNA polymerase omega chain; 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.
   
   0.549
rpoB
DNA-directed RNA polymerase beta chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.455
DIP1653
Putative exported protein.
  
 
 0.446
DIP1859
DeaD/DeaH family helicase; Similar to Escherichia coli probable ATP-dependent helicase DinG SW:DING_ECOLI (P27296) (716 aa) fasta scores: E(): 5.6e-15, 27.57% id in 689 aa, and to Mycobacterium tuberculosis probable ATP-dependent helicase DinG homologue Rv1329c SW:DING_MYCTU (Q10640) (664 aa) fasta scores: E(): 2.2e-131, 55.84% id in 659 aa.
    
   0.432
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
Server load: medium (42%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.