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
DIP1373Hypothetical protein; No significant database matches. (61 aa)    
Predicted Functional Partners:
secF
Putative protein export membrane protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
       0.773
secD
Putative protein export membrane protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
       0.773
DIP1374
Conserved hypothetical protein; Similar to Corynebacterium glutamicum hypothetical 13.5 kDa protein SWALL:Q9AE08 (EMBL:AF038651) (121 aa) fasta scores: E(): 7.2e-10, 34.83% id in 89 aa, and to Mycobacterium tuberculosis hypothetical 13.0 kDa protein Rv2588c precursor or MT2665 or MTCY227.13 SWALL:YP88_MYCTU (SWALL:Q50633) (115 aa) fasta scores: E(): 5.9e-05, 37.77% id in 90 aa.
       0.645
ruvB
Holliday junction DNA-helicase; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
       0.645
ruvA
Holliday junction DNA-helicase; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
       0.612
DIP1370
Conserved hypothetical protein; Similar to Corynebacterium glutamicum dipeptide-binding protein DciaE SWALL:O87329 (EMBL:AF038651) (502 aa) fasta scores: E(): 4e-83, 48.61% id in 434 aa, and to Mycobacterium tuberculosis hypothetical lipoprotein Rv2585c precursor or MT2662 or MTCY227.16 SWALL:YP85_MYCTU (SWALL:Q50636) (557 aa) fasta scores: E(): 7.1e-30, 29.09% id in 574 aa.
       0.576
ruvC
Crossover junction endodeoxyribonuclease; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
       0.521
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
       0.460
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
Server load: low (40%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.