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
ORL30266.1Pyridoxal-dependent decarboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. (488 aa)    
Predicted Functional Partners:
ORL30267.1
MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.959
glsA
Glutaminase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family.
  
  
 0.560
nnrE
Bifunctional ADP-dependent (S)-NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-spec [...]
  
 
 0.558
dnaJ
Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]
   
 
 0.536
dnaJ-2
Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]
   
 
 0.536
ORL35529.1
Exopolyphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.532
ORL35546.1
Type VII secretion-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.532
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.532
ORL33622.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.
   
 0.532
ORL33633.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.532
Your Current Organism:
Rhodococcus hoagii
NCBI taxonomy Id: 43767
Other names: ATCC 14887 [[Nocardia restricta]], ATCC 25729 [[Rhodococcus equi]], ATCC 6939 [[Rhodococcus equi]], ATCC 7005 [[Corynebacterium hoagii]], Bacillus hoagii, CCUG 17758 [[Nocardia restricta]], CCUG 20991 [[Corynebacterium hoagii]], CCUG 892 [[Rhodococcus equi]], CIP 54.72 [[Rhodococcus equi]], CIP 81.17 [[Corynebacterium hoagii]], Corynebacterium (pyogenes) equi roseum, Corynebacterium hoagii, Corynebacterium magnusson-holth, Corynebacterium purulentus, Corynebacterium pyogenes (equi), DSM 20295 [[Corynebacterium hoagii]], DSM 20307 [[Rhodococcus equi]], DSM 43199 [[Nocardia restricta]], HAMBI 2061 [[Rhodococcus equi]], IFO 14956 [[Rhodococcus equi]], JCM 3209 [[Rhodococcus equi]], JCM 3223 [[Nocardia restricta]], LMG 18452 [[Rhodococcus equi]], LMG 7335 [[Nocardia restricta]], LMG:18452 [[Rhodococcus equi]], LMG:7335 [[Nocardia restricta]], Mycobacterium equi, Mycobacterium restrictum, NBRC 101255 [[Rhodococcus equi]], NBRC 103062 [[Corynebacterium hoagii]], NBRC 14956 [[Rhodococcus equi]], NCTC 10673 [[Corynebacterium hoagii]], NRRL B-16538 [[Rhodococcus equi]], Nocardia restricta, Prescottella equi, Prescottia equi, Proactinomyces restrictus, R. hoagii, Rhodococcus equi, VKM Ac-953 [[Rhodococcus equi]]
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