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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
hslOChaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. (288 aa)    
Predicted Functional Partners:
NifR
TIM-barrel protein, nifR3 family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family.
  
  
 0.825
KXU57758.1
S4 domain protein; KEGG: hiq:CGSHiGG_06085 1.9e-06 glucose-6-phosphate 1-dehydrogenase K04762; Psort location: Cytoplasmic, score: 8.96.
  
  
 0.774
KXU59402.1
Hypothetical protein.
       0.564
grpE
Co-chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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-depend [...]
   
  
 0.555
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.506
dnaJ
Chaperone protein 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, D [...]
  
  
 0.483
AdcC1
ABC transporter, ATP-binding protein; KEGG: ssr:SALIVB_0205 7.5e-124 adcC; zinc (Zn2+) ABC uptake transporter ATP-binding protein; K09817 zinc transport system ATP-binding protein.
       0.481
KXU59399.1
KEGG: ppr:PBPRA0481 7.0e-06 MarR family transcriptional regulator; K03828 putative acetyltransferase; Psort location: Cytoplasmic, score: 8.96.
       0.481
KXU59404.1
KEGG: llk:LLKF_0402 6.4e-134 optD; peptide ABC transporter ATP-binding protein K15583; Psort location: CytoplasmicMembrane, score: 10.00.
   
   0.464
Fbp
Fibronectin-binding domain protein; KEGG: edi:EDI_341030 0.0081 intracellular protein transport protein USO1; Psort location: Cytoplasmic, score: 8.96.
  
     0.447
Your Current Organism:
Streptococcus salivarius
NCBI taxonomy Id: 1304
Other names: ATCC 7073, CCUG 11878, CCUG 17825, CCUG 50207, CIP 102503, DSM 20560, JCM 5707, LMG 11489, LMG:11489, NCIMB 701779, NCTC 8618, S. salivarius, Streptococcus salivarius subsp. salivarius, Streptococcus sp. FStet12, Streptococcus sp. HSISS4
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