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
RP433SUCCINYL-COA SYNTHETASE BETA CHAIN (sucC); Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (386 aa)    
Predicted Functional Partners:
RP432
SUCCINYL-COA LIGASE (sucD); Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
 0.999
RP128
SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT (sdhA).
  
 0.992
RP126
SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT (sdhC); Membrane-anchoring subunit of succinate dehydrogenase (SDH).
  
 
 0.991
RP044
SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN (sdhB); Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
  
 0.990
RP127
SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN (sdhD); Membrane-anchoring subunit of succinate dehydrogenase (SDH).
  
 
 0.990
RP179
DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT (sucB); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
  
 0.987
RP180
2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT (sucA); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
 
 
 0.987
RP530
DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT (pdhC); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
  
 0.975
RP844
CITRATE SYNTHASE (gltA).
  
 
 0.972
RP354
NADH DEHYDROGENASE I CHAIN D (nuoD); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
  
 
 0.898
Your Current Organism:
Rickettsia prowazekii
NCBI taxonomy Id: 272947
Other names: R. prowazekii str. Madrid E, Rickettsia prowazekii str. Madrid E, Rickettsia prowazekii strain Madrid E
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.