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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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ttrCTetrathionate reductase complex, subunit C; Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrC probably anchors TtrA and TtrB to the periplasmic face of the cytoplasmic membrane. May transfer electrons from membrane quinol to TtrB. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut. Belongs to the NrfD family. (340 aa)    
Predicted Functional Partners:
ttrA
Tetrathionate reductase complex, subunit A; Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrA is the catalytic subunit. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
 
 0.999
ttrB
Tetrathionate reductase complex, subunit B; Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
 
 
 0.999
ttrS
Tetrathionate reductase complex: sensory transduction histidine kinase; Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue in response to tetrathionate, and transfers its phosphate group to TtrR. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
 
   
 0.986
ttrR
Tetrathionate reductase complex: response regulator; Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Positively regulates transcription of the ttrBCA operon. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
 
  
 0.976
phsC
Hydrogen sulfide production membrane anchoring protein; Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsC subunit anchors the complex to the membrane and contains the site for menaquinol oxidation.
  
 
 0.971
phsA
Hydrogen sulfide production membrane anchoring protein; Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsA subunit contains the active site molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor.
 
 
 0.951
phsB
Hydrogen sulfide production iron-sulfur subunit; Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsB subunit transfers electrons between PhsC and PhsA.
  
 
 0.924
sseA-2
Similar to E. coli putative thiosulfate sulfurtransferase (AAC75574.1); Blastp hit to AAC75574.1 (334 aa), 80% identity in aa 54 - 332.
  
 
  0.911
glpE
Thiosulfate/cyanide sulfurtransferase; Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
    
  0.900
misL
Putative autotransported protein; Pathogenicity island encoded protein: SPI3; MisL (gi|4324610).
  
  
 0.850
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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