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qrcC protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"qrcC" - Menaquinone reductase, iron-sulfur cluster-binding subunit in Desulfovibrio vulgaris Hildenborough
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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qrcCMenaquinone reductase, iron-sulfur cluster-binding subunit; Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. QrcC is an electron-transferring subunit; its cubane iron sulfur clusters form a pathway for electron transfer between the hemes of QrcA and th [...] (255 aa)    
Predicted Functional Partners:
qrcB
Menaquinone reductase, molybdopterin-binding-like subunit; Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. The function of the QrcB subunit is unknown; in the absence of a catalytic site, it may provide a structural scaffold for the other subunits; Be [...] (691 aa)
 
  0.996
qrcD
Menaquinone reductase, integral membrane subunit; Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. The QrcD subunit anchors the protein complex to the membrane and likely interacts with the quinone pool (419 aa)
 
  0.985
fdnG-2
Formate dehydrogenase, alpha subunit, selenocysteine-containing; Selenoprotein; identified by similarity to SP-P24183; match to protein family HMM PF00384; match to protein family HMM PF01568; match to protein family HMM PF04879; match to protein family HMM TIGR01409; match to protein family HMM TIGR01553; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family (1003 aa)
 
 
  0.847
fdnG-1
Formate dehydrogenase, alpha subunit, selenocysteine-containing; Selenoprotein; identified by similarity to SP-P24183; match to protein family HMM PF00384; match to protein family HMM PF01568; match to protein family HMM PF04879; match to protein family HMM TIGR01409; match to protein family HMM TIGR01553 (1005 aa)
 
 
  0.846
fdnG-3
Formate dehydrogenase 2 subunit alpha (cytochrome c-553); Alpha chain of the formate dehydrogenase (FDH) that catalyzes the reversible two-electron oxidation of formate to carbon dioxide. The alpha subunit of formate dehydrogenase forms the active site (1012 aa)
 
 
  0.845
DVU_1614
Iron-sulfur cluster-binding protein; Identified by similarity to SP-P30132; match to protein family HMM PF00037 (176 aa)
   
          0.734
DVU_0173
Thiosulfate reductase, putative; Identified by similarity to SP-P37600; match to protein family HMM PF00384; match to protein family HMM PF01568; match to protein family HMM PF04879 (733 aa)
 
 
  0.733
DVU_1286
Reductase, transmembrane subunit, putative; Identified by match to protein family HMM PF03916 (387 aa)
 
 
  0.689
DVU_2481
Formate dehydrogenase, beta subunit, putative; Identified by similarity to SP-P32175 (260 aa)
   
     
  0.660
DVU_0534
Protein DVU_0534; HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates (388 aa)
 
  0.655
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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