STRINGSTRING
sufU sufU iscSB iscSB nifS nifS iscSA iscSA dnaK dnaK ispH ispH ispG ispG miaB miaB nsrR nsrR salA salA sufC sufC sufD sufD sufS sufS sufB sufB
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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textmining
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sufUIron-sulfur cluster assembly scaffold protein; Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein , but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein. Has been shown to bind low levels of a labile, air- sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkyl [...] (147 aa)
iscSBCysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (381 aa)
nifSPutative desulfurase involved in iron-sulfur clusters for NAD biosynthesis; Catalyzes the removal of elemental sulfur from cysteine to produce alanine (By similarity). Seems to be required for NAD biosynthesis. (395 aa)
iscSACysteine desulfurase involved in tRNA thiolation; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (379 aa)
dnaKMolecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. (611 aa)
ispH1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Belongs to the IspH family. (314 aa)
ispG4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. (377 aa)
miaBEnzyme for ms(2)i(6)A formation for tRNA modification; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (509 aa)
nsrRNO-dependent activator of the ResDE regulon; Nitric oxide-responsive transcriptional regulator. It represses the expression of flavohemoprotein hmp and the nitrite reductase nasD. Probably plays a role in the up-regulation of the resDE regulon in the presence of nitric oxide. (146 aa)
salAMrp family regulator; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (352 aa)
sufCSulfur mobilizing ABC protein, ATPase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the ABC transporter superfamily. Ycf16 family. (261 aa)
sufDFeS assembly protein SufD; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation (By similarity). Belongs to the UPF0051 (ycf24) family. (437 aa)
sufSCysteine desulfurase; Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40- to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. (406 aa)
sufBFeS cluster formation protein; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation (By similarity). Belongs to the UPF0051 (ycf24) family. (465 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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