STRINGSTRING
pcrA pcrA pcrB pcrB fra fra sufC sufC sufD sufD sufU sufU sufB sufB iscSB iscSB nifS nifS iscSA iscSA mutY mutY
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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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pcrAATP-dependent DNA helicase; DNA helicase used for plasmid rolling-circle replication and also involved in UV repair. (739 aa)
pcrBHeptaprenylglyceryl-phosphate synthase; Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Ca [...] (228 aa)
fraFrataxin; Possible global iron distributor for the cell. Promotes the biosynthesis of iron-sulfur clusters by delivering Fe to the iron- sulfur cluster assembly scaffold protein SufU. In the presence of SufS and L-cysteine reconstitutes Fe-S clusters on SufU, which when further incubated with apo-aconitase (citB) reconstitutes aconitase activity. Able to reconstitute an Fe-S cluster on Thermotoga maritima IscU. (123 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)
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)
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)
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)
mutYA/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...] (369 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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