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bpr bpr rpoZ rpoZ iscSA iscSA cymR cymR nifS nifS iscSB iscSB sufU sufU sufD sufD sufC sufC fliS fliS
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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
Predicted Interactions
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bprEvidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (1433 aa)
rpoZOmega subunit of RNA polymerase; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). (67 aa)
iscSACysteine desulfurase involved in tRNA thiolation; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (379 aa)
cymRTranscriptional regulator of cysteine biosynthesis; Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the Cy [...] (138 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)
iscSBCysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (381 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)
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)
sufCSulfur mobilizing ABC protein, ATPase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the ABC transporter superfamily. Ycf16 family. (261 aa)
fliSFlagellar assembly protein FliS; Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly. Belongs to the FliS family. (133 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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