Frataxin; 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.

Iron-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 [...]

Non essential component of Na+/H+ antiporter; May enhance MrpA stability, assembly, or function. May play chaperone or assembly roles for MrpA and perhaps for other mrp proteins.

Putative ferredoxin/thioredoxin reductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.

Non essential component of Na+/H+ antiporter; Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+). Belongs to the [...]

Proton transporter component of Na+/H+ antiporter; Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+). Belongs to [...]

Efflux transporter for Na+ and cholate; Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).

Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.

Putative regulatory protein; Regulates sporulation prior to stage II. Positively controls the competence regulator ComK at a post-transcriptional level. May modulate the translation, stability or activity of ComS. May work together with YmcA to regulate community development.