Probable cysteine desulfurase (NifS protein homolog). Homology to iscS of M. thermophila of 40% (sprot|ISCS_METTE) Catalyzes the removal of elemental sulfur from cysteine to produce alanine (By similarity). InterPro: Aminotransferase class-V (IPR000192) Pfam: aminotransferase class-V no signal peptide no TMHs ahpD: alkylhydroperoxidase AhpD; Family membership.

Putative co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.

Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.

Putative regulatory Protein yfhF, 72% identity (82% similarity) to TrEMBL;P36539 of E.coli. Has PF01521, HesB-like domain;(IPR000361, HesB_yadR_yfhF); This family includes HesB which may be involved in nitrogen fixation; the hesB gene is expressed only under nitrogen fixation conditions. Other members of this family include various hypothetical proteins of which P46847 and NP31774 also contains NifU-like domains NifU which is also involved in nitrogen fixation. In the gram-negative soil bacterium Rhizobium etli, the hesB-like gene iscN is required for nitrogen fixation; High confidence [...]

Cysteine desulphurase; Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine.

Probable nitrogen fixation protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.

Fdx2 protein; Ferredoxin 2Fe-2S. Homology to fdx of E. coli of 70% (sprot|FER_ECOLI). Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron- sulfur proteins. InterPro: Ferredoxin (IPR001055); Adrenodoxin (IPR001055) Pfam: 2Fe-2S iorn-sulfur cluster binding domain no signal peptide no TMHs; High confidence in function and specificity.

Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION (BY SIMILARITY). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity.

Conserved hypothetical protein. Homology to CV1087 of C.violaceum of 69% (trembl:Q7NZ35). Has PF04384; Protein of unknown function (DUF528);IPR007479: Small bacterial protein of unknown function. No signal peptide or TMH present.