UniProt functional annotation for O32163



	UniProt functional annotation for O32163

UniProt code: O32163.

Organism: Bacillus subtilis (strain 168).

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.

Function: Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). 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. Alkylation eliminates its ability to stimulate SufS. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. {ECO:0000269|PubMed:20097860, ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255, ECO:0000269|PubMed:21744456, ECO:0000269|PubMed:24321018}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24321018}; Note=Bind 1 Zn(2+) per monomer. {ECO:0000269|PubMed:24321018};

Subunit: Interacts with SufS; the complex is more stable in the presence of L-cysteine. An N-terminal His-tag of SufS destabilizes this interaction. {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255, ECO:0000269|Ref.7, ECO:0000269|Ref.8}.

Disruption phenotype: Essential, it cannot be deleted. Upon depletion cells grow very slowly while aconitase and succinate dehydrogenase, both of which contain Fe-S clusters, have decreased activity. Upon depletion no change in reactive oxygen species is observed, while a modified bacillibactin (BB), an endogenous siderophore, is produced. {ECO:0000269|PubMed:20097860, ECO:0000269|PubMed:21744456}.

Similarity: Belongs to the NifU family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus subtilis (strain 168).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.



Function:		Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). 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. Alkylation eliminates its ability to stimulate SufS. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. {ECO:0000269\|PubMed:20097860, ECO:0000269\|PubMed:20822158, ECO:0000269\|PubMed:21236255, ECO:0000269\|PubMed:21744456, ECO:0000269\|PubMed:24321018}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:24321018}; Note=Bind 1 Zn(2+) per monomer. {ECO:0000269\|PubMed:24321018};
Subunit:		Interacts with SufS; the complex is more stable in the presence of L-cysteine. An N-terminal His-tag of SufS destabilizes this interaction. {ECO:0000269\|PubMed:20822158, ECO:0000269\|PubMed:21236255, ECO:0000269\|Ref.7, ECO:0000269\|Ref.8}.
Disruption phenotype:		Essential, it cannot be deleted. Upon depletion cells grow very slowly while aconitase and succinate dehydrogenase, both of which contain Fe-S clusters, have decreased activity. Upon depletion no change in reactive oxygen species is observed, while a modified bacillibactin (BB), an endogenous siderophore, is produced. {ECO:0000269\|PubMed:20097860, ECO:0000269\|PubMed:21744456}.
Similarity:		Belongs to the NifU family. {ECO:0000305}.