biostudies-literatureVerstraete MMGouvernement du Canada Natural Sciences and Engineering Research Council of Canada (NSERC)Gouvernement du Canada Canadian Institutes of Health Research (CIHR)CIHR6147-6160https://www.ebi.ac.uk/biostudies/studies/S-EPMC5912478biostudies-literatureUnknown293(16)Staphyloferrin B (SB) is an iron-chelating siderophore produced by <i>Staphylococcus aureus</i> in invasive infections. Proteins for SB biosynthesis and export are encoded by the <i>sbnABCDEFGHI</i> gene cluster, in which SbnI, a member of the ParB/Srx superfamily, acts as a heme-dependent transcriptional regulator of the <i>sbn</i> locus. However, no structural or functional information about SbnI is available. Here, a crystal structure of SbnI revealed striking structural similarity to an ADP-dependent free serine kinase, SerK, from the archaea <i>Thermococcus kodakarensis</i> We found that features of the active sites are conserved, and biochemical assays and ³¹P NMR and HPLC analyses indicated that SbnI is also a free serine kinase but uses ATP rather than ADP as phosphate dThe Journal of biological chemistrySbnI is a free serine kinase that generates <b><i>O</i></b> -phospho-l-serine for staphyloferrin B biosynthesis in <b><i>Staphylococcus aureus</i></b>.PMC5912478MOP-49597MOP-38002Post Graduate Scholarship - DoctoralMurphy MEPVerstraete MMBrown KLHeinrichs DEPerez-Borrajero CfalseSbnI is a free serine kinase that generates <b><i>O</i></b> -phospho-l-serine for staphyloferrin B biosynthesis in <b><i>Staphylococcus aureus</i></b>.Staphyloferrin B (SB) is an iron-chelating siderophore produced by <i>Staphylococcus aureus</i> in invasive infections. Proteins for SB biosynthesis and export are encoded by the <i>sbnABCDEFGHI</i> gene cluster, in which SbnI, a member of the ParB/Srx superfamily, acts as a heme-dependent transcriptional regulator of the <i>sbn</i> locus. However, no structural or functional information about SbnI is available. Here, a crystal structure of SbnI revealed striking structural similarity to an ADP-dependent free serine kinase, SerK, from the archaea <i>Thermococcus kodakarensis</i> We found that features of the active sites are conserved, and biochemical assays and ³¹P NMR and HPLC analyses indicated that SbnI is also a free serine kinase but uses ATP rather than ADP as phosphate d2018-01-01T00:00:00Z2018 Apr2026-05-03T08:03:27.082Z2019-06-06T19:23:07ZS-EPMC59124782948319010.1074/jbc.ra118.00187510.1074/jbc.RA118.001875