{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Verstraete MM"],"funding":["Gouvernement du Canada Natural Sciences and Engineering Research Council of Canada (NSERC)","Gouvernement du Canada Canadian Institutes of Health Research (CIHR)","CIHR"],"pagination":["6147-6160"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5912478"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(16)"],"pubmed_abstract":["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 <sup>31</sup>P NMR and HPLC analyses indicated that SbnI is also a free serine kinase but uses ATP rather than ADP as phosphate d"],"journal":["The Journal of biological chemistry"],"pubmed_title":["SbnI 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>."],"pmcid":["PMC5912478"],"funding_grant_id":["MOP-49597","MOP-38002","Post Graduate Scholarship - Doctoral"],"pubmed_authors":["Murphy MEP","Verstraete MM","Brown KL","Heinrichs DE","Perez-Borrajero C"],"additional_accession":[]},"is_claimable":false,"name":"SbnI 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>.","description":"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 <sup>31</sup>P NMR and HPLC analyses indicated that SbnI is also a free serine kinase but uses ATP rather than ADP as phosphate d","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2026-05-03T08:03:27.082Z","creation":"2019-06-06T19:23:07Z"},"accession":"S-EPMC5912478","cross_references":{"pubmed":["29483190"],"doi":["10.1074/jbc.ra118.001875","10.1074/jbc.RA118.001875"]}}