Protein Domain : Enterobactin synthetase-like, component D IPR003542

Type	Family
Description	Iron is essential for growth in both bacteria and mammals. Controlling the amount of free iron in solution is often used as a tactic by hosts to limit invasion of pathogenic microbes; binding iron tightly within protein molecules can accomplish this. Such iron-protein complexes include haem in blood, lactoferrin in tears/saliva and transferrin in blood plasma. Some bacteria express surface receptors to capture eukaryotic iron-binding compounds, while others have evolved siderophores to scavenge iron from iron-binding host proteins [ ].The absence of free iron molecules in the surrounding environment triggers transcription of gene clusters that encode both siderophore-synthesis enzymes, and receptors that recognise iron-bound siderophores [ ]. Classic examples are the enterobactin/enterochelin clusters found in Escherichia coli and Salmonella, although similar moieties in other pathogens have been identified. The enzymic machinery that produces vibrionectin in Vibrio cholerae is such a homologue [].EntD (also known as 4'-phosphopantetheinyl transferase EntD) forms part of the enterobactin-synthetase enzyme complex. It plays an essential role in the assembly of the enterobactin by catalysing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively []. Deletion studies involving EntD- mutants have shown that it is essential for virulence [].This entry also identifies some 4'-phosphopantetheinyl transferase proteins.
Short Name	Enbac_synth_compD-like