6.2.1.55	additional information	many of the sampylated proteins that are identified are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)	-, 746408	
6.2.1.55	additional information	UbaA is ubiquitin-like-automodified at lysine residues required for early (ATP binding) and late (sulfur mobilization) stages of enzyme activity revealing multiple layers of autoregulation. Cysteine residues, distinct from the canonical E1 active site cysteine, are found important in UbaA function supporting a model that this non-canonical E1 is structurally flexible in its active site to allow Ubl-adenylate, Ubl-E1-like thioester and cysteine persulfide(s) intermediates to form. Thermodynamics of Ubl protein binding, thioester intermediate, regulation by auto-modification, and amino acid residues important for catalytic function, overview. UbaA is autosampylated, autosampylation of K87 and K157 likely regulates UbaA function	-, 744867