Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
FkpA + H2O | Escherichia coli | periplasmic peptidyl-prolyl cistrans isomerase, chaperone | ? | - |
? | |
MalE + H2O | Escherichia coli | periplasmic maltose-binding protein | ? | - |
? | |
additional information | Escherichia coli | identification of beta-barrel outer membrane proteins, OMPs, as major natural substrates by photo-crosslinking using non-natural amino acid DiZPK, 3-(3-methyl-3H-diazirine-3-yl)-propaminocarbonyl-Nepsilon-L-lysine, as the photo-crosslinker. Isoform DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded outer membrane proteins, with hardly any appreciable chaperone activity in cells. The toxic and cell membrane-damaging misfolded outer membrane proteins would accumulate in DegP-lacking cells cultured under heat shock conditions | ? | - |
? | |
OmpA + H2O | Escherichia coli | outer membrane porin protein | ? | - |
? | |
OmpC + H2O | Escherichia coli | outer membrane porin protein | ? | - |
? | |
OmpF + H2O | Escherichia coli | outer membrane porin protein | ? | - |
? | |
OmpW + H2O | Escherichia coli | outer membrane porin protein | ? | - |
? | |
OmpX + H2O | Escherichia coli | outer membrane porin protein | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FkpA + H2O | periplasmic peptidyl-prolyl cistrans isomerase, chaperone | Escherichia coli | ? | - |
? | |
FkpA + H2O | periplasmic peptidyl-prolyl cis-trans isomerase, chaperone | Escherichia coli | ? | - |
? | |
MalE + H2O | periplasmic maltose-binding protein | Escherichia coli | ? | - |
? | |
additional information | identification of beta-barrel outer membrane proteins, OMPs, as major natural substrates by photo-crosslinking using non-natural amino acid DiZPK, 3-(3-methyl-3H-diazirine-3-yl)-propaminocarbonyl-Nepsilon-L-lysine, as the photo-crosslinker. Isoform DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded outer membrane proteins, with hardly any appreciable chaperone activity in cells. The toxic and cell membrane-damaging misfolded outer membrane proteins would accumulate in DegP-lacking cells cultured under heat shock conditions | Escherichia coli | ? | - |
? | |
OmpA + H2O | outer membrane porin protein | Escherichia coli | ? | - |
? | |
OmpC + H2O | outer membrane porin protein | Escherichia coli | ? | - |
? | |
OmpF + H2O | outer membrane porin protein | Escherichia coli | ? | - |
? | |
OmpW + H2O | outer membrane porin protein | Escherichia coli | ? | - |
? | |
OmpX + H2O | outer membrane porin protein | Escherichia coli | ? | - |
? |