Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of a DELTA2-76 truncated enzyme mutant by deletion. The mutant is soluble and lacks both N-terminal transmembrane domains | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell membrane | the enzyme is an intergral membrane protein | Escherichia coli | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P00803 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | cleavage site specificity of Escherichia coli SPase I, overview. Cobstruction of different signal peptides of MBP and binding analysis with the enzyme | Escherichia coli | ? | - |
? | |
pre-maltose binding protein + H2O | the maltose binding protein (MBP) is mutated to introduce aromatic amino acids (tryptophan, tyrosine and phenylalanine) at P2' of the signal peptidase I cleavage sequence. All mutants with aromatic amino acids at P2' are exported less efficiently as indicated by a slight increase in precursor protein in vivo. Binding of LepB to peptides that encompass the MBP cleavage site are analysed using surface plasmon resonance. The presence of phenylalanine and tyrosine at P2', but not tryptophan, increase to a small extent the amount of preMBP in the sample | Escherichia coli | maltose binding protein + signal peptide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LepB | - |
Escherichia coli |
Spase I | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | exported proteins require an N-terminal signal peptide to direct them from the cytoplasm to the periplasm. Once the protein has been translocated across the cytoplasmic membrane, the signal peptide is cleaved by a signal peptidase, allowing the remainder of the protein to fold into its mature state in the periplasm. Signal peptidase I (LepB) cleaves non-lipoproteins and recognises the sequence Ala-X-Ala. Amino acids present at the N-terminus of mature, exported proteins affect the efficiency at which the protein is exported | Escherichia coli |