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Literature summary for 3.4.21.89 extracted from

  • Musik, J.E.; Zalucki, Y.M.; Day, C.J.; Jennings, M.P.
    Efficient function of signal peptidase 1 of Escherichia coli is partly determined by residues in the mature N-terminus of exported proteins (2019), Biochim. Biophys. Acta, 1861, 1018-1022 .
    View publication on PubMed
Search for more literature for 3.4.21.89

Protein Variants

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

Localization Comment Organism GeneOntology No. Textmining
cell membrane the enzyme is an intergral membrane protein Escherichia coli
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-

Organism

Organism UniProt Comment Textmining
Escherichia coli P00803
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-

Substrates and Products (Substrate)

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 ?
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 ?
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
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 ?

Synonyms

Synonyms Comment Organism
LepB
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 Escherichia coli
Spase I
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 Escherichia coli

General Information

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