Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli

Abstract

The nucleotide sequence of the tspA gene coding for lipoprotein signal peptidase of Escherichia coti was determined and the amino acid sequence of the peptidase was deduced from it. The molecular mass and amino acid composition of the predicted lipoprotein signai peptidase were consistent with those of the signal peptidase purified from ceils harboring the tspA gene-carrying plasmid. The peptidase most probably has no cleavable signal peptide. The tspA gene was preceded by the iteS gene coding for isoleucyltRNA synthetase and the tandem termination codons of the iteS gene overlapped with the initiation codon of the tspA gene.Lipoprotein signat peptidase DNA sequence Lipoprotein

Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide.

“…The amino terminal sequence of Ro/SS-A appears to be unique among 4,000 proteins so far searched by computer analysis. However, it does have limited sequence similarity to the human C4a (25%) (amino acids 511-538) (23), lipoprotein signal peptidase (33%) (amino acids 51-73) (24,25), epidermal growth factor-binding protein type B precursor (29%) (amino acids 39-58) (26), human low density lipoprotein receptor precursor (17%) (amino acids 10-27) (27), and B-2 glycoprotein (21%) (amino acids 264-282) (28).…”

Elucidation of the function of lipoprotein-sorting signals that determine membrane localization

“…Moreover, it is not known how the sorting signals determine the membrane specificity. Because apolipoprotein transacylase (15), which catalyzes the last step of lipoprotein maturation, is not found in Bacillus subtilis, despite the high conservation of the other two lipoprotein-processing enzymes, prolipoprotein diacylglyceryl transferase (16) and prolipoprotein signal peptidase (17,18), it has been suggested to be possible that aspartate at position 2 might inhibit the last step of lipid modification, thereby causing the generation of different species of lipoproteins that are specific to the inner membrane (19). However, so far, we have found no difference in lipid modification between inner membrane-specific and outer membrane-specific lipoproteins (T. Hara, S.M., and H.T., unpublished observations), indicating that the lipoprotein-sorting signals function at the release step but not at the step of lipid modification.…”

Identification and Characterization of an Invasion Antigen B Gene from the Oral Pathogen Campylobacter rectus

“…In contrast to Cr-CiaB and Cr-LspA, the bacterial LspA are predicted to contain membrane helices and are likely to be located within membranes (Table 5). For E. coli LspA, the membrane helices and cellular location have been demonstrated [38]. In addition, bacterial LspA are less than 200 amino acids long.…”