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Gene Review:

lspA - lipoprotein signal peptidase

Escherichia coli UTI89

Inukai, M. et al., Shang, E.S. et al., Yamada, H. et al., Ichikawa, J.K. et al.

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Disease relevance of lspA

We also show that treatment of E. coli cells with globomycin, an inhibitor of the lipoprotein signal peptidase, results in the accumulation of a 46-kDa precursor [1].

High impact information on lspA

It is believed that the lipoprotein signal peptidase directly cleaves the lipoprotein signal peptide at the peptide bond between the glycine residue at position 20 and the cysteine residue at position 21 of the prolipoprotein [2].
Processing of LipL41 is inhibited by globomycin, a selective inhibitor of lipoprotein signal peptidase [3].
The deduced amino acid sequence of LipL41 would encode a 355-amino-acid polypeptide with a 19-amino-acid signal peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site [3].
In this work, lipoprotein signal peptidase that processes the precursor of the major lipoprotein was partially purified from cells harboring a plasmid that carries the gene for this enzyme (1spA) [4].

References

A gene at 59 minutes on the Escherichia coli chromosome encodes a lipoprotein with unusual amino acid repeat sequences. Ichikawa, J.K., Li, C., Fu, J., Clarke, S. J. Bacteriol. (1994) [Pubmed]
Apolipoprotein, an intermediate in the processing of the major lipoprotein of the Escherichia coli outer membrane. Inukai, M., Ghrayeb, J., Nakamura, K., Inouye, M. J. Biol. Chem. (1984) [Pubmed]
Molecular cloning and sequence analysis of the gene encoding LipL41, a surface-exposed lipoprotein of pathogenic Leptospira species. Shang, E.S., Summers, T.A., Haake, D.A. Infect. Immun. (1996) [Pubmed]
The major outer membrane lipoprotein and new lipoproteins share a common signal peptidase that exists in the cytoplasmic membrane of Escherichia coli. Yamada, H., Yamagata, H., Mizushima, S. FEBS Lett. (1984) [Pubmed]

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