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Gene Review

lspA  -  prolipoprotein signal peptidase (signal...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0028, JW0025
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Disease relevance of lspA


High impact information on lspA

  • Here we experimentally verify this prediction by metabolic labeling of subunit b with [14C]palmitic acid and by in vivo interfering with the processing of the prolipoprotein form of subunit b by the antibiotic globomycin, a specific inhibitor of the signal peptidase II [6].
  • Unexpectedly, induced expression of MBP27-P was found to have an adverse effect on the processing kinetics of five different nonlipoprotein precursors analyzed, but not precursor Lpp (the major outer membrane lipoprotein) processed by a different enzyme, signal peptidase II [7].
  • Taken together, these results strongly support the predicted model for SPase II topology, i.e. this enzyme spans the cytoplasmic membrane four times with both the amino and the carboxyl termini facing the cytoplasm [2].
  • A series of lsp-phoA and lsp-lacZ gene fusions have been constructed in vitro to determine the topology of SPase II [2].
  • This new cleavage between alanine and lysine residues was resistant to globomycin, a specific inhibitor for signal peptidase II [8].

Chemical compound and disease context of lspA


Biological context of lspA


Other interactions of lspA

  • The transcription of lspA, lgt (encoding prolipoprotein transferase), and lepB (encoding type I signal peptidase), monitored by real-time quantitative reverse transcription-PCR, reveals a differential expression pattern during various stages of rickettsial intracellular growth [4].
  • Radioactive labeling experiments in the presence or absence of globomycin showed that the hybrid protein is modified with a diglyceride and fatty acids and is processed by signal peptidase II, as is the murein lipoprotein [16].


  1. The type II signal peptidase of Legionella pneumophila. Geukens, N., De Buck, E., Meyen, E., Maes, L., Vranckx, L., Van Mellaert, L., Ann??, J., Lammertyn, E. Res. Microbiol. (2006) [Pubmed]
  2. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). Muñoa, F.J., Miller, K.W., Beers, R., Graham, M., Wu, H.C. J. Biol. Chem. (1991) [Pubmed]
  3. The signal peptidase II (Isp) gene of Bacillus subtilis. Prágai, Z., Tjalsma, H., Bolhuis, A., van Dijl, J.M., Venema, G., Bron, S. Microbiology (Reading, Engl.) (1997) [Pubmed]
  4. The lspA Gene, Encoding the Type II Signal Peptidase of Rickettsia typhi: Transcriptional and Functional Analysis. Rahman, M.S., Ceraul, S.M., Dreher-Lesnick, S.M., Beier, M.S., Azad, A.F. J. Bacteriol. (2007) [Pubmed]
  5. Cloning and nucleotide sequence of the Enterobacter aerogenes signal peptidase II (lsp) gene. Isaki, L., Kawakami, M., Beers, R., Hom, R., Wu, H.C. J. Bacteriol. (1990) [Pubmed]
  6. The subunit b of the F0F1-type ATPase of the bacterium Mycoplasma pneumoniae is a lipoprotein. Pyrowolakis, G., Hofmann, D., Herrmann, R. J. Biol. Chem. (1998) [Pubmed]
  7. Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo. Barkocy-Gallagher, G.A., Bassford, P.J. J. Biol. Chem. (1992) [Pubmed]
  8. An alternate pathway for the processing of the prolipoprotein signal peptide in Escherichia coli. Ghrayeb, J., Lunn, C.A., Inouye, S., Inouye, M. J. Biol. Chem. (1985) [Pubmed]
  9. Defective Escherichia coli signal peptides function in yeast. Pines, O., Lunn, C.A., Inouye, M. Mol. Microbiol. (1988) [Pubmed]
  10. Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli. Yakushi, T., Tajima, T., Matsuyama, S., Tokuda, H. J. Bacteriol. (1997) [Pubmed]
  11. Generation of antibodies to the signal peptide of the MPT83 lipoprotein of Mycobacterium tuberculosis. Harboe, M., Whelan, A.O., Ulvund, G., McNair, J., Pollock, J.M., Hewinson, R.G., Wiker, H.G. Scand. J. Immunol. (2002) [Pubmed]
  12. Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes. Isaki, L., Beers, R., Wu, H.C. J. Bacteriol. (1990) [Pubmed]
  13. Molecular cloning and immunological characterization of a novel linear-plasmid-encoded gene, pG, of Borrelia burgdorferi expressed only in vivo. Wallich, R., Brenner, C., Kramer, M.D., Simon, M.M. Infect. Immun. (1995) [Pubmed]
  14. Similarity between the 38-kilodalton lipoprotein of Treponema pallidum and the glucose/galactose-binding (MglB) protein of Escherichia coli. Becker, P.S., Akins, D.R., Radolf, J.D., Norgard, M.V. Infect. Immun. (1994) [Pubmed]
  15. Lipoproteins in bacteria. Hayashi, S., Wu, H.C. J. Bioenerg. Biomembr. (1990) [Pubmed]
  16. Modification, processing, and subcellular localization in Escherichia coli of the pCloDF13-encoded bacteriocin release protein fused to the mature portion of beta-lactamase. Luirink, J., Watanabe, T., Wu, H.C., Stegehuis, F., de Graaf, F.K., Oudega, B. J. Bacteriol. (1987) [Pubmed]
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