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Literature for peptidase A08.001: signal peptidase II

Summary Alignment Tree Sequences Sequence features Distribution Literature Substrates

(Topics flags: A Assay, S Structure, T Target, K Knockout, P Specificity, I Inhibitor, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

    2025
  1. Ramberg,K.O., Boland,C., Kooshapur,H., Soubias,O., Wiktor,M., Huang,C.Y., Bailey,J., Gawrisch,K. and Caffrey,M.
    Solid-State NMR of Membrane Peptides and Proteins in the Lipid Cubic Phase
    Biophys J PubMed  Europe PubMed DOI  I
    2. 2022
  2. Huang,K.J., Pantua,H., Diao,J., Skippington,E., Volny,M., Sandoval,W., Tiku,V., Peng,Y., Sagolla,M., Yan,D., Kang,J., Katakam,A.K., Michaelian,N., Reichelt,M., Tan,M.W., Austin,C.D., Xu,M., Hanan,E. and Kapadia,S.B.
    Deletion of a previously uncharacterized lipoprotein lirL confers resistance to an inhibitor of type II signal peptidase in Acinetobacter baumannii
    Proc Natl Acad Sci U S A119, e2123117119-e2123117119. PubMed  Europe PubMed DOI  I
    3. 2020
  3. Olatunji,S., Yu,X., Bailey,J., Huang,C.Y., Zapotoczna,M., Bowen,K., Remskar,M., Muller,R., Scanlan,E.M., Geoghegan,J.A., Olieric,V. and Caffrey,M.
    Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin
    Nat Commun11, 140-140. PubMed  Europe PubMed DOI  S  I
  4. Pantua,H., Skippington,E., Braun,M.G., Noland,C.L., Diao,J., Peng,Y., Gloor,S.L., Yan,D., Kang,J., Katakam,A.K., Reeder,J., Castanedo,G.M., Garland,K., Komuves,L., Sagolla,M., Austin,C.D., Murray,J., Xu,Y., Modrusan,Z., Xu,M., Hanan,E.J. and Kapadia,S.B.
    Unstable Mechanisms of Resistance to Inhibitors of Escherichia coli Lipoprotein Signal Peptidase
    MBio11, PubMed  Europe PubMed DOI  I
    5. 2018
  5. Kitamura,S. and Wolan,D.W.
    Probing substrate recognition of bacterial lipoprotein signal peptidase using FRET reporters
    FEBS Lett592, 2289-2296. PubMed  Europe PubMed DOI  A  P
  6. Kitamura,S., Owensby,A., Wall,D. and Wolan,D.W.
    Lipoprotein signal peptidase inhibitors with antibiotic properties identified through design of a robust in vitro HT platform
    Cell Chem Biol25, 301-308. PubMed  Europe PubMed DOI  I
    7. 2017
  7. Sangith,N. and Sankaran,K.
    Stringency of bacterial prolipoprotein signal peptidase (LspA) in recognition of signal peptides - structure-function correlation
    Biochem Biophys Res Commun488, 413-417. PubMed  Europe PubMed DOI  P
    8. 2016
  8. Vogeley,L., El Arnaout,T., Bailey,J., Stansfeld,P.J., Boland,C. and Caffrey,M.
    Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
    Science351, 876-880. PubMed  Europe PubMed DOI  S  I
    9. 2014
  9. Xiao,Y. and Wall,D.
    Genetic redundancy, proximity, and functionality of lspA, the target of antibiotic TA, in the Myxococcus xanthus producer strain
    J Bacteriol196, 1174-1183. PubMed  Europe PubMed DOI  I
    10. 2013
  10. Gullon,S., Arranz,E.I. and Mellado,R.P.
    Transcriptional characterisation of the negative effect exerted by a deficiency in type II signal peptidase on extracellular protein secretion in Streptomyces lividans
    Appl Microbiol Biotechnol97, 10069-10080. PubMed  Europe PubMed DOI  K
    11. 2012
  11. Chimalapati,S., Sankaran,K. and Brown,J.S.
    Signal peptidase II
    [ISSN:978-0-12-407744-7]3, 258-261. DOI
  12. Xiao,Y., Gerth,K., Muller,R. and Wall,D.
    Myxobacterium-produced antibiotic TA (myxovirescin) inhibits type II signal peptidase
    Antimicrob Agents Chemother56, 2014-2021. PubMed  Europe PubMed DOI  I
    13. 2010
  13. Remans,K., Vercammen,K., Bodilis,J. and Cornelis,P.
    Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa
    Microbiology (Reading)156, 2597-2607. PubMed  Europe PubMed DOI
    14. 2009
  14. Banaei,N., Kincaid,E.Z., Lin,S.Y., Desmond,E., Jacobs,W.R., Jr. and Ernst,J.D.
    Lipoprotein processing is essential for resistance of Mycobacterium tuberculosis to malachite green
    Antimicrobial Agents Chemother53, 3799-3802. PubMed  Europe PubMed DOI
  15. Das,S., Kanamoto,T., Ge,X., Xu,P., Unoki,T., Munro,C.L. and Kitten,T.
    Contribution of lipoproteins and lipoprotein processing to endocarditis virulence in Streptococcus sanguinis
    J Bacteriol191, 4166-4179. PubMed  Europe PubMed DOI
  16. Denham,E.L., Ward,P.N. and Leigh,J.A.
    In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp
    Microbiology (Reading)155, 134-141. PubMed  Europe PubMed DOI
    17. 2008
  17. Arimoto,T. and Igarashi,T.
    Role of prolipoprotein diacylglyceryl transferase (Lgt) and lipoprotein-specific signal peptidase II (LspA) in localization and physiological function of lipoprotein MsmE in Streptococcus mutans
    Oral Microbiol Immunol23, 515-519. PubMed  Europe PubMed DOI
  18. Denham,E.L., Ward,P.N. and Leigh,J.A.
    Lipoprotein signal peptides are processed by Lsp and Eep of Streptococcus uberis
    J Bacteriol190, 4641-4647. PubMed  Europe PubMed DOI
  19. Henneke,P., Dramsi,S., Mancuso,G., Chraibi,K., Pellegrini,E., Theilacker,C., Hubner,J., Santos-Sierra,S., Teti,G., Golenbock,D.T., Poyart,C. and Trieu-Cuot,P.
    Lipoproteins are critical TLR2 activating toxins in group B streptococcal sepsis
    J Immunol180, 6149-6158. PubMed  Europe PubMed
  20. Khandavilli,S., Homer,K.A., Yuste,J., Basavanna,S., Mitchell,T. and Brown,J.S.
    Maturation of Streptococcus pneumoniae lipoproteins by a type II signal peptidase is required for ABC transporter function and full virulence
    Mol Microbiol67, 541-557. PubMed  Europe PubMed DOI
  21. Rampini,S.K., Selchow,P., Keller,C., Ehlers,S., Bottger,E.C. and Sander,P.
    LspA inactivation in Mycobacterium tuberculosis results in attenuation without affecting phagosome maturation arrest
    Microbiology (Reading)154, 2991-3001. PubMed  Europe PubMed DOI  K
    22. 2007
  22. Baumgartner,M., Karst,U., Gerstel,B., Loessner,M., Wehland,J. and Jansch,L.
    Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes
    J Bacteriol189, 313-324. PubMed  Europe PubMed DOI
  23. Rahman,M.S., Ceraul,S.M., Dreher-Lesnick,S.M., Beier,M.S. and Azad,A.F.
    The lspA gene, encoding the type II signal peptidase of Rickettsia typhi: transcriptional and functional analysis
    J Bacteriol189, 336-341. PubMed  Europe PubMed DOI
    24. 2006
  24. [YEAR:12-7-2006]Geukens,N., De Buck,E., Meyen,E., Maes,L., Vranckx,L., Van Mellaert,L., Anne,J. and Lammertyn,E.
    The type II signal peptidase of Legionella pneumophila
    Res Microbiol157, 836-841. PubMed  Europe PubMed DOI  T
    25. 2004
  25. Gonnet,P., Rudd,K.E. and Lisacek,F.
    Fine-tuning the prediction of sequences cleaved by signal peptidase II: a curated set of proven and predicted lipoproteins of Escherichia coli K-12
    Proteomics4, 1597-1613. PubMed  Europe PubMed DOI  P
  26. Sander,P., Rezwan,M., Walker,B., Rampini,S.K., Kroppenstedt,R.M., Ehlers,S., Keller,C., Keeble,J.R., Hagemeier,M., Colston,M.J., Springer,B. and Bottger,E.C.
    Lipoprotein processing is required for virulence of Mycobacterium tuberculosis
    Mol Microbiol52, 1543-1552. PubMed  Europe PubMed DOI
  27. Sankaran,K.
    Signal peptidase II
    [ISSN:0-12-079610-4]2, 201-204.  V
    28. 2003
  28. De Greeff,A., Hamilton,A., Sutcliffe,I.C., Buys,H., van Alphen,L. and Smith,H.E.
    Lipoprotein signal peptidase of Streptococcus suis serotype 2
    Microbiology (Reading, Engl )149, 1399-1407. PubMed  Europe PubMed
  29. Kiho,T., Iwata,Y., Kogen,H. and Miyamoto,S.
    Conformational analysis of globomycin with a signal peptidase II inhibitory activity using molecular dynamics simulation
    Drug Des Discov18, 109-116. PubMed  Europe PubMed DOI  I
  30. [YEAR:3-3-2003]Kiho,T., Nakayama,M. and Kogen,H.
    Total synthesis and NMR conformational study of signal peptidase II inhibitors, globomycin and SF-1902 A5
    Tetrahedron59, 1685-1697.  I
  31. Reglier-Poupet,H., Frehel,C., Dubail,I., Beretti,J.L., Berche,P., Charbit,A. and Raynaud,C.
    Maturation of lipoproteins by type II signal peptidase is required for phagosomal escape of Listeria monocytogenes
    J Biol Chem278, 49469-49477. PubMed  Europe PubMed DOI
  32. Venema,R., Tjalsma,H., van Dijl,J.M., de Jong,A., Leenhouts,K., Buist,G. and Venema,G.
    Active lipoprotein precursors in the Gram-positive eubacterium Lactococcus lactis
    J Biol Chem278, 14739-14746. PubMed  Europe PubMed DOI
    33. 2002
  33. Paetzel,M., Karla,A., Strynadka,N.C. and Dalbey,R.E.
    Signal peptidases
    Chem Rev102, 4549-4580. PubMed  Europe PubMed DOI  V
    34. 1999
  34. Paitan,Y., Orr,E., Ron,E.Z. and Rosenberg,E.
    A nonessential signal peptidase II (Lsp) of Myxococcus xanthus might be involved in biosynthesis of the polyketide antibiotic TA
    J Bacteriol181, 5644-5651. PubMed  Europe PubMed
  35. [YEAR:1-10-1999]Tjalsma,H., Zanen,G., Venema,G., Bron,S. and van Dijl,J.M.
    The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis
    J Biol Chem274, 28191-28197. PubMed  Europe PubMed DOI
  36. [YEAR:15-1-1999]Tjalsma,H., Kontinen,V.P., Pragai,Z., Wu,H., Meima,R., Venema,G., Bron,S., Sarvas,M. and van Dijl,J.M.
    The role of lipoprotein processing by signal peptidase II in the Gram-positive eubacterium Bacillus subtilis. Signal peptidase II is required for the efficient secretion of alpha-amylase, a non-lipoprotein
    J Biol Chem274, 1698-1707. PubMed  Europe PubMed DOI
    37. 1997
  37. Pragai,Z., Tjalsma,H., Bolhuis,A., van Dijl,J.M., Venema,G. and Bron,S.
    The signal peptidase II (Isp) gene of Bacillus subtilis
    Microbiology (Reading, Engl )143, 1327-1333. PubMed  Europe PubMed
    38. 1996
  38. Beven,L., Le Henaff,M., Fontenelle,C. and Wroblewski,H.
    Inhibition of spiralin processing by the lipopeptide antibiotic globomycin
    Curr Microbiol33, 317-322. PubMed  Europe PubMed DOI  I
    39. 1995
  39. Sankaran,K. and Wu,H.C.
    Bacterial prolipoprotein signal peptidase
    Methods Enzymol248, 169-180. PubMed  Europe PubMed DOI  V
  40. Witke,C. and Gotz,F.
    Cloning and nucleotide sequence of the signal peptidase II (lsp)-gene from Staphylococcus carnosus
    FEMS Microbiol Lett126, 233-239. PubMed  Europe PubMed DOI
    41. 1992
  41. Zhao,X.J. and Wu,H.C.
    Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene
    FEBS Lett299, 80-84. PubMed  Europe PubMed DOI
    42. 1991
  42. Munoa,F.J., Miller,K.W., Beers,R., Graham,M. and Wu,H.C.
    Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)
    J Biol Chem266, 17667-17672. PubMed  Europe PubMed
    43. 1990
  43. Isaki,L., Kawakami,M., Beers,R., Hom,R. and Wu,H.C.
    Cloning and nucleotide sequence of the Enterobacter aerogenes signal peptidase II (lsp) gene
    J Bacteriol172, 469-472. PubMed  Europe PubMed
  44. Isaki,L., Beers,R. and Wu,H.C.
    Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes
    J Bacteriol172, 6512-6517. PubMed  Europe PubMed
    45. 1989
  45. von Heijne,G.
    The structure of signal peptides from bacterial lipoproteins
    Protein Eng2, 531-534. PubMed  Europe PubMed  P
    46. 1986
  46. Pollitt,S., Inouye,S. and Inouye,M.
    Effect of amino acid substitutions at the signal peptide cleavage site of the Escherichia coli major outer membrane lipoprotein
    J Biol Chem261, 1835-1837. PubMed  Europe PubMed
    47. 1985
  47. Dev,I.K., Harvey,R.J. and Ray,P.H.
    Inhibition of prolipoprotein signal peptidase by globomycin
    J Biol Chem260, 5891-5894. PubMed  Europe PubMed  I
    48. 1984
  48. Dev,I.K. and Ray,P.H.
    Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B
    J Biol Chem259, 11114-11120. PubMed  Europe PubMed  I
  49. Innis,M.A., Tokunaga,M., Williams,M.E., Loranger,J.M., Chang,S.Y., Chang,S. and Wu,H.C.
    Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene
    Proc Natl Acad Sci U S A81, 3708-3712. PubMed  Europe PubMed
  50. Tokunaga,M., Loranger,J.M. and Wu,H.C.
    A distinct signal peptidase for prolipoprotein in Escherichia coli
    J Cell Biochem24, 113-120. PubMed  Europe PubMed DOI
  51. Yamada,H., Yamagata,H. and Mizushima,S.
    The major outer membrane lipoprotein and new lipoproteins share a common signal peptidase that exists in the cytoplasmic membrane of Escherichia coli
    FEBS Lett166, 179-182. PubMed  Europe PubMed
  52. Yu,F., Yamada,H., Daishima,K. and Mizushima,S.
    Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli
    FEBS Lett173, 264-268. PubMed  Europe PubMed
    53. 1983
  53. Inouye,S., Franceschini,T., Sato,M., Itakura,K. and Inouye,M.
    Prolipoprotein signal peptidase of Escherichia coli requires a cysteine residue at the cleavage site
    EMBO J2, 87-91. PubMed  Europe PubMed
  54. [YEAR:25-10-1983]Tokunaga,M., Loranger,J.M. and Wu,H.C.
    Isolation and characterization of an Escherichia coli clone overproducing prolipoprotein signal peptidase
    J Biol Chem258, 12102-12105. PubMed  Europe PubMed  I
  55. Yamagata,H., Daishima,K. and Mizushima,S.
    Cloning and expression of a gene coding for the prolipoprotein signal peptidase of Escherichia coli
    FEBS Lett158, 301-304. PubMed  Europe PubMed
    56. 1982
  56. Hussain,M., Ichihara,S. and Mizushima,S.
    Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane
    J Biol Chem257, 5177-5182. PubMed  Europe PubMed
  57. Hussain,M., Ozawa,Y., Ichihara,S. and Mizushima,S.
    Signal peptide digestion in Escherichia coli. Effect of protease inhibitors on hydrolysis of the cleaved signal peptide of the major outer-membrane lipoprotein
    Eur J Biochem129, 233-239. PubMed  Europe PubMed  I
    58. 1980
  58. Hussain,M., Ichihara,S. and Mizushima,S.
    Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    J Biol Chem255, 3707-3712. PubMed  Europe PubMed  I
    59. 1977
  59. Inouye,S., Wang,S., Sekizawa,J., Halegoua,S. and Inouye,M.
    Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane
    Proc Natl Acad Sci U S A74, 1004-1008. PubMed  Europe PubMed

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