3.4.23.36: Signal peptidase II
This is an abbreviated version!
For detailed information about Signal peptidase II, go to the full flat file.
Word Map on EC 3.4.23.36
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3.4.23.36
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globomycin
-
intramembrane
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3hpalmitate
-
sppl2b
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lipobox
-
lipid-modified
-
diacylglyceryl
-
spp-like
-
isoleucyl-trna
-
braun
-
intramembrane-cleaving
-
triacylated
-
medicine
- 3.4.23.36
- globomycin
-
intramembrane
-
3hpalmitate
- sppl2b
-
lipobox
-
lipid-modified
-
diacylglyceryl
-
spp-like
-
isoleucyl-trna
-
braun
-
intramembrane-cleaving
-
triacylated
- medicine
Reaction
Release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein. Hydrolyses -Xaa-Yaa-Zaa-/-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral sidechains =
Synonyms
EC 3.4.99.35, Leader peptidase II, lipoprotein signal peptidase, lipoprotein signal peptidase II, lipoprotein-specific (typeII) signal peptidase, lipoprotein-specific signal peptidase, lipoprotein-specific type II signal peptidase, LspA, More, Premurein leader peptidase, Premurein leader proteinase, Premurein-leader peptidase, Prolipoprotein signal peptidase, Proteinase, premurein leader, Signal peptide peptidase, signal peptide peptidase-like 2a, Sp0928, SPase II, SpiI, SPP, SPPL2a, SPPL2c, type II signal peptidase
ECTree
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Reference on EC 3.4.23.36 - Signal peptidase II
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Innis, M.A.; Tokunaga, M.; Williams, M.E.; Loranger, J.M.; Chang, S.Y.; Chang, S.; Wu, H.C.
Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene
Proc. Natl. Acad. Sci. USA
81
3708-3712
1984
Escherichia coli
Isaki, L.; Kawakami, M.; Beers, R.; Hom, R.; Wu, H.C.
Cloning and nucleotide sequence of the Enterobacter aerogenes signal peptidase II (lsp) gene
J. Bacteriol.
172
469-472
1990
Klebsiella aerogenes
Yu, F.; Yamada, H.; Daishima, K.; Mizushima, S.
Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli
FEBS Lett.
173
264-268
1984
Escherichia coli
Yamada, H.; Yamagata, H.; 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 Lett.
166
179-182
1984
Escherichia coli
Dev, I.K.; Ray, P.H.
Signal peptidases and signal peptide hydrolases
J. Bioenerg. Biomembr.
22
271-290
1990
Escherichia coli
Sankaran, K.; Wu, H.C.
Bacterial prolipoprotein signal peptidase
Methods Enzymol.
248
169-180
1995
Escherichia coli, Escherichia coli B / ATCC 11303
Zhao, X.J.; Wu, H.C.
Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene
FEBS Lett.
299
80-84
1992
Staphylococcus aureus
Tjalsma, H.; Zanen, G.; Venema, G.; Bron, S.; Van Dijl, J.M.
The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis
J. Biol. Chem.
274
28191-28197
1999
Bacillus subtilis
Sankaran, K.
Signal peptidase II
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
201-204
2004
Klebsiella aerogenes, Bacillus subtilis, Escherichia coli, Staphylococcus aureus, Myxococcus xanthus, Pseudomonas fluorescens
-
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.; Boettger, E.C.
Lipoprotein processing is required for virulence of Mycobacterium tuberculosis
Mol. Microbiol.
52
1543-1552
2004
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Gonnet, P.; Rudd, K.E.; 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
Proteomics
4
1597-1613
2004
Escherichia coli K-12
Rahman, M.S.; Ceraul, S.M.; Dreher-Lesnick, S.M.; Beier, M.S.; Azad, A.F.
The lspA gene, encoding the type II signal peptidase of Rickettsia typhi: transcriptional and functional analysis
J. Bacteriol.
189
336-341
2007
Rickettsia typhi
Khandavilli, S.; Homer, K.A.; Yuste, J.; Basavanna, S.; Mitchell, T.; Brown, J.S.
Maturation of Streptococcus pneumoniae lipoproteins by a type II signal peptidase is required for ABC transporter function and full virulence
Mol. Microbiol.
67
541-557
2008
Streptococcus pneumoniae
Geukens, N.; De Buck, E.; Meyen, E.; Maes, L.; Vranckx, L.; Van Mellaert, L.; Anne, J.; Lammertyn, E.
The type II signal peptidase of Legionella pneumophila
Res. Microbiol.
157
836-841
2006
Legionella pneumophila
Arimoto, T.; 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. Immunol.
23
515-519
2008
Streptococcus mutans (Q8DUQ0), Streptococcus mutans
Banaei, N.; Kincaid, E.Z.; Lin, S.Y.; Desmond, E.; Jacobs, W.R.; Ernst, J.D.
Lipoprotein processing is essential for resistance of Mycobacterium tuberculosis to malachite green
Antimicrob. Agents Chemother.
53
3799-3802
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Schmaler, M.; Jann, N.J.; Goetz, F.; Landmann, R.
Staphylococcal lipoproteins and their role in bacterial survival in mice
Int. J. Med. Microbiol.
300
155-160
2010
Staphylococcus aureus
Das, S.; Kanamoto, T.; Ge, X.; Xu, P.; Unoki, T.; Munro, C.L.; Kitten, T.
Contribution of lipoproteins and lipoprotein processing to endocarditis virulence in Streptococcus sanguinis
J. Bacteriol.
191
4166-4179
2009
Streptococcus sanguinis, Streptococcus sanguinis SK36
Vickerman, M.M.; Flannagan, S.E.; Jesionowski, A.M.; Brossard, K.A.; Clewell, D.B.; Sedgley, C.M.
A genetic determinant in Streptococcus gordonii Challis encodes a peptide with activity similar to that of enterococcal sex pheromone cAM373, which facilitates intergeneric DNA transfer
J. Bacteriol.
192
2535-2545
2010
Streptococcus gordonii
Xiao, Y.; Gerth, K.; Mueller, R.; Wall, D.
Myxobacteria antibiotic TA (myxovirescin) inhibits type II signal peptidase
Antimicrob. Agents Chemother.
56
2014-2021
2012
Escherichia coli
Huettl, S.; Helfrich, F.; Mentrup, T.; Held, S.; Fukumori, A.; Steiner, H.; Saftig, P.; Fluhrer, R.; Schroeder, B.
Substrate determinants of signal peptide peptidase-like 2a (SPPL2a)-mediated intramembrane proteolysis of the invariant chain CD74
Biochem. J.
473
1405-1422
2016
Mus musculus
Niemeyer, J.; Mentrup, T.; Heidasch, R.; Mueller, S.A.; Biswas, U.; Meyer, R.; Papadopoulou, A.A.; Dederer, V.; Haug-Kroeper, M.; Adamski, V.; Luellmann-Rauch, R.; Bergmann, M.; Mayerhofer, A.; Saftig, P.; Wennemuth, G.; Jessberger, R.; Fluhrer, R.; Lichtenthaler, S.F.; Lemberg, M.K.; Schroeder, B.
The intramembrane protease SPPL2c promotes male germ cell development by cleavingphospholamban
EMBO Rep.
20
e46449
2019
Mus musculus
Hsu, F.F.; Chou, Y.T.; Chiang, M.T.; Li, F.A.; Yeh, C.T.; Lee, W.H.; Chau, L.Y.
Signal peptide peptidase promotes tumor progression via facilitating FKBP8 degradation
Oncogene
38
1688-1701
2019
Homo sapiens
Vogeley, L.; El Arnaout, T.; Bailey, J.; Stansfeld, P.J.; Boland, C.; Caffrey, M.
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
Science
351
876-880
2016
Pseudomonas aeruginosa
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