BRENDA - Enzyme Database show
show all sequences of 3.4.23.36

Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene

Innis, M.A.; Tokunaga, M.; Williams, M.E.; Loranger, J.M.; Chang, S.Y.; Chang, S.; Wu, H.C.; Proc. Natl. Acad. Sci. USA 81, 3708-3712 (1984)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18140
-
E. coli, calculation from nucleotide sequence
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18140
-
E. coli, calculation from nucleotide sequence
Escherichia coli
Other publictions for EC 3.4.23.36
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
717100
Xiao
Myxobacteria antibiotic TA (my ...
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56
2014-2021
2012
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708786
Schmaler
Staphylococcal lipoproteins an ...
Staphylococcus aureus
Int. J. Med. Microbiol.
300
155-160
2010
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708937
Vickerman
A genetic determinant in Strep ...
Streptococcus gordonii
J. Bacteriol.
192
2535-2545
2010
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1
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1
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1
1
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707166
Banaei
Lipoprotein processing is esse ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Antimicrob. Agents Chemother.
53
3799-3802
2009
-
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2
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163
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2
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2
2
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708925
Das
Contribution of lipoproteins a ...
Streptococcus sanguinis, Streptococcus sanguinis SK36
J. Bacteriol.
191
4166-4179
2009
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2
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9
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2
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1
1
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682007
Khandavilli
Maturation of Streptococcus pn ...
Streptococcus pneumoniae
Mol. Microbiol.
67
541-557
2008
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1
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1
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4
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1
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1
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700533
Arimoto
Role of prolipoprotein diacylg ...
Streptococcus mutans
Oral Microbiol. Immunol.
23
515-519
2008
-
-
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-
1
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3
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680486
Rahman
The lspA gene, encoding the ty ...
Rickettsia typhi
J. Bacteriol.
189
336-341
2007
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1
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1
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1
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5
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1
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1
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682822
Geukens
The type II signal peptidase o ...
Legionella pneumophila
Res. Microbiol.
157
836-841
2006
-
1
1
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5
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668802
Sankaran
-
Signal peptidase II ...
Bacillus subtilis, Escherichia coli, Klebsiella aerogenes, Myxococcus xanthus, Pseudomonas fluorescens, Staphylococcus aureus
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
201-204
2004
1
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5
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10
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6
6
2
6
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6
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2
1
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19
5
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1
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7
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1
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1
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5
6
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10
1
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2
6
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1
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19
5
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1
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7
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670307
Sander
Lipoprotein processing is requ ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Mol. Microbiol.
52
1543-1552
2004
-
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1
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1
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2
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161
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1
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2
1
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670851
Gonnet
Fine-tuning the prediction of ...
Escherichia coli K-12
Proteomics
4
1597-1613
2004
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4
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651951
Tjalsma
The potential active site of t ...
Bacillus subtilis
J. Biol. Chem.
274
28191-28197
1999
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1
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16
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4
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1
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16
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1
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30813
Sankaran
Bacterial prolipoprotein signa ...
Escherichia coli, Escherichia coli B / ATCC 11303
Methods Enzymol.
248
169-180
1995
2
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1
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1
9
1
1
1
1
2
-
177
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1
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1
6
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1
1
1
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1
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2
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1
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1
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9
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1
1
1
1
2
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1
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1
6
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1
1
1
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1
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30814
Zhao
Nucleotide sequence of the Sta ...
Staphylococcus aureus
FEBS Lett.
299
80-84
1992
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1
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1
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6
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30809
Isaki
Cloning and nucleotide sequenc ...
Klebsiella aerogenes
J. Bacteriol.
172
469-472
1990
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1
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3
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30812
Dev
Signal peptidases and signal p ...
Escherichia coli
J. Bioenerg. Biomembr.
22
271-290
1990
2
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1
1
1
1
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1
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1
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1
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30808
Innis
Nucleotide sequence of the Esc ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
81
3708-3712
1984
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30810
Yu
Nucleotide sequence of the lsp ...
Escherichia coli
FEBS Lett.
173
264-268
1984
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1
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30811
Yamada
The major outer membrane lipop ...
Escherichia coli
FEBS Lett.
166
179-182
1984
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1
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2
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1
1
4
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