BRENDA - Enzyme Database show
show all sequences of 3.4.22.71

Identification of substrates of the Listeria monocytogenes sortases A and B by a non-gel proteomic analysis

Pucciarelli, M.G.; Calvo, E.; Sabet, C.; Bierne, H.; Cossart, P.; Garcia-del Portillo, F.; Proteomics 5, 4808-4817 (2005)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Listeria monocytogenes
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
non-gel proteomics is a powerful technique to rapidly identify sortase substrates and to gain insights on potential sorting motifs. Two surface proteins, Lmo2185 and Lmo2186 are identified only when SrtB is active. The analysis of the peptides identified in these proteins suggests that SrtB of Listeria monocytogenes may recognize two different sorting motifs, NXZTN and NPKXZ
666890
Listeria monocytogenes
?
-
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
non-gel proteomics is a powerful technique to rapidly identify sortase substrates and to gain insights on potential sorting motifs. Two surface proteins, Lmo2185 and Lmo2186 are identified only when SrtB is active. The analysis of the peptides identified in these proteins suggests that SrtB of Listeria monocytogenes may recognize two different sorting motifs, NXZTN and NPKXZ
666890
Listeria monocytogenes
?
-
-
-
-
Other publictions for EC 3.4.22.71
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)
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Crystal structure of Spy0129, ...
Streptococcus pyogenes, Streptococcus pyogenes M1 SF370
PLoS ONE
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e15969
2011
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440-444
2010
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693248
Mariscotti
The Listeria monocytogenes sor ...
Listeria monocytogenes
J. Biol. Chem.
284
6140-6146
2009
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680796
Maresso
Activation of inhibitors by so ...
Bacillus anthracis
J. Biol. Chem.
282
23129-23139
2007
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680881
Bentley
Engineering the substrate spec ...
Staphylococcus aureus
J. Biol. Chem.
282
6571-6581
2007
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663737
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Inhibition of sortase-mediated ...
Staphylococcus aureus
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70
102-106
2006
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664280
Kang
Flavonols inhibit sortases and ...
Staphylococcus aureus
Biol. Pharm. Bull.
29
1751-1755
2006
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680473
Maresso
Surface protein IsdC and sorta ...
Bacillus anthracis
J. Bacteriol.
188
8145-8152
2006
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665174
Zink
Importance of srtA and srtB fo ...
Bacillus anthracis
Infect. Immun.
73
5222-5228
2005
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665617
Marraffini
Anchor structure of staphyloco ...
Staphylococcus aureus
J. Biol. Chem.
280
16263-16271
2005
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666393
Newton
The svpA-srtB locus of Listeri ...
Listeria monocytogenes
Mol. Microbiol.
55
927-940
2005
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666890
Pucciarelli
Identification of substrates o ...
Listeria monocytogenes
Proteomics
5
4808-4817
2005
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647690
Zong
The structure of sortase B, a ...
Staphylococcus aureus
Structure
12
105-112
2004
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647691
Bierne
Sortase B, a new class of sort ...
Listeria monocytogenes
J. Bacteriol.
186
1972-1982
2004
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666932
Zhang
Structures of sortase B from S ...
Bacillus anthracis, Staphylococcus aureus
Structure
12
1147-1156
2004
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647386
Jonsson
The role of Staphylococcus aur ...
Staphylococcus aureus
Microbes Infect.
5
775-780
2003
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