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2 amylase-binding adhesin AbpA
(amylase-binding adhesin AbpA)2 + H2O
AbpA-LPKTSAVKLE-green fluorescent protein + H2O
AbpA-LPKT + SAVKLE-green fluorescent protein
Abz-KDFEVPTGVAM-Dap(Dnp)-NH2 + H2O
?
Dabcyl-QANPQTNEE-Edans + H2O
Dabcyl-QANPQT + NEE-Edans
DNPNTGDE + H2O
?
-
-
-
-
?
Lmo2185 + H2O
?
-
-
-
-
?
Lmo2186 + H2O
?
-
NPKSS is a sorting motif of Lmo2186. Recognition of NPKSS by SrtB, even when placed in the context of the heterologous sorting signal of Lmo2185. Proline at position 2, and not lysine at position 3, is essential for the recognition of NPKSS by SrtB
-
-
?
SvpA + H2O
?
-
anchoring of SvpA to the bacterial cell wall is specifically mediated by SrzB
-
-
?
additional information
?
-
2 amylase-binding adhesin AbpA
(amylase-binding adhesin AbpA)2 + H2O
-
-
-
?
2 amylase-binding adhesin AbpA
(amylase-binding adhesin AbpA)2 + H2O
-
-
-
?
AbpA-LPKTSAVKLE-green fluorescent protein + H2O
AbpA-LPKT + SAVKLE-green fluorescent protein
C-terminal sequence of AbpA fused to green fluorescent protein
-
-
?
AbpA-LPKTSAVKLE-green fluorescent protein + H2O
AbpA-LPKT + SAVKLE-green fluorescent protein
C-terminal sequence of AbpA fused to green fluorescent protein
-
-
?
Abz-KDFEVPTGVAM-Dap(Dnp)-NH2 + H2O
?
-
-
-
-
?
Abz-KDFEVPTGVAM-Dap(Dnp)-NH2 + H2O
?
-
-
-
-
?
Dabcyl-QANPQTNEE-Edans + H2O
Dabcyl-QANPQT + NEE-Edans
-
-
-
-
?
Dabcyl-QANPQTNEE-Edans + H2O
Dabcyl-QANPQT + NEE-Edans
-
-
-
-
?
IsdC + H2O
?
-
IsdC is a surface protein necessary for heme iron uptake in Bacillus anthracis. SrtB recognizes the NPKTG sequence present
-
-
?
IsdC + H2O
?
-
the enzyme cleaves the C-terminal sorting signal of IsdC at the NPQTN motif and rethers the polypeptide to the pentaglycine cell wall cross-bridge. During catalysis, the active site cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges
-
-
?
IsdC + H2O
?
-
the enzyme anchors the IsdC precursor with a C-terminal NPQTN motif sorting sognal, to the cell wall envelope. The sorting signal of IsdC is cleaved between threonine and asparagine of the NPQTN motif, and the carboxyl group of the thrteonine is amide-linked to the amino group of pentaglycine cross-bridges
-
-
?
PPKTG + H2O
?
-
-
-
?
additional information
?
-
-
sortase B may be critical in the early stage of inhaltation anthrax
-
-
?
additional information
?
-
-
surface protein IsdC and sortase B are required for heme-iron scavenging of Bacillus anthracis
-
-
?
additional information
?
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anchoring of SvpA to the bacterial cell wall is specifically mediated by SrzB. The enzyme is involved in the attachment of a subset of proteins to the cell wall, most likely by recognizing an NXZTN sorting motif. SrtB-mediated anchoring can be required to anchor surface proteins involved in the adaption of this microorganism to different environmental conditions
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-
?
additional information
?
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-
the svpA-srtB locus is regulated by iron availability, mediated by Fur
-
-
?
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
-
-
?
additional information
?
-
-
gram-positive pathogenic bacteria display proteins on their surface that play important roles during infection. In Staphylococcus aureus these surface proteins are anchored to the cell wall by two sortases, sortase A and sortaseB that recognize specific surface protein sorting signals. Sortase B plays a contributing role during the pathogenesis of staphylococcal infections
-
-
?
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(Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile
berberine chloride
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
beta-sitosterol-3-O-glucopyranoside
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
coptisine
-
coptisine can bind to the active pocket of SrtB, residues Arg115, Asn116, and Ile182 play a vital role in the interaction of SrtB with coptisine. Coptisine can reduce the adhesion of Staphylococcus aureus to human lung epithelial cells
galangin
-
IC50 for recombinant SrtB(DELTA30): 0.03837 mM, no antibacterial activity against Staphylococcus aureus
galangin-3-methyl ether
-
IC50 for recombinant SrtB(DELTA30): 0.1136 mM, no antibacterial activity against Staphylococcus aureus
isorhamnetin
-
IC50 for recombinant SrtB(DELTA30): 0.04335 mM, no antibacterial activity against Staphylococcus aureus
kaempferol
-
IC50 for recombinant SrtB(DELTA30): 0.02455 mM, no antibacterial activity against Staphylococcus aureus
morin
-
IC50 for recombinant SrtB(DELTA30): 0.00854 mM, no antibacterial activity against Staphylococcus aureus
myricetin
-
IC50 for recombinant SrtB(DELTA30): 0.03689 mM, no antibacterial activity against Staphylococcus aureus
phloretin
-
compound shows little anti-Staphylococcus aureus activity, but significantly inhibit SrtB activity in vitro. Phloretin reduces human alveolar epithelial cell damage caused by Staphylococcus aureus. Phloretin directly localizes in the active pocket of SrtB and blocks substrate binding
psammaplin A1
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
quercetin
-
IC50 for recombinant SrtB(DELTA30): 0.03328 mM, no antibacterial activity against Staphylococcus aureus
quercetin-3,3'-dimethyl ether
-
IC50 for recombinant SrtB(DELTA30): 0.0603 mM, no antibacterial activity against Staphylococcus aureus
additional information
-
aryl (beta-amino)ethyl ketones inhibit sortase enzymes. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol
-
(Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile
-
potential of this inhibitor for the treatment of Staphylococcus aureus infections
(Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile
-
50% inhibition with 0.0101 mg/ml
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Jonsson, I.M.; Mazmanian, S.K.; Schneewind, O.; Bremell, T.; Tarkowski, A.
The role of Staphylococcus aureus sortase A and sortase B in murine arthritis
Microbes Infect.
5
775-780
2003
Staphylococcus aureus
brenda
Zong, Y.; Mazmanian, S.K.; Schneewind, O.; Narayana, S.V.L.
The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall
Structure
12
105-112
2004
Staphylococcus aureus
brenda
Bierne, H.; Garandeau, C.; Pucciarelli, M.G.; Sabet, C.; Newton, S.; Garcia-del Portillo, F.; Cossart, P.; Charbit, A.
Sortase B, a new class of sortase in Listeria monocytogenes
J. Bacteriol.
186
1972-1982
2004
Listeria monocytogenes
brenda
Oh, K.B.; Oh, M.N.; Kim, J.G.; Shin, D.S.; Shin, J.
Inhibition of sortase-mediated Staphylococcus aureus adhesion to fibronectin via fibronectin-binding protein by sortase inhibitors
Appl. Microbiol. Biotechnol.
70
102-106
2006
Staphylococcus aureus
brenda
Kang, S.S.; Kim, J.G.; Lee, T.H.; Oh, K.B.
Flavonols inhibit sortases and sortase-mediated Staphylococcus aureus clumping to fibrinogen
Biol. Pharm. Bull.
29
1751-1755
2006
Staphylococcus aureus
brenda
Zink, S.D.; Burns, D.L.
Importance of srtA and srtB for growth of Bacillus anthracis in macrophages
Infect. Immun.
73
5222-5228
2005
Bacillus anthracis
brenda
Marraffini, L.A.; Schneewind, O.
Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC
J. Biol. Chem.
280
16263-16271
2005
Staphylococcus aureus
brenda
Newton, S.M.; Klebba, P.E.; Raynaud, C.; Shao, Y.; Jiang, X.; Dubail, I.; Archer, C.; Frehel, C.; Charbit, A.
The svpA-srtB locus of Listeria monocytogenes: fur-mediated iron regulation and effect on virulence
Mol. Microbiol.
55
927-940
2005
Listeria monocytogenes
brenda
Pucciarelli, M.G.; Calvo, E.; Sabet, C.; Bierne, H.; Cossart, P.; Garcia-del Portillo, F.
Identification of substrates of the Listeria monocytogenes sortases A and B by a non-gel proteomic analysis
Proteomics
5
4808-4817
2005
Listeria monocytogenes
brenda
Zhang, R.; Wu, R.; Joachimiak, G.; Mazmanian, S.K.; Missiakas, D.M.; Gornicki, P.; Schneewind, O.; Joachimiak, A.
Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site
Structure
12
1147-1156
2004
Bacillus anthracis, Staphylococcus aureus
brenda
Maresso, A.W.; Chapa, T.J.; Schneewind, O.
Surface protein IsdC and sortase B are required for heme-iron scavenging of Bacillus anthracis
J. Bacteriol.
188
8145-8152
2006
Bacillus anthracis
brenda
Maresso, A.W.; Wu, R.; Kern, J.W.; Zhang, R.; Janik, D.; Missiakas, D.M.; Duban, M.; Joachimiak, A.; Schneewind, O.
Activation of inhibitors by sortase triggers irreversible modification of the active site
J. Biol. Chem.
282
23129-23139
2007
Bacillus anthracis
brenda
Bentley, M.L.; Gaweska, H.; Kielec, J.M.; McCafferty, D.G.
Engineering the substrate specificity of Staphylococcus aureus sortase A. The beta6/beta7 loop from SrtB confers NPQTN recognition to SrtA
J. Biol. Chem.
282
6571-6581
2007
Staphylococcus aureus
brenda
Mariscotti, J.F.; Garcia-del Portillo, F.; Pucciarelli, M.G.
The Listeria monocytogenes sortase-B recognizes varied amino acids at position 2 of the sorting motif
J. Biol. Chem.
284
6140-6146
2009
Listeria monocytogenes
brenda
Oh, K.B.; Nam, K.W.; Ahn, H.; Shin, J.; Kim, S.; Mar, W.
Therapeutic effect of (Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile (DMMA) against Staphylococcus aureus infection in a murine model
Biochem. Biophys. Res. Commun.
396
440-444
2010
Staphylococcus aureus, Staphylococcus aureus Newman
brenda
Spirig, T.; Weiner, E.; Clubb, R.
Sortase enzymes in Gram-positive bacteria
Mol. Microbiol.
82
1044-1059
2011
Staphylococcus aureus (A0A0H3JPP1)
brenda
Kang, H.J.; Coulibaly, F.; Proft, T.; Baker, E.N.
Crystal structure of Spy0129, a Streptococcus pyogenes class B sortase involved in pilus assembly
PLoS ONE
6
e15969
2011
Streptococcus pyogenes, Streptococcus pyogenes M1 SF370
brenda
Jacobitz, A.W.; Wereszczynski, J.; Yi, S.W.; Amer, B.R.; Huang, G.L.; Nguyen, A.V.; Sawaya, M.R.; Jung, M.E.; McCammon, J.A.; Clubb, R.T.
Structural and computational studies of the Staphylococcus aureus sortase B-substrate complex reveal a substrate-stabilized oxyanion hole
J. Biol. Chem.
289
8891-8902
2014
Staphylococcus aureus (A0A0H2XI76), Staphylococcus aureus
brenda
Wang, G.; Gao, Y.; Wang, H.; Wang, J.; Niu, X.
Phloretin reduces cell injury and inflammation mediated by Staphylococcus aureus via targeting sortase B and the molecular mechanism
Appl. Microbiol. Biotechnol.
102
10665-10674
2018
Staphylococcus aureus
brenda
Tamai, E.; Sekiya, H.; Maki, J.; Nariya, H.; Yoshida, H.; Kamitori, S.
X-ray structure of Clostridium perfringens sortase B cysteine transpeptidase
Biochem. Biophys. Res. Commun.
493
1267-1272
2017
Clostridium perfringens (Q8XN25), Clostridium perfringens, Clostridium perfringens 13 (Q8XN25)
brenda
Puorger, C.; Di Girolamo, S.; Lipps, G.
Elucidation of the recognition sequence of sortase B from Bacillus anthracis by using a newly developed liquid chromatography-mass spectrometry-based method
Biochemistry
56
2641-2650
2017
Bacillus anthracis
brenda
Yin, J.; Fei, C.; Lo, Y.; Hsiao, Y.; Chang, J.; Nix, J.; Chang, Y.; Yang, L.; Huang, I.; Wang, S.
Structural insights into substrate recognition by Clostridium difficile sortase
Front. Cell. Infect. Microbiol.
6
00160
2016
Clostridioides difficile (Q183F3), Clostridioides difficile, Clostridioides difficile 630 (Q183F3)
brenda
Wang, G.; Wang, X.; Sun, L.; Gao, Y.; Niu, X.; Wang, H.
Novel Inhibitor discovery of Staphylococcus aureus sortase B and the mechanism confirmation via molecular modeling
Molecules
23
977
2018
Staphylococcus aureus, Staphylococcus aureus ATCC 29213
brenda
Liang, X.; Liu, B.; Zhu, F.; Scannapieco, F.; Haase, E.; Matthews, S.; Wu, H.
A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property
Sci. Rep.
6
30966
2016
Streptococcus parasanguinis (I1ZJ31), Streptococcus parasanguinis FW213 (I1ZJ31)
brenda