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Dabcyl-ancillary protein 1-Edans + H2O
?
Dabcyl-ancillary protein 2-Edans + H2O
?
Dabcyl-BP-1 peptide-Edans + H2O
?
Dabcyl-KKVTIPQTGGIGT-EDANS + H2O
?
-
-
-
?
surface protein containing a QVPTGV motif + H2O
?
-
SrtC2 anchors a surface protein containing a QVPTGV motif (followed by a hydrophobic region and a charged tail) to the cell wall
-
-
?
additional information
?
-
BasH polypeptide + H2O
?
-
sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine. Sortase C substrate BasH is expressed in the forespore
-
-
?
BasH polypeptide + H2O
?
-
sortase C specifically recognizes and cleaves the BasI LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine. Sortase C substrate BasH is expressed in the forespore
-
-
?
BasI polypeptide + H2O
?
-
sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine
-
-
?
BasI polypeptide + H2O
?
-
the LPNTA motif of BasI is cleaved between the threonine and the alanine residue. The C-terminal carboxyl group of threonine is subsequently amide linked to the side chain amino group of diaminopimelic acid within the wall peptides of Bacillus anthracis peptidoglycan (predivisional cell envelope). Sortase C with an active-site cysteine and the LPNTA sorting signal of BasI are required for anchoring of the polypeptide to the cell wall envelope
-
-
?
BasI polypeptide + H2O
?
-
sortase C specifically recognizes and cleaves the BasI LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine
-
-
?
BasI polypeptide + H2O
?
-
the LPNTA motif of BasI polypeptide is cleaved between the threonine and the alanine residue. The C-terminal carboxyl group of threonine is subsequently amide-linked to the side chain amino group of diaminopimelic acid within the wall peptides of Bacillus anthracis peptidoglycan
-
-
?
Dabcyl-ancillary protein 1-Edans + H2O
?
preferred substrate of SrtC2
-
-
?
Dabcyl-ancillary protein 1-Edans + H2O
?
Streptococcus agalactiae serogroup V ATCC BAA-611
preferred substrate of SrtC2
-
-
?
Dabcyl-ancillary protein 2-Edans + H2O
?
preferred substrate of SrtC1
-
-
?
Dabcyl-ancillary protein 2-Edans + H2O
?
Streptococcus agalactiae serogroup V ATCC BAA-611
preferred substrate of SrtC1
-
-
?
Dabcyl-BP-1 peptide-Edans + H2O
?
-
-
-
?
Dabcyl-BP-1 peptide-Edans + H2O
?
Streptococcus agalactiae serogroup V ATCC BAA-611
-
-
-
?
additional information
?
-
-
assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF
-
-
?
additional information
?
-
-
the enzyme is required for efficient pilusassembly
-
-
?
additional information
?
-
-
assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF
-
-
?
additional information
?
-
-
of the three genes for structural subunits, rrgB encodes the major pilin, while rrgA and rrgC encode ancillary pilin subunits decorating the pilus shaft and tip. Deletion of all three pilus associated sortase genes, srtB, srtC and srtD, completely prevents pilus biogenesis. Both SrtB and SrtC act as pilus subunit polymerases, with SrtB processing all three pilus subunit proteins, while SrtC processes only RrgB and RrgA
-
-
?
additional information
?
-
-
pilus-associated sortase C from Streptococcus pneumoniae acts as a polymerase for the pilus subunit proteins RrgA and RrgB
-
-
?
additional information
?
-
-
SrtC-1, SrtC-2, and SrtC-3 are responsible for RlrA pilus assembly and exhibit functional redundancy with respect to backbone assembly and cell wall localization. SrtC-3 is required for the incorporation of the accessory subunits RrgA and RrgC. Deleterious effect on pilus assembly upon alteration of the cell wall sorting signals of the accessory subunit proteins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
BasH polypeptide + H2O
?
-
sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine. Sortase C substrate BasH is expressed in the forespore
-
-
?
Dabcyl-ancillary protein 1-Edans + H2O
?
Dabcyl-ancillary protein 2-Edans + H2O
?
Dabcyl-BP-1 peptide-Edans + H2O
?
surface protein containing a QVPTGV motif + H2O
?
-
SrtC2 anchors a surface protein containing a QVPTGV motif (followed by a hydrophobic region and a charged tail) to the cell wall
-
-
?
additional information
?
-
BasI polypeptide + H2O
?
-
sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine
-
-
?
BasI polypeptide + H2O
?
-
the LPNTA motif of BasI is cleaved between the threonine and the alanine residue. The C-terminal carboxyl group of threonine is subsequently amide linked to the side chain amino group of diaminopimelic acid within the wall peptides of Bacillus anthracis peptidoglycan (predivisional cell envelope). Sortase C with an active-site cysteine and the LPNTA sorting signal of BasI are required for anchoring of the polypeptide to the cell wall envelope
-
-
?
Dabcyl-ancillary protein 1-Edans + H2O
?
preferred substrate of SrtC2
-
-
?
Dabcyl-ancillary protein 1-Edans + H2O
?
Streptococcus agalactiae serogroup V ATCC BAA-611
preferred substrate of SrtC2
-
-
?
Dabcyl-ancillary protein 2-Edans + H2O
?
preferred substrate of SrtC1
-
-
?
Dabcyl-ancillary protein 2-Edans + H2O
?
Streptococcus agalactiae serogroup V ATCC BAA-611
preferred substrate of SrtC1
-
-
?
Dabcyl-BP-1 peptide-Edans + H2O
?
-
-
-
?
Dabcyl-BP-1 peptide-Edans + H2O
?
Streptococcus agalactiae serogroup V ATCC BAA-611
-
-
-
?
additional information
?
-
-
assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF
-
-
?
additional information
?
-
-
the enzyme is required for efficient pilusassembly
-
-
?
additional information
?
-
-
assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF
-
-
?
additional information
?
-
-
of the three genes for structural subunits, rrgB encodes the major pilin, while rrgA and rrgC encode ancillary pilin subunits decorating the pilus shaft and tip. Deletion of all three pilus associated sortase genes, srtB, srtC and srtD, completely prevents pilus biogenesis. Both SrtB and SrtC act as pilus subunit polymerases, with SrtB processing all three pilus subunit proteins, while SrtC processes only RrgB and RrgA
-
-
?
additional information
?
-
-
pilus-associated sortase C from Streptococcus pneumoniae acts as a polymerase for the pilus subunit proteins RrgA and RrgB
-
-
?
additional information
?
-
-
SrtC-1, SrtC-2, and SrtC-3 are responsible for RlrA pilus assembly and exhibit functional redundancy with respect to backbone assembly and cell wall localization. SrtC-3 is required for the incorporation of the accessory subunits RrgA and RrgC. Deleterious effect on pilus assembly upon alteration of the cell wall sorting signals of the accessory subunit proteins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00358 - 0.06036
Dabcyl-ancillary protein 1-Edans
-
0.01421 - 0.02733
Dabcyl-ancillary protein 2-Edans
-
0.02156 - 0.04385
Dabcyl-BP-1 peptide-Edans
-
0.0138 - 0.0294
Dabcyl-KKVTIPQTGGIGT-EDANS
0.00358
Dabcyl-ancillary protein 1-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
0.00569
Dabcyl-ancillary protein 1-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
0.006385
Dabcyl-ancillary protein 1-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
0.06036
Dabcyl-ancillary protein 1-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
0.01421
Dabcyl-ancillary protein 2-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
0.01639
Dabcyl-ancillary protein 2-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
0.01814
Dabcyl-ancillary protein 2-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
0.02733
Dabcyl-ancillary protein 2-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
0.02156
Dabcyl-BP-1 peptide-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
0.031
Dabcyl-BP-1 peptide-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
0.03235
Dabcyl-BP-1 peptide-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
0.04385
Dabcyl-BP-1 peptide-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
0.0138
Dabcyl-KKVTIPQTGGIGT-EDANS
wild type enzyme, at 37°C in 20 mM HEPES (pH 7.5), 75 mM NaCl, and 1 mM dithiothreitol
0.0294
Dabcyl-KKVTIPQTGGIGT-EDANS
mutant enzyme Y86A, at 37°C in 20 mM HEPES (pH 7.5), 75 mM NaCl, and 1 mM dithiothreitol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00104 - 0.0049
Dabcyl-ancillary protein 1-Edans
-
0.00041 - 0.00113
Dabcyl-ancillary protein 2-Edans
-
0.000731 - 0.00298
Dabcyl-BP-1 peptide-Edans
-
0.00104
Dabcyl-ancillary protein 1-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
0.00116
Dabcyl-ancillary protein 1-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
0.00216
Dabcyl-ancillary protein 1-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
0.0049
Dabcyl-ancillary protein 1-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
0.00041
Dabcyl-ancillary protein 2-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
0.000436
Dabcyl-ancillary protein 2-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
0.00077
Dabcyl-ancillary protein 2-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
0.00113
Dabcyl-ancillary protein 2-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
0.000731
Dabcyl-BP-1 peptide-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
0.00106
Dabcyl-BP-1 peptide-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
0.00177
Dabcyl-BP-1 peptide-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
0.00298
Dabcyl-BP-1 peptide-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
16.2 - 810
Dabcyl-ancillary protein 1-Edans
-
159 - 797
Dabcyl-ancillary protein 2-Edans
-
243 - 922
Dabcyl-BP-1 peptide-Edans
-
16.2
Dabcyl-ancillary protein 1-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
32.5
Dabcyl-ancillary protein 1-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
38.1
Dabcyl-ancillary protein 1-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
810
Dabcyl-ancillary protein 1-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
159
Dabcyl-ancillary protein 2-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
226
Dabcyl-ancillary protein 2-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
470
Dabcyl-ancillary protein 2-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
797
Dabcyl-ancillary protein 2-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
243
Dabcyl-BP-1 peptide-Edans
F86A mutant isoform SrtC2, at pH 7.5 and 37°C
-
339
Dabcyl-BP-1 peptide-Edans
wild type isoform SrtC2, at pH 7.5 and 37°C
-
570
Dabcyl-BP-1 peptide-Edans
wild type isoform SrtC1, at pH 7.5 and 37°C
-
922
Dabcyl-BP-1 peptide-Edans
Y92A mutant isoform SrtC1, at pH 7.5 and 37°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hanging drop vapor diffusion method, using 10% (w/v) PEG monomethyl ether 2000 and 100 mM MES (pH 6.4)
-
sitting drop vapor diffusion method, using 100 mM Tris (pH 8.5), 200 mM NaOAc, and 30% (w/v) PEG-4000
apoprotein, hanging drop vapor diffusion method, using 15-25% (w/v) polyethylene glycol 3350 and 0.2 M Tris buffer (pH 8.0-8.8) and 0.2 M ammonium acetate at 4°C. In complex with inhibitor 2-(trimethylammonium)ethyl thiol, hanging drop vapor diffusion method, using 1.6 M ammonium sulfate, 5% (w/v) polyethylene glycol 3350, and sodium cacodylate (pH 6.5) at 4°C
isofofm SrtC1, hanging drop vapor diffusion method, using 0.4 M sodium formate, 0.1 M Bis-Tris propane pH 6.5, and 22% (w/v) PEG 3350. Isoform SrtC1, hanging drop vapor diffusion method, using 0.26 M CaCl2, 19% (w/v) PEG 6000, 0.1 M HEPES pH 7.0
molecular dynamics simulations of SrtC isozymes with the sorting signals of RrgA, RrgB, and RrgC to determine the structural and thermodynamic basis of pilin recognition. Both isozymes SrtC-1 and SrtC-3 are selective for RrgB. This specificity is tuned by the sorting signal binding conformation in which the first two residue side-chains complement hydrophobic residues around the active site, while the third residue projects away from the catalytic triad and makes specific interactions based on its charge and reach
-
molecular dynamics simulations of SrtC isozymes with the sorting signals of RrgA, RrgB, and RrgC to determine the structural and thermodynamic basis of pilin recognition. SrtC-2 is selective for RrgA. This specificity is tuned by the sorting signal binding conformation in which the first two residue sidechains complement hydrophobic residues around the active site, while the third residue projects away from the catalytic triad and makes specific interactions based on its charge and reach
-
sitting drop vapor diffusion method
three different crystals are obtained using both the sitting-drop and hanging-drop vapour-diffusion methods. The three crystals belonged to different space groups and diffracted to resolutions ranging between 2.3 and 1.7 A. One crystal form belongs to space group P212121, with unit cell parameters a = 48.9, b = 96.9, c = 98.9 A, alpha = beta = gamma = 90°. The other two crystal forms belong to space group P222, with unit-cell parameters a = 48.8, b = 97.2, c= 99.2 A, alpha = beta = gamma = 90° and a = 48.6, b= 96.5, c = 98.8 A, alpha = beta = gamma = 90°, respectively
-
hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.5, 0.54 M sodium citrate, 8% (v/v) iso-propanol, 8% (v/v) tert-butanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Neiers, F.; Madhurantakam, C.; Flker, S.; Normark, S.; Henriques-Normark, B.; Achour, A.
Cloning, expression, purification, crystallization and preliminary X-ray analysis of the pilus-associated sortase C from Streptococcus pneumoniae
Acta Crystallogr. Sect. F
65
55-58
2009
Streptococcus pneumoniae
brenda
Barnett, T.C.; Patel, A.R.; Scott, J.R.
A novel sortase, SrtC2, from Streptococcus pyogenes anchors a surface protein containing a QVPTGV motif to the cell wall
J. Bacteriol.
186
5865-5875
2004
Streptococcus pyogenes
brenda
Marraffini, L.A.; Schneewind, O.
Sortase C-mediated anchoring of BasI to the cell wall envelope of Bacillus anthracis
J. Bacteriol.
189
6425-6436
2007
Bacillus anthracis
brenda
LeMieux, J.; Woody, S.; Camilli, A.
Roles of the sortases of Streptococcus pneumoniae in assembly of the RlrA pilus
J. Bacteriol.
190
6002-6013
2008
Streptococcus pneumoniae
brenda
Kline, K.A.; Kau, A.L.; Chen, S.L.; Lim, A.; Pinkner, J.S.; Rosch, J.; Nallapareddy, S.R.; Murray, B.E.; Henriques-Normark, B.; Beatty, W.; Caparon, M.G.; Hultgren, S.J.
Mechanism for sortase localization and role in efficient pilus assembly in Enterococcus faecalis
J. Bacteriol.
191
3237-3247
2009
Enterococcus faecalis
brenda
Nallapareddy, S.R.; Singh, K.V.; Sillanp, J.; Garsin, D.A.; Hk, M.; Erlandsen, S.L.; Murray, B.E.
Endocarditis and biofilm-associated pili of Enterococcus faecalis
J. Clin. Invest.
116
2799-2807
2006
Enterococcus faecalis, Enterococcus faecalis OG1RF
brenda
Marraffini, L.A.; Schneewind, O.
Targeting proteins to the cell wall of sporulating Bacillus anthracis
Mol. Microbiol.
62
1402-1417
2006
Bacillus anthracis
brenda
Flker, S.; Nelson, A.L.; Morfeldt, E.; Jonas, K.; Hultenby, K.; Ries, J.; Melefors, O.; Normark, S.; Henriques-Normark, B.
Sortase-mediated assembly and surface topology of adhesive pneumococcal pili
Mol. Microbiol.
70
595-607
2008
Streptococcus pneumoniae
brenda
Neiers, F.; Madhurantakam, C.; Faelker, S.; Manzano, C.; Dessen, A.; Normark, S.; Henriques-Normark, B.; Achour, A.
Two crystal structures of pneumococcal pilus sortase C provide novel insights into catalysis and substrate specificity
J. Mol. Biol.
393
704-716
2009
Streptococcus pneumoniae (A0A0H2UNU0), Streptococcus pneumoniae
brenda
Cozzi, R.; Malito, E.; Nuccitelli, A.; DOnofrio, M.; Martinelli, M.; Ferlenghi, I.; Grandi, G.; Telford, J.L.; Maione, D.; Rinaudo, C.D.
Structure analysis and site-directed mutagenesis of defined key residues and motives for pilus-related sortase C1 in group B Streptococcus
FASEB J.
25
1874-1886
2011
Streptococcus agalactiae (Q69EY7)
brenda
Khare, B.; Fu, Z.Q.; Huang, I.H.; Ton-That, H.; Narayana, S.V.
The crystal structure analysis of group B Streptococcus sortase C1: a model for the "lid" movement upon substrate binding
J. Mol. Biol.
414
563-577
2011
Streptococcus agalactiae serogroup V (Q8E0S7), Streptococcus agalactiae serogroup V ATCC BAA-611 (Q8E0S7)
brenda
Khare, B.; Krishnan, V.; Rajashankar, K.R.; I-Hsiu, H.; Xin, M.; Ton-That, H.; Narayana, S.V.
Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1
PLoS ONE
6
e22995
2011
Streptococcus agalactiae, Streptococcus agalactiae 2603 V/R
brenda
Lu, G.; Qi, J.; Gao, F.; Yan, J.; Tang, J.; Gao, G.
A novel "open-form" structure of sortaseC from Streptococcus suis
Proteins
79
2764-2769
2011
Streptococcus suis (A4VY75), Streptococcus suis 05ZYH33 (A4VY75)
brenda
Cozzi, R.; Prigozhin, D.; Rosini, R.; Abate, F.; Bottomley, M.J.; Grandi, G.; Telford, J.L.; Rinaudo, C.D.; Maione, D.; Alber, T.
Structural basis for group B Streptococcus pilus 1 sortases C regulation and specificity
PLoS ONE
7
e49048
2012
Streptococcus agalactiae serogroup V (Q8E0S7), Streptococcus agalactiae serogroup V ATCC BAA-611 (Q8E0S7)
brenda
Oxaran, V.; Ledue-Clier, F.; Dieye, Y.; Herry, J.M.; Pechoux, C.; Meylheuc, T.; Briandet, R.; Juillard, V.; Piard, J.C.
Pilus biogenesis in Lactococcus lactis: molecular characterization and role in aggregation and biofilm formation
PLoS ONE
7
e50989
2012
Lactococcus lactis (Q9CHH2), Lactococcus lactis, Lactococcus lactis IL1403 (Q9CHH2)
brenda
Naziga, E.B.; Wereszczynski, J.
Molecular mechanisms of the binding and specificity of Streptooccus pneumoniae sortase C enzymes for pilin subunits
Sci. Rep.
7
13119
2017
Streptococcus pneumoniae
brenda