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Literature summary extracted from

  • Chi, Y.C.; Rahkola, J.T.; Kendrick, A.A.; Holliday, M.J.; Paukovich, N.; Roberts, T.S.; Janoff, E.N.; Eisenmesser, E.Z.
    Streptococcus pneumoniae IgA1 protease a metalloprotease that can catalyze in a split manner in vitro (2017), Protein Sci., 26, 600-610 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.13 recombinant expression of N-terminally tagged wild-type and mutant active mature enzymes in Escherichia coli strain BL21(DE3). The constructs contain an N-terminal 6xHis tag and a C-terminal MBP tag harboring an N-terminal TEV cleavage site and a C-terminal thrombin cleavage site, respectively, or the constructs contain a C-terminal His6-tag with thrombin cleavage site Streptococcus pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.13 E1605A site-directed mutagenesis, the IgA1P mutation completely abrogates the proteolytic activity Streptococcus pneumoniae
3.4.24.13 E1628A site-directed mutagenesis, the IgA1P mutation reduces the proteolytic activity of the enzyme Streptococcus pneumoniae
3.4.24.13 E1661A site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type Streptococcus pneumoniae
3.4.24.13 E1695A site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type Streptococcus pneumoniae
3.4.24.13 E1698A site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type Streptococcus pneumoniae
3.4.24.13 additional information proteolytic preparation of wild-type and mutant N- and C-terminal constructs of the recombinant enzyme: IgA1P154-1963, E1605A-IgA1P, IgA1P154-1611, IgA1P1612-1963, and IgA1P1593-1963 and the combination of IgA1P154-1611 and IgA1P1612-196. The Streptococcus pneumoniae IgA1P activity can be reconstituted in trans by the independently purified N-terminal and C-terminal domains Streptococcus pneumoniae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.13 EDTA
-
 Streptococcus pneumoniae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.13 cell surface
-
 Streptococcus pneumoniae 9986
-
3.4.24.13 extracellular
-
 Streptococcus pneumoniae
-
-
3.4.24.13 additional information the mature Streptococcus pneumoniae IgA1P form is both attached to the bacterial cell surface and released in its full form Streptococcus pneumoniae
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.13 Zn2+ dependent on, metalloproteinase, the enzyme owns a conserved HExxH Zn-binding motif (1604-1608), which coordinates Zn2+ via residues His1604 and His1608, and a third one, and provides the catalytic base, Glu1605 Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.13 human immunoglobulin A1 + H2O Streptococcus pneumoniae specific cleavage in the hinge region ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.13 Streptococcus pneumoniae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.13 proteolytic modification the fully mature form of Streptococcus pneumoniae IgA1P comprises residues 154-1963 Streptococcus pneumoniae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.13 recombinant N-terminally tagged wild-type and mutant active mature enzymes from Escherichia coli strain BL21(DE3) by nickel and amylose affinity chromatography, MBP-tag cleavage through TEV and the His-tag through thrombin, and gel filtration. Recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography an, tag cleavage through thrombin, and gel filtration Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.13 human immunoglobulin A1 + H2O specific cleavage in the hinge region Streptococcus pneumoniae ?
-
 ?
3.4.24.13 human immunoglobulin A1 + H2O specific cleavage in the hinge region, the C-terminal region of enzyme IgA1P is necessary for cleavage of IgA1 Streptococcus pneumoniae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.13 IgA1 protease
-
 Streptococcus pneumoniae
3.4.24.13 IgA1P
-
 Streptococcus pneumoniae
3.4.24.13 Streptococcus pneumoniae IgA1 protease
-
 Streptococcus pneumoniae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.13 22
-
 assay at room temperature Streptococcus pneumoniae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.13 7.4
-
 assay at Streptococcus pneumoniae

General Information

EC Number General Information Comment Organism
3.4.24.13 additional information the conserved HExxH motif (amino acid residues 1604-1608) coordinates Zn2+ and provides the catalytic base, Glu1605. Residue Glu1628 also contributes to IgA1P catalytic activity. The C-terminal domain, IgA1P1612-1963, exhibits no detectable binding to IgA1. The Streptococcus pneumoniae IgA1P N- and C-terminal regions are catalytically active when combined in trans Streptococcus pneumoniae
3.4.24.13 physiological function IgA1 protease (IgA1P) specifically cleaves human immunoglobulin A1 (IgA1) at the hinge region dissociating the effector Fc region while the IgA1 FAB remains bound to the bacterial surface. This cleavage promotes infection by two mechanisms. Firstly, Fc receptors on neutrophils can no longer recognize the cleaved and released IgA1 Fc to bind and kill the bacterial cells. Secondly, the IgA1 FAB fragment remaining on the Streptococcus pneumoniae cell surface enhances Streptococcus pneumoniae binding to epithelial cells and can no longer prevent colonization Streptococcus pneumoniae