Any feedback?
Information on EC 3.4.24.13 - IgA-specific metalloendopeptidase
for references in articles please use BRENDA:EC3.4.24.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.24.13 IgA-specific metalloendopeptidaseSpecify your search results
Word Map
- 3.4.24.13
- medicine
- hinge
- gonorrhoeae
- influenzae
-
haemophilus
- proteinases
-
neisserial
-
20-year
-
colostrum
-
nontypeable
- fcalpha
-
hexxh
- meningitidis
- airways
- tetrapeptide
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Cleavage of Pro-/-Thr bond in the hinge region of the heavy chain of human IgA
Synonyms
streptococcus pneumoniae iga1 protease, iga1 proteinase, iga protease b1, igab1, zinc metalloprotease zmpc, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HP1022
IgA protease
IgA1 protease
IgA1 proteinase
-
-
-
-
IgA1-specific proteinase
-
-
-
-
IgA1P
IgA1pr
igaB
IgaB2
immunoglobulin A1 protease
proteinase, immunoglobulin A1
-
-
-
-
zinc metalloprotease zmpC
IgA1 protease
-
-
-
-
IgA1 protease
Neisseria meningitidis serogroup B B44/76
-
-
-
IgA1 protease
-
IgA1pr
Neisseria meningitidis serogroup B B44/76
-
-
-
igaB
-
represents a second immunoglobulin A1 protease gene in nontypeable Haemophilus influenza
immunoglobulin A1 protease
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of Pro-/-Thr bond in the hinge region of the heavy chain of human IgA
localization of the cleavage site specificity determinant
-
Cleavage of Pro-/-Thr bond in the hinge region of the heavy chain of human IgA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
-
hydrolysis of peptide bond
-
-
peptides, endopeptidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
72231-73-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human immunoglobulin A1 + H2O
Fc fragment + Fab fragment
-
cleavage of the hinge region
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fc + immunoglobulin Fab
-
cleavage of the hinge region
-
-
?
immunoglobulin A1 + H2O
immunoglobulin A1 Fabalpha fragments + immunglobulin A1 Fcalpha
-
-
-
-
?
immunoglobulin IgA1 + H2O
effector domain of IgA1 + Fab determinants of IgA1
-
-
specific cleavage of hinge region. IgA1 bound to bacterial porin A is masked by the serogroup B polysaccharide capsule and less accessible to degradation. De novo synthesis of enzyme is required for degradation of porin-A-bound IgA1, specific cleavage of hinge region
-
?
Dabcyl-gammaPRPPAPVFY-Edans + H2O
Dabcyl-gammaPRPP + APVFY-Edans
-
-
-
?
Dabcyl-gammaPRPPAPVFY-Edans + H2O
Dabcyl-gammaPRPP + APVFY-Edans
-
-
-
?
human IgA1 + H2O
?
-
-
cleavage of the peptide bond between amino acid residues 231-232 in each alpha chain
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
human IgA1 possesses a unique hinge region composed of a repeated sequence rich in proline, serine and threonine, which are the specific cleavage sites of IgA1 protease
-
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
?
-
-
-
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
?
-
-
-
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
?
-
-
-
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
?
-
-
-
-
?
human immunoglobulin A1 + H2O
?
-
specific cleavage in the hinge region
-
-
?
human immunoglobulin A1 + H2O
?
-
specific cleavage in the hinge region, the C-terminal region of enzyme IgA1P is necessary for cleavage of IgA1
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
Immunoglobulin A1 + H2O
?
-
amino acid sequence requirements in the hinge of human immunoglobulin A1. Absolute requirement for Pro227 but not for Thr228, which can be replaced by Val. Enzyme from different strains may have different amino acid requirements for cleavage
-
?
Immunoglobulin A1 + H2O
?
-
amino acid sequence requirements in the hinge of human immunoglobulin A1. Absolute requirement for Pro227 but not for Thr228, which can be replaced by Val
-
?
Immunoglobulin A1 + H2O
?
-
amino acid sequence requirements in the hinge of human immunoglobulin A1. The enzyme shows no absolute requirement for either Pro or Thr at residue 227 to 228
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
amino acid sequence requirements in the hinge of human immunoglobulin A1. Absolute requirement for Pro227 but not for Thr228, which can be replaced by Val
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
cleavage products have MW of 30000 Da and 33000 Da
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
type 1 protease cleaves peptide bond Pro231-Ser232
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
type 2 protease cleaves peptide bond 235-236
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
type 3 protease cleaves peptide bond 237-238
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
Fsalpha1 fragment + Fcalpha1 fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
alpha-chain
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
type 2 enzyme cleaves peptide bond 235-236, type 1 enzyme cleaves bond 237-238 in the alpha chain of IgA
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
cleavage of peptide bond Pro235-Thr236
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
the activity level of the type 2 enzyme is 10fold that observed for the type 1 enzyme
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
type 2 protease cleaves peptide bond 235-236
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
type 1 protease cleaves peptide bond 237-238
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
specific for human IgA1
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
enzyme cleaves the alpha-chain at the Pro223-Ser224 bond
Fcalpha fragment + Fabalpha fragment
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
Streptococcus mitior
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
cleavage products have MW of 30000 Da and 33000 Da
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
cleaves peptide bond Pro227-Thr228
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
cleaves peptide bond Pro227-Thr228
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
cleavage of peptide bond Pro235-Thr236
MW of the Fabalpha fragment is 28500 Da and the MW of the Fcalpha fragement is 33000 Da
?
LAMP1 + H2O
?
-
i.e. lysosome-associated membrane protein 1. The enzyme cleaves LAMP1 thereby accelerating its degradation rate in infected A431 human epidermoid carcinoma cells and resulting in the alteration of lysosomes
-
?
LAMP1 + H2O
?
-
i.e. lysosome-associated membrane protein 1. The enzyme cleaves LAMP1 thereby accelerating its degradation rate in infected A431 human epidermoid carcinoma cells and resulting in the alteration of lysosomes. Infection of T84 monolayers also results in IgA1 protease-mediated reduction of LAMP1
-
?
LAMP1 + H2O
?
-
LAMP1 is a major integral membrane glycoprotein of lysosomes and significantly reduces its steady-state levels in an infected cell. Pilus-induced Ca2+ flux triggers lysosome exocytosis and increases the amount of LAMP1 accessible to IgA1 protease
-
?
NIVVAPPSPQANQAEEY + H2O
NIVVAPP + SPQANQAEEY
-
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 protease is an important factor of meningitis
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
retained antigen-binding activity of Fabalpha fragments of human monoclonal immunoglobulin A1 cleaved by IgA 1 protease opens the possibility that IgA1 protease-producing bacteria growing in the presence of IgA1 antibodies are coated with Fabalpha fragments. Such fragments may conceivably protect the microorganism from the immune system by blocking access of intact antibody molecules of the same or other isotypes and of immunocompetent cells
-
-
?
additional information
?
-
-
IgA1 protease of the Brazilian purpuric fever clone may contribute to the pathogenic potential of the virulent phenotype in Brazil
-
-
?
additional information
?
-
-
the enzyme cleaves myeloma IgA1 and secretory IgA but not myeloma IgA2, IgM, or IgG
-
-
?
additional information
?
-
-
enzyme requires 10 or more appropriate amino acids between the Fab and Fc region to maintain a minimum critical distance between the scissile bond and the start of the Fc
-
-
?
additional information
?
-
-
no substrate: human IgA1 with CH3 domain exchanged for that of human IgG1. CH3 domain residues E403, Q406, T409 influence sensitivity to cleavage by enzyme
-
-
?
additional information
?
-
-
all three forms of capsule-specific IgA show comparable susceptibilities to cleavage by bacterial IgA1 protease, demonstrating that secretory component does not prevent the proteolytic degradation of IgA1 by IgA1 protease. IgA1 cleavage results in formation of identical Fab fragments for each of the molecular forms, thereby abolishing the contribution of multivalence of polymeric IgA and secretory IgA
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
the cleavage of IgA1 by gonococcal IgA1 protease within the lumen of the female lower genital tract is unlikely to be a significant factor in the pathogenesis of infections by Neisseria gonorrhoeae
-
-
?
additional information
?
-
-
enzyme requires 9 or more appropriate amino acids between the Fab and Fc region to maintain a minimum critical distance between the scissile bond and the start of the Fc
-
-
?
additional information
?
-
-
no substrate: human IgA1 with CH3 domain exchanged for that of human IgG1
-
-
?
additional information
?
-
-
IgA1 protease is an important factor of meningitis
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
enzyme requires 10 or more appropriate amino acids between the Fab and Fc region to maintain a minimum critical distance between the scissile bond and the start of the Fc
-
-
?
additional information
?
-
-
no substrate: human IgA1 with CH3 domain exchanged for that of human IgG1
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
Streptococcus mitior
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
no substrate: IgA2-IgA1 half hinge, an antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
potential impotance of IgA proteases as an ecological determinant in the oral cavity and their role as a determinant of pathogenesis of pathogenic bacteria whose portal of entry is the mucosal surface
-
-
?
additional information
?
-
-
no substrate: IgA2-IgA1 half hinge, an antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
IgA1 protease is an important factor of meningitis
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
the enzyme cleaves myeloma IgA1 and secretory IgA but not myeloma IgA2, IgM, or IgG
-
-
?
additional information
?
-
-
enzyme requires 12 or more appropriate amino acids between the Fab and Fc region to maintain a minimum critical distance between the scissile bond and the start of the Fc
-
-
?
additional information
?
-
-
polymeric and secretory IgA show comparable susceptibilities to functional inhibition by bacterial IgA1 protease cleavage, demonstrating that secretory component does not prevent the proteolytic degradation of IgA1 by IgA1 protease
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
enzyme requires 12 or more appropriate amino acids between the Fab and Fc region to maintain a minimum critical distance between the scissile bond and the start of the Fc
-
-
?
additional information
?
-
-
no substrate: IgA2-IgA1 half hinge, an antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
enzyme requires 12 or more appropriate amino acids between the Fab and Fc region to maintain a minimum critical distance between the scissile bond and the start of the Fc
-
-
?
additional information
?
-
-
no substrate: IgA2-IgA1 half hinge, an antibody with half of the IgA1 hinge region incorporated into the equivalent site in enzyme-resistant IgA2
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human immunoglobulin A1 + H2O
?
-
specific cleavage in the hinge region
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fc + immunoglobulin Fab
-
cleavage of the hinge region
-
-
?
immunoglobulin A1 + H2O
immunoglobulin A1 Fabalpha fragments + immunglobulin A1 Fcalpha
-
-
-
-
?
immunoglobulin IgA1 + H2O
effector domain of IgA1 + Fab determinants of IgA1
-
-
specific cleavage of hinge region. IgA1 bound to bacterial porin A is masked by the serogroup B polysaccharide capsule and less accessible to degradation. De novo synthesis of enzyme is required for degradation of porin-A-bound IgA1
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
-
-
-
-
?
LAMP1 + H2O
?
-
i.e. lysosome-associated membrane protein 1. The enzyme cleaves LAMP1 thereby accelerating its degradation rate in infected A431 human epidermoid carcinoma cells and resulting in the alteration of lysosomes. Infection of T84 monolayers also results in IgA1 protease-mediated reduction of LAMP1
-
?
LAMP1 + H2O
?
-
LAMP1 is a major integral membrane glycoprotein of lysosomes and significantly reduces its steady-state levels in an infected cell. Pilus-induced Ca2+ flux triggers lysosome exocytosis and increases the amount of LAMP1 accessible to IgA1 protease
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 protease is an important factor of meningitis
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
retained antigen-binding activity of Fabalpha fragments of human monoclonal immunoglobulin A1 cleaved by IgA 1 protease opens the possibility that IgA1 protease-producing bacteria growing in the presence of IgA1 antibodies are coated with Fabalpha fragments. Such fragments may conceivably protect the microorganism from the immune system by blocking access of intact antibody molecules of the same or other isotypes and of immunocompetent cells
-
-
?
additional information
?
-
-
IgA1 protease of the Brazilian purpuric fever clone may contribute to the pathogenic potential of the virulent phenotype in Brazil
-
-
?
additional information
?
-
-
the enzyme cleaves myeloma IgA1 and secretory IgA but not myeloma IgA2, IgM, or IgG
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
the cleavage of IgA1 by gonococcal IgA1 protease within the lumen of the female lower genital tract is unlikely to be a significant factor in the pathogenesis of infections by Neisseria gonorrhoeae
-
-
?
additional information
?
-
-
IgA1 protease is an important factor of meningitis
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
Streptococcus mitior
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
potential impotance of IgA proteases as an ecological determinant in the oral cavity and their role as a determinant of pathogenesis of pathogenic bacteria whose portal of entry is the mucosal surface
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
IgA1 protease is an important factor of meningitis
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
the enzyme cleaves myeloma IgA1 and secretory IgA but not myeloma IgA2, IgM, or IgG
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
IgA1 proteases are the principal etiologic agents of bacterial meningitis, gonorrhoea and periodontal disease
-
-
?
additional information
?
-
-
streptococcal immunglobulin A1 protease does not cleave porcine IgA
-
-
?
additional information
?
-
-
the enzyme could play a role in the selective host specificity of mucosal pathogens
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
Zn2+
additional information
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(tert-butylamino)-3-[[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]propan-2-ol
-
-
1-[2-(3-bromophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
-
-
1-[2-(3-chloro-4-methoxyphenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
-
-
1-[2-(3-chlorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
-
-
1-[2-(3-fluorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
-
-
3-hydroxy-1-[2-(3-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
-
-
3-hydroxy-1-[2-(4-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
-
-
3-hydroxy-2-methyl-1-[2-(3-methylphenyl)ethyl]pyridine-4(1H)-thione
-
-
4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl morpholine-4-carboxylate
-
-
4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl piperidine-1-carboxylate
-
-
4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl pyrrolidine-1-carboxylate
-
-
4-(piperidin-1-yl)-1,2,5-thiadiazol-3-yl morpholine-4-carboxylate
-
-
4-methyl-N'-[(morpholin-4-ylcarbonyl)oxy]benzenecarboximidamide
-
-
6-deoxy-6-demethyl-4-dimethylaminotetracycline
-
i.e. CMT-3, 50% inhibition at 0.01 to 0.05 mM. Presence of 1.5 mM CaCl2 enhances inhibition
methyl 3-[([[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]acetyl)amino]benzoate
-
-
N-(1,3-benzodioxol-5-yl)-2-[[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]acetamide
-
-
N-cyclopentyl-2-[[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]acetamide
-
-
Human serum
-
all or nearly all of the sera of 34 periodontally diseased and healthy individuals inhibit
-
Human serum
-
a minor portion of the sera of 34 periodontally diseased and healthy individuals inhibit
-
Human serum
-
a minor portion of the sera of 34 periodontally diseased and healthy individuals inhibit
-
Human serum
-
all or nearly all of the sera of 34 periodontally diseased and healthy individuals inhibit
-
Human serum
-
a minor portion of the sera of 34 periodontally diseased and healthy individuals inhibit
-
Human serum
-
all or nearly all of the sera of 34 periodontally diseased and healthy individuals inhibit
-
peptide boronic acids
-
inhibition of the type 1 and the type 2 protease
-
peptide boronic acids
-
inhibition of the type 1 and the type 2 protease
-
phenylmethylsulfonyl fluoride
-
inhibition of the type 1 protease, no inhibition of the type 2 protease
additional information
-
inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions
-
additional information
-
detection of small molecule, nonpeptidic inhibitors of Haemophilus influenzae IgA1 proteases, inhibitor screening and structure-activity relationship analysis. Improved inhibition and selectivity for IgA protease over other serine proteases
-
additional information
-
inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions
-
additional information
-
inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions
-
additional information
-
inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Persistent Infection
Changes in IgA Protease Expression Are Conferred by Changes in Genomes during Persistent Infection by Nontypeable Haemophilus influenzae in Chronic Obstructive Pulmonary Disease.
Pulmonary Disease, Chronic Obstructive
Changes in IgA Protease Expression Are Conferred by Changes in Genomes during Persistent Infection by Nontypeable Haemophilus influenzae in Chronic Obstructive Pulmonary Disease.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.962
1,2-diethyl-3-hydroxypyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.887
1-ethyl-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00614
1-[2-(3-bromophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00498
1-[2-(3-chloro-4-methoxyphenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.0043
1-[2-(3-chlorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00774
1-[2-(3-fluorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
1.3
3-hydroxy-1,2-dimethylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00664
3-hydroxy-1-[2-(3-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.007
3-hydroxy-1-[2-(4-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.0127
3-hydroxy-2-methyl-1-(2-phenylethyl)pyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00914
3-hydroxy-2-methyl-1-[2-(3-methylphenyl)ethyl]pyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a rapid method for the detection and quantitation of the igA protease activity
additional information
-
IgA1 protease activity assays on 20 clinical isolates indicates that the igaB gene is associated with increased levels of IgA1 protease activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the brain of a diseased piglet collected during the 2005 Sichuan outbreak in China that expressed MRP, EF, and SLY
UniProt
brenda
Streptococcus suis DAT1 SC-19
isolated from the brain of a diseased piglet collected during the 2005 Sichuan outbreak in China that expressed MRP, EF, and SLY
UniProt
brenda
Streptococcus suis DAT1 ZYS
isolated from the brain of a diseased piglet collected during the 2005 Sichuan outbreak in China that expressed MRP, EF, and SLY
UniProt
brenda
-
29648, 29649, 29651, 37001, 37008, 37009, 37012, 37013, 37015, 37016, 37017, 37018, 37022, 37030, 669721, 680133, 680136, 695450, 732284
-
-
brenda
antigenic heterogeneity of immunoglobulin A1 proteases from encapsulated and non-encapsulated Haemophilus influenzae
-
-
brenda
biogroup aegypticus isolates of the clone associated with Brazilian purpuric fever
-
-
brenda
Brazilian purpuric fever strain F3031, type 2 enzyme, expression of enzyme is not regulated by iron or hemin
-
-
brenda
Nontypeable Haemophilus influenzae, four IgA1 protease forms: A1, A2, B1, and B2
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
ureaplasmas isolated from nonhuman hosts, feline, canine, avian or bovine do not cleave human IgA1
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
reverse transcriptase PCR shows that igB is transcribed in Haemophilus influenza
brenda
-
the enzyme is secreted into the culture medium throughout the exponential growth
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to external side of bacterial membrane. Localization requires the LPNTG sorting motif near the amino terminus of protein
brenda
-
recombinant enzyme produced in Escherichia coli is localized in the periplasmic space, a sequence linked to the carboxyl terminus of the iga gene but not present in the original clone is shown to be necessary to achieve normal secretion
brenda
additional information
-
the mature Streptococcus pneumoniae IgA1P form is both attached to the bacterial cell surface and released in its full form
-
brenda
associated via an N-terminal membrane anchor, release upon proteolytic cleavage
brenda
surface distribution of IgA1 protease on SS2 strain ZYS, overview
brenda
Streptococcus suis DAT1 SC-19
-
surface distribution of IgA1 protease on SS2 strain ZYS, overview
-
brenda
Streptococcus suis DAT1 ZYS
-
surface distribution of IgA1 protease on SS2 strain ZYS, overview
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
expression of IgA proteases is variable from strain to strain among NTHi. Analysis of IgA protease expression by 101 persistent strains (median duration of persistence) collected longitudinally from patients enrolled in a 20-year study of COPD upon initial acquisition and immediately before clearance from the host. Upon acquisition, 89 (88%) express IgA protease. A total of 16 of 101 (16%) strains of NTHi alter expression of IgA protease during persistence. Indels and slipped-strand mispairing of mononucleotide repeats confer changes in expression of igaA2. Mechanism of changes in expression, overview
physiological function
additional information
physiological function
-
IgA1 protease may play an important role in the pathogenesis of Streptococcus suis
physiological function
-
the enzyme catalyzes the proteolysis of human IgA1 at its hinge region to leave the bacterial cell surface masked by IgA1 Fab, enabling the bacteria to evade the host's immune system and adhere to host epithelial cells to promote colonization
physiological function
-
enzyme IgA1P cleaves human immunoglobulin A1 (IgA1), the predominant antibody on human mucosal surfaces. The actions of IgA1Ps impede IgA1 from neutralizing the bacteria. Specifically, IgA1P cleaves IgA1 at a unique hinge region, separating the Fc and Fab fragments of the immunoglobulin. This impairs its Fc-mediated effector response and can even allow bacteria to retain the Fab fragment on their surface in order to mask their polysaccharide capsule and other surface antigens
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
physiological function
-
nontypeable Haemophilus influenzae (NTHi) expresses four IgA protease variants (A1, A2, B1, and B2) that play different roles in virulence
physiological function
the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2
physiological function
Streptococcus suis DAT1 SC-19
-
the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2
-
physiological function
Streptococcus suis DAT1 ZYS
-
the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2
-
physiological function
-
IgA1 protease may play an important role in the pathogenesis of Streptococcus suis
-
additional information
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a BALB/c mouse model
additional information
-
immunization of mice with recombinant IgA1 protease of Neisseria meningitidis or several structural derivatives thereof protects the animals infected with a variety of deadly pathogens, including Neissseria meningitidis serogroups A, B, and C and 3 serotypes of Streptococcus pneumonia. In sera of rabbits immunized with inactivated pneumococcal cultures, antibodies binding IgA1-protease from Neisseria meningitidis serogroup B are detected. Cross-reactive protection against meningococcal and pneumococcal infections in vivo
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
additional information
Streptococcus suis DAT1 SC-19
-
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a BALB/c mouse model
-
additional information
Streptococcus suis DAT1 ZYS
-
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a BALB/c mouse model
-
additional information
Neisseria meningitidis serogroup B B44/76
-
immunization of mice with recombinant IgA1 protease of Neisseria meningitidis or several structural derivatives thereof protects the animals infected with a variety of deadly pathogens, including Neissseria meningitidis serogroups A, B, and C and 3 serotypes of Streptococcus pneumonia. In sera of rabbits immunized with inactivated pneumococcal cultures, antibodies binding IgA1-protease from Neisseria meningitidis serogroup B are detected. Cross-reactive protection against meningococcal and pneumococcal infections in vivo
-
Show AA Sequence and Transmembrane Helices (742 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
108000
-
x * 108000, product of gene fragment missing about 1300 bp in the 3 region, SDS-PAGE
114000
-
x * 114000, the 114000 Da peptide is converted to a still active 109000 Da peptide during isolation, type 2 protease, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 108000, product of gene fragment missing about 1300 bp in the 3 region, SDS-PAGE
?
-
x * 114000, the 114000 Da peptide is converted to a still active 109000 Da peptide during isolation, type 2 protease, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
the unexpected self-cleavage and subsequent extracellular release of mature IgA1 protease from mutants lacking the previously defined consensus cleavage site (P-P-S-P, residues 1003-1006) and/or the putative (P-V-P-S-P, residues 1003-1006) self-cleavage site is shown
proteolytic modification
-
the unexpected self-cleavage and subsequent extracellular release of mature IgA1 protease from mutants lacking the previously defined consensus cleavage site (P-P-S-P, residues 1003-1006) and/or the putative (P-V-P-S-P, residues 1003-1006) self-cleavage site is shown
-
proteolytic modification
-
posttranslational processing possibly as a result of autoproteolysis at post-proline peptide bonds in the N-terminal parts of the molecule
proteolytic modification
-
posttranslational processing possibly as a result of autoproteolysis at post-proline peptide bonds in the N-terminal parts of the molecule
proteolytic modification
-
correct localization requires the LPNTG sorting motif near the amino terminus of protein. Processing takes place at a site downstream of the sorting signal. Non-covalent re-association between the carboxyterminal enzymatic domain and the cleaved, sorted aminoterminal domain
proteolytic modification
-
the fully mature form of Streptococcus pneumoniae IgA1P comprises residues 154-1963
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1003-1006
-
mutant lacking the confirmed self-cleavage recognition site shows only little reduction in secreted protease
DELTA1005-1006
-
mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
DELTA974-1002
-
mutant lacking the putative self-cleavage recognition site and the intervening residues shows only little reduction in secreted protease
DELTA974-978
-
mutant lacking the putative self-cleavage recognition site shows only little reduction in secreted protease
DELTA974-978/DELTA1003-1007
-
double deletion mutant lacking both self-cleavage recognition sites shows only a 40% reduced secretion
P1004T/S1005E/S1006A
-
mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
P975E/P1004E
-
mutant containing modified consensus recognition sites shows 30% lower secreted protease levels than wild-type
S1005E
-
mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
S267V
-
this mutant fails to undergo self-cleavage and shows no enzymatic activity
DELTA1005-1006
-
mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
-
P1004T/S1005E/S1006A
-
mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
-
S1005E
-
mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
-
S267V
-
this mutant fails to undergo self-cleavage and shows no enzymatic activity
-
E1605A
E1628A
-
site-directed mutagenesis, the IgA1P mutation reduces the proteolytic activity of the enzyme
E1661A
-
site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type
E1695A
-
site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type
E1698A
-
site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type
additional information
E1605A
-
site-directed mutagenesis, the IgA1P mutation completely abrogates the proteolytic activity
additional information
-
Blastx analysis shows that the igaB gene is homologous to the IgA1 protease genes of Neisseria gonorrhoeae and Neisseria meningitidis. The degree of homology of igaB to neisserial iga genes is greater than the homology of igaB to Haemophilus iga genes
additional information
-
mutants that are deficient in iga, igaB, and both genes are constructed in Haemophilus influenzae strain 11P6H. Analysis of these mutants indicates that igaB is the primary mediator of IgA1 protease activity in this strain
additional information
-
a mutant in which the entire region spanning the putative (residues 974-978) and the confirmed self-cleavage site (residues 1003-1006) is replaced by a hexahistidine linker fails to produce any detectable secreted protease
additional information
-
a mutant in which the entire region spanning the putative (residues 974-978) and the confirmed self-cleavage site (residues 1003-1006) is replaced by a hexahistidine linker fails to produce any detectable secreted protease
-
additional information
-
disruption of the region between the signal peptidase cleavage site and the LPNTG sorting motif results in a localization defect, premature degradation, and an alteration of the ability of the enzyme to act on a monoclonal human IgA1 substrate
additional information
-
an antigenic sequence corresponding to amino acids 420-457 (epiA) of the iga gene product is identified by screening a pneumococcal phage display library with patient's sera. The epiA peptide is conserved in all pneumococci and in two out of three Sreptococcus mitis strains. This epitope is specifically recognized by antibodies present in sera from 90% of healthy adults, thus representing an important target of the humoral response to Streptococcus pneumoniae and Streptococcus mitis infection
additional information
-
polymeric IgA and secretory IgA are tested for killing of an IgA1 protease producing strain and a congenic IgA1 protease-negative strain of Streptococcus pneumoniae after a 2 h bacterium-antibody exposure time. Exposure of polymeric IgA and secretory IgA to the protease-producing strain inhibits IgA-mediated killing compared with the results seen with polymeric IgA and secretory IgA exposed to a protease-negative mutant. No difference in killing is observed between the two bacterial strains when polymeric IgA and secretory IgA of subclass IgA2 are used
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
about 30% loss of activity after 2 h, about 50% loss of activity after 3 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-acetate, pH 7.5, 20% glycerol, 0.1 mM dithiothreitol, 5 mM EDTA, type 1 protease, less than 10% loss of activity after 2 weeks
-
4°C, long term storage of the 109000 Da type 2 protease, breakdown yields fragments of 95000 and 15000 Da and loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
recombinant glutathione S-transferase fusion proteins of three segments of enzyme, comprising amino acids 1032-1964, 708-1964, and 104-1964. Segment 1032-1964 is catalytically inactive. Recombinant proteins are highly instable.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged Haemophilus influenzae type 1 IgA1 protease
-
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
expression in Escherichia coli, construction of mutants of Neisseria gonorrhoeae that fail to produce the activity
-
expression in Haemophilis influenzae with His-tag. Protein is autoprocessed and secreted
-
fragment missing about 1300 bp in the 3 region, purified protein fragment is active
-
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
-
recombinant expression of tagged IgA1 protease of Neisseria meningitidis or several structural derivatives thereof, recombinant IgA1pr from Neisseria meningitidis serogroup B strain B44/76 with the primary structure MA28-P1004LEH6 and its N-terminal fragment (protein I, ME135-H328LEH6), proteins II and III are fusion recombinant proteins containing three or two fragments from different regions of base molecule IgA1pr MA28-P1004LEH6. Protein II contains fragments from the N-terminal, central, and C-terminal regions of the base molecule MA28-P1004LEH6, protein III contains fragments from the N-terminal and C-terminal regions of the base molecule
-
the Streptococcus pneumoniae gene is 64% identical and 76% similar to that of Streptococcus sanguis. The zinc-binding sequence is conserved in the two proteins
three segments of enzyme, comprising amino acids 1032-1964, 708-1964, and 104-1964
expressed in Escherichia coli as a His-tagged fusion protein
the Streptococcus pneumoniae gene is 64% identical and 76% similar to that of Streptococcus sanguis. The zinc-binding sequence is conserved in the two proteins
-
the Streptococcus pneumoniae gene is 64% identical and 76% similar to that of Streptococcus sanguis. The zinc-binding sequence is conserved in the two proteins
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
three of the igA gene restriction types, which appear to represent 98% of the Haemophilus influenzae serotype b population, encode IgA1 proteases that are inhibited by antisera to any one of theses types and therefore could form the basis for the development of a vaccine against Haemophilus influenzae meningitis
medicine
enzyme is a major Streptococcus pneumoniae antigen in humans
medicine
-
enzyme, as well as pneumococcal proteins alpha-enolase, immunoglobulin streptococcal lipoprotein rotamase A, and putative proteinase maturation protein A are immunogenic proteins that elicit antibody response early in life. No significant correlation between antibody titers to these proteins and pneumococcal carriage or infection
medicine
-
the broad and specific recognition of the epiA polypeptide by human sera demonstrate that the pneumococcal IgA1 protease contains an immunodominant B-cell epitope
medicine
-
systemically administered IgA protease is able to remove glomerular IgA immune complexes, both the antigen and antibody components, in a passive mouse model of IgA nephropathy. IgA protease decreases the amount of injected human IgA immune complexes deposited in the kidneys in vivo. The quantity of deposited complexes is reduced by digestion of IgA1 at a single site, the peptide bond between amino acid residues 231-232 in each alpha chain
medicine
-
IgA1 protease may be an effective therapeutic candidate for IgAN by removing the mesangial deposited IgA1 in glomerular mesangium leading to immunoglobulin A nephropathy. The removal of IgA1 by IgA1 protease may separate the IgA1-containing immune complexes thereby eliminating its other components at the same time
medicine
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a mouse model. rIgAP emulsified with a Marcol 52-based adjuvant can induce high titers of specific IgG antibodies, including high levels of antibodies with bactericidal activity in the presence of phagocytes, as well as confer good protection against SS2 infection. The virulence-associated protein IgA1 protease is a protective antigen and one of promising and effective vaccine candidates against SS2
medicine
-
immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines
medicine
Streptococcus suis DAT1 SC-19
-
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a mouse model. rIgAP emulsified with a Marcol 52-based adjuvant can induce high titers of specific IgG antibodies, including high levels of antibodies with bactericidal activity in the presence of phagocytes, as well as confer good protection against SS2 infection. The virulence-associated protein IgA1 protease is a protective antigen and one of promising and effective vaccine candidates against SS2
-
medicine
Streptococcus suis DAT1 ZYS
-
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a mouse model. rIgAP emulsified with a Marcol 52-based adjuvant can induce high titers of specific IgG antibodies, including high levels of antibodies with bactericidal activity in the presence of phagocytes, as well as confer good protection against SS2 infection. The virulence-associated protein IgA1 protease is a protective antigen and one of promising and effective vaccine candidates against SS2
-
medicine
Neisseria meningitidis serogroup B B44/76
-
immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bachovchin, W.W.; Plaut, A.G.; Flentke, G.R.; Lynch, M.; Kettner, C.A.
Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids
J. Biol. Chem.
265
3738-3743
1990
Haemophilus influenzae, Neisseria gonorrhoeae, Streptococcus sanguinis
brenda
Plaut, A.G.
The IgA1 proteases of pathogenic bacteria
Annu. Rev. Microbiol.
37
603-622
1983
Prevotella melaninogenica, Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Streptococcus mitior, Streptococcus sanguinis
brenda
Grundy, F.J.; Plaut, A.; Wright, A.
Haemophilus influenzae immunoglobulin A1 protease genes: cloning by plasmid integration-excision, comparative analyses, and localization of secretion determinants
J. Bacteriol.
169
4442-4450
1987
Haemophilus influenzae
brenda
Grundy, F.J.; Plaut, A.; Wright, A.
Localization of the cleavage site specificity determinant of Haemophilus influenzae immunoglobulin A1 protease genes
Infect. Immun.
58
320-331
1990
Haemophilus influenzae
brenda
Plaut, A.G.
Production and isolation of neissereal IgA proteases
Methods Enzymol.
165
117-120
1988
Neisseria gonorrhoeae
brenda
Simpson, D.A.; Hausinger, R.P.; Mulks, M.H.
Purification, characterization, and comparison of the immunoglobulin A1 proteases of Neisseria gonorrhoeae
J. Bacteriol.
170
1866-1873
1988
Neisseria gonorrhoeae
brenda
Frandsen, E.V.G.; Reinholdt, J.; Kilian, M.
Enzymatic and antigenic characterization of immunoglobulin A1 proteases from Bacteroides and Capnocytophaga spp.
Infect. Immun.
55
631-638
1987
Prevotella buccae, Prevotella buccalis, Prevotella oralis, Prevotella veroralis, Capnocytophaga gingivalis, Capnocytophaga ochracea, Capnocytophaga sputigena
brenda
Kapatais-Zoumbos, K.; Chandler, D.K.F.; Barile, M.F.
Survey of immunoglobulin A protease activity among selected species of Ureaplasma and Mycoplasma: specificity for host immunoglobulin A
Infect. Immun.
47
704-709
1985
Mycoplasma genitalium, Mycoplasma hominis, Mycoplasma pneumoniae, Ureaplasma urealyticum
brenda
Mortensen, S.B.; Kilian, M.
Purification and characterization of an immunoglobulin A1 protease from Bacteroides melaninogenicus
Infect. Immun.
45
550-557
1984
Prevotella melaninogenica
brenda
Mortensen, S.B.; Kilian, M.
A rapid method for the detection and quantitation of IgA protease activity by macrobore gel-permeation chromatography
J. Chromatogr.
296
257-262
1984
Haemophilus influenzae
brenda
Koomey, J.M.; Falkow, S.
Nucleotide sequence homology between the immunoglobulin A1 protease genes of Neisseria gonorrhoeae, Neisseria meningitidis, and Haemophilus influenzae
Infect. Immun.
43
101-107
1984
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
brenda
Kilian, M.; Thomsen, B.
Antigenic heterogeneity of immunoglobulin A1 proteases from encapsulated and non-encapsulated Haemophilus influenzae
Infect. Immun.
42
126-132
1983
Haemophilus aegyptius, Haemophilus influenzae
brenda
Kilian, M.; Thomsen, B.; Petersen, T.E.; Bleeg, H.S.
Occurrence and nature of bacterial IgA proteases
Ann. N. Y. Acad. Sci.
409
612-624
1983
Porphyromonas asaccharolytica, Prevotella buccae, Porphyromonas gingivalis, Prevotella intermedia, Prevotella loescheii, Prevotella melaninogenica, Prevotella oris, Capnocytophaga gingivalis, Capnocytophaga ochracea, Capnocytophaga sputigena, Streptococcus pneumoniae, Gemella haemolysans, Haemophilus aegyptius, Haemophilus influenzae, Haemophilus parahaemolyticus, Neisseria gonorrhoeae, Neisseria meningitidis, Pseudomonas aeruginosa, Streptococcus mitior, Streptococcus sanguinis
brenda
Bricker, J.; Mulks, M.H.; Plaut, A.G.; Moxon, E.R.; Wright, A.
IgA1 proteases of Haemophilus influenzae: cloning and characterization in Escherichia coli K-12
Proc. Natl. Acad. Sci. USA
80
2681-2685
1983
Haemophilus influenzae
brenda
Koomey, J.M.; Gill, R.E.; Falkow, S.
Genetic and biochemical analysis of gonococcal IgA1 protease: cloning in Escherichia coli and construction of mutants of gonococci that fail to produce the activity
Proc. Natl. Acad. Sci. USA
79
7881-7885
1982
Neisseria gonorrhoeae
brenda
Kornfeld, S.J.; Plaut, A.G.
Secretory immunity and the bacterial IgA proteases
Rev. Infect. Dis.
3
521-534
1981
Streptococcus pneumoniae, Haemophilus influenzae, Haemophilus parahaemolyticus, Neisseria gonorrhoeae, Neisseria meningitidis, Streptococcus sanguinis
brenda
Kilian, M.; Mestecky, J.; Kulhavy, R.; Tomana, M.; Butler, W.T.
IgA1 proteases from Haemophilus influenzae, Streptococcus pneumoniae, Neisseria meningitidis, and Streptococcus sanguis: comparative immunochemical studies
J. Immunol.
124
2596-2600
1980
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria meningitidis, Streptococcus sanguinis
brenda
Kilian, M.; Mestecky, J.; Schrohenloher, R.E.
Pathogenic species of the genus Haemophilus and Streptococcus pneumoniae produce immunoglobulin A1 protease
Infect. Immun.
26
143-149
1979
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria meningitidis
brenda
Male, C.J.
Immunoglobulin A1 protease production by Haemophilus influenzae and Streptococcus pneumoniae
Infect. Immun.
26
254-261
1979
Streptococcus pneumoniae, Haemophilus influenzae
brenda
Blake, M.S.; Swanson, J.
Studies on gonococcus infection. XVI. Purification of Neisseria gonorrhoeae immunoglobulin A1 protease
Infect. Immun.
22
350-358
1978
Neisseria gonorrhoeae
brenda
Gilbert, J.V.; Plaut, A.G.; Fishman, Y.; Wright, A.
Cloning of the gene encoding streptococcal immunoglobulin A protease and its expression in Escherichia coli
Infect. Immun.
56
1961-1966
1988
Streptococcus sanguinis
brenda
Reinholt, J.
A method for titration of inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions
J. Immunol. Methods
191
39-48
1996
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria meningitidis, Streptococcus sanguinis
brenda
Hedges, S.R.; Mayo, M.S.; Kallman, L.; Mestecky, J.; Hook III, E.W.; Russell, M.W.
Evaluation of immunoglobulin A1 (IgA1) protease and IgA1 protease-inhibitory activity in human female genital infection with Neisseria gonorrhoeae
Infect. Immun.
66
5826-5832
1998
Neisseria gonorrhoeae
brenda
Lomholt, H.; Kilian, M.
Distinct antigenic and genetic properties of the immunoglobulin A1 protease produced by Haemophilus influenzae biogroup aegyptius associated with Brazilian purpuric fever in Brazil
Infect. Immun.
63
4389-4394
1995
Haemophilus influenzae
brenda
Frandsen, E.V.G.; Kjeldsen, M.; Kilian, M.
Inhibition of Prevotella and Capnocytophaga immunoglobulin A1 proteases by human serum
Clin. Diagn. Lab. Immunol.
4
458-464
1997
Prevotella buccae, Prevotella buccalis, Prevotella loescheii, Prevotella melaninogenica, Prevotella oris, Capnocytophaga ochracea, Prevotella denticola
brenda
Spooner, R.K.; Russell, W.C.; Thirkell, D.
Characterization of the immunoglobulin A protease of Ureaplasma urealyticum
Infect. Immun.
60
2544-2546
1992
Ureaplasma urealyticum
brenda
Poulsen, K.; Reinholdt, J.; Kilian, M.
Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product
Infect. Immun.
64
3957-3966
1996
Streptococcus pneumoniae, Streptococcus sanguinis
brenda
Poulsen, K.; Reinholdt, J.; Jespergaard, C.; Boye, K.; Brown, T.A.; Hauge, M.; Kilian, M.
A comprehensive genetic study of streptococcal immunoglobulin A1 proteases: evidence for recombination within and between species
Infect. Immun.
66
181-190
1998
Streptococcus mitis, Streptococcus oralis
brenda
Blake, M.S.; Eastby, C.
Studies on the gonococcal IgA1 protease II. Improved methods of enzyme purification and production of monoclonal antibodies to the enzyme
J. Immunol. Methods
144
215-221
1991
Neisseria gonorrhoeae, Neisseria meningitidis
brenda
Mansa, B.; Kilian, M.
Retained antigen-binding activity of Fab alpha fragments of human monoclonal immunoglobulin A1 (IgA1) cleaved by IgA1 protease
Infect. Immun.
52
171-174
1986
Haemophilus influenzae
brenda
Poulsen, K.; Hjorth, J.P.; Kilian, M.
Limited diversity of the immunoglobulin A1 protease gene (iga) among Haemophilus influenzae serotype b strains
Infect. Immun.
56
987-992
1988
Haemophilus influenzae
brenda
Tyler, B.M.; Cole, M.F.
Effect of IgA1 protease on the ability of secretory IgA1 antibodies to inhibit the adherence of Streptococcus mutans
Microbiol. Immunol.
42
503-508
1998
Streptococcus mutans
brenda
McLeod, D.T.; Croughan, M.J.; Brettle, R.P.; Calder, M.A.
Lack of immunoglobulin A1 protease production by Branhamella catarrhalis
Infect. Immun.
52
631-632
1986
no activity in Moraxella catarrhalis
brenda
Ayala, B.P.; Vasquez, B.; Clary, S.; Tainer, J.A.; Rodland, K.; So, M.
The pilus-induced Ca2+ flux triggers lysosome exocytosis and increases the amount of Lamp1 accessible to Neisseria IgA1 protease
Cell. Microbiol.
3
265-275
2001
Neisseria gonorrhoeae
brenda
Hopper, S.; Vasquez, B.; Merz, A.; Clary, S.; Wilbur, J.S.; So, M.
Effects of the immunoglobulin A1 protease on Neisseria gonorrhoeae trafficking across polarized T84 epithelial monolayers
Infect. Immun.
68
906-911
2000
Neisseria gonorrhoeae
brenda
Batten, M.R.; Senior, B.W.; Kilian, M.; Woof, J.M.
Amino acid sequence requirements in the hinge of human immunoglobulin A1 (IgA1) for cleavage by streptococcal IgA1 proteases
Infect. Immun.
71
1462-1469
2003
Streptococcus pneumoniae, Streptococcus mitis, Streptococcus oralis, Streptococcus sanguinis
brenda
McGillivary, G.; Smoot, L.M.; Actis, L.A.
Characterization of the IgA1 protease from the Brazilian purpuric fever strain F3031 of Haemophilus influenzae biogroup aegyptius
FEMS Microbiol. Lett.
250
229-236
2005
Haemophilus influenzae
brenda
Vidarsson, G.; Overbeeke, N.; Stemerding, A.M.; van den Dobbelsteen, G.; van Ulsen, P.; van der Ley, P.; Kilian, M.; van de Winkel, J.G.
Working mechanism of immunoglobulin A1 (IgA1) protease: cleavage of IgA1 antibody to Neisseria meningitidis PorA requires de novo synthesis of IgA1 Protease
Infect. Immun.
73
6721-6726
2005
Neisseria meningitidis
brenda
Bender, M.H.; Weiser, J.N.
The atypical amino-terminal LPNTG-containing domain of the pneumococcal human IgA1-specific protease is required for proper enzyme localization and function
Mol. Microbiol.
61
526-543
2006
Streptococcus pneumoniae
brenda
Romanello, V.; Marcacci, M.; Dal Molin, F.; Moschioni, M.; Censini, S.; Covacci, A.; Baritussio, A.G.; Montecucco, C.; Tonello, F.
Cloning, expression, purification, and characterization of Streptococcus pneumoniae IgA1 protease
Protein Expr. Purif.
45
142-149
2006
Streptococcus pneumoniae (Q59947), Streptococcus pneumoniae
brenda
Walker, S.G.; Carnu, O.I.; Tueter, G.; Ryan, M.E.
The immunoglobulin A1 proteinase from Streptococcus pneumoniae is inhibited by tetracycline compounds
FEMS Immunol. Med. Microbiol.
48
218-222
2006
Streptococcus pneumoniae
brenda
Senior, B.W.; Woof, J.M.
The influences of hinge length and composition on the susceptibility of human IgA to cleavage by diverse bacterial IgA1 proteases
J. Immunol.
174
7792-7799
2005
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Streptococcus mitis, Streptococcus oralis, Streptococcus sanguinis, Streptococcus sanguinis SK1
brenda
Senior, B.W.; Woof, J.M.
Sites in the CH3 domain of human IgA1 that influence sensitivity to bacterial IgA1 proteases
J. Immunol.
177
3913-3919
2006
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Streptococcus mitis, Streptococcus oralis, Streptococcus sanguinis
brenda
Adrian, P.V.; Bogaert, D.; Oprins, M.; Rapola, S.; Lahdenkari, M.; Kilpi, T.; de Groot, R.; Kaeyhty, H.; Hermans, P.W.
Development of antibodies against pneumococcal proteins alpha-enolase, immunoglobulin A1 protease, streptococcal lipoprotein rotamase A, and putative proteinase maturation protein A in relation to pneumococcal carriage and Otitis Media
Vaccine
22
2737-2742
2004
Streptococcus pneumoniae
brenda
de Paolis, F.; Beghetto, E.; Spadoni, A.; Montagnani, F.; Felici, F.; Oggioni, M.R.; Gargano, N.
Identification of a human immunodominant B-cell epitope within the immunoglobulin A1 protease of Streptococcus pneumoniae
BMC Microbiol.
7
113
2007
Streptococcus pneumoniae
brenda
Fernaays, M.M.; Lesse, A.J.; Cai, X.; Murphy, T.F.
Characterization of igaB, a second immunoglobulin A1 protease gene in nontypeable Haemophilus influenzae
Infect. Immun.
74
5860-5870
2006
Haemophilus influenzae
brenda
Fasching, C.E.; Grossman, T.; Corthesy, B.; Plaut, A.G.; Weiser, J.N.; Janoff, E.N.
Impact of the molecular form of immunoglobulin A on functional activity in defense against Streptococcus pneumoniae
Infect. Immun.
75
1801-1810
2007
Streptococcus pneumoniae, Haemophilus influenzae
brenda
Vitovski, S.; Sayers, J.R.
Relaxed cleavage specificity of an immunoglobulin A1 protease from Neisseria meningitidis
Infect. Immun.
75
2875-2885
2007
Neisseria meningitidis, Neisseria meningitidis NMB
brenda
Takenouchi-Ohkubo, N.; Mortensen, L.M.; Drasbek, K.R.; Kilian, M.; Poulsen, K.
Horizontal transfer of the immunoglobulin A1 protease gene (iga) from Streptococcus to Gemella haemolysans
Microbiology
152
2171-2180
2006
Streptococcus mitis (Q4U6L1), Streptococcus mitis (Q4U6L2), Gemella haemolysans (Q6TL30), Gemella haemolysans CCUG4815 (Q6TL30), Streptococcus mitis SK609 (Q4U6L2), Streptococcus mitis SK564 (Q4U6L1)
brenda
Lamm, M.E.; Emancipator, S.N.; Robinson, J.K.; Yamashita, M.; Fujioka, H.; Qiu, J.; Plaut, A.G.
Microbial IgA protease removes IgA immune complexes from mouse glomeruli in vivo: potential therapy for IgA nephropathy
Am. J. Pathol.
172
31-36
2008
Haemophilus influenzae
brenda
Zhang, A.; Mu, X.; Chen, B.; Liu, C.; Han, L.; Chen, H.; Jin, M.
Identification and characterization of IgA1 protease from Streptococcus suis
Vet. Microbiol.
140
171-175
2010
Streptococcus suis, Streptococcus suis 05ZYS
brenda
Xie, L.S.; Huang, J.; Qin, W.; Fan, J.M.
Immunoglobulin A1 protease: a new therapeutic candidate for immunoglobulin A nephropathy
Nephrology
15
584-586
2010
Streptococcus pneumoniae
brenda
Choudary, S.K.; Qiu, J.; Plaut, A.G.; Kritzer, J.A.
Versatile substrates and probes for IgA1 protease activity
ChemBioChem
14
2007-2012
2013
Streptococcus sanguinis (Q59986), Streptococcus sanguinis ATCC 10556 (Q59986)
brenda
Garner, A.L.; Fullagar, J.L.; Day, J.A.; Cohen, S.M.; Janda, K.D.
Development of a high-throughput screen and its use in the discovery of Streptococcus pneumoniae immunoglobulin A1 protease inhibitors
J. Am. Chem. Soc.
135
10014-10017
2013
Streptococcus pneumoniae
brenda
Murphy, T.F.; Kirkham, C.; Jones, M.M.; Sethi, S.; Kong, Y.; Pettigrew, M.M.
Expression of IgA proteases by Haemophilus influenzae in the respiratory tract of adults with chronic obstructive pulmonary disease
J. Infect. Dis.
212
1798-1805
2015
Haemophilus influenzae, Haemophilus influenzae 2019
brenda
Bek-Thomsen, M.; Poulsen, K.; Kilian, M.
Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal species
mBio
3
e00303-12
2012
Streptococcus pneumoniae, Streptococcus oralis
brenda
Bek-Thomsen, M.; Poulsen, K.; Kilian, M.
Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal species
mBio
3
00303-00312
2012
Gemella haemolysans, Streptococcus sanguinis
brenda
Bek-Thomsen, M.; Poulsen, K.; Kilian, M.
Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal species
mBio
3
e00303
2012
Streptococcus mitis, Streptococcus mitis (A0A380KVU2), Streptococcus mitis (F9HE84), Streptococcus mitis (F9HP13), no activity in Streptococcus gordonii, Streptococcus infantis, Streptococcus infantis (E1M8Z5), Streptococcus infantis (F9PW76), no activity in Streptococcus parasanguinis, no activity in Streptococcus suis, no activity in Streptococcus cristatus, no activity in Streptococcus oligofermentans, no activity in Streptococcus australis, no activity in Streptococcus peroris, Streptococcus pseudopneumoniae, Streptococcus sanguinis (A0A2X3VMP4), Streptococcus sanguinis (A3CMW3), Streptococcus sanguinis (F0I116), Streptococcus sanguinis (F0I1W6), Streptococcus sanguinis (F0I7T0), Streptococcus sanguinis (F0IUS4), Streptococcus sanguinis (F2BS82), Streptococcus sanguinis (F2C6A9), Streptococcus sanguinis (F2CCY5), Streptococcus sanguinis (F3SHU7), Streptococcus sanguinis (F3US40), Streptococcus sanguinis (F3UXX0), Streptococcus oralis (P96466), Streptococcus pneumoniae (Q54875), Streptococcus pneumoniae (Q59947), Streptococcus pneumoniae (Q97QP7), Gemella haemolysans (Q6TL30), Streptococcus mitis SK1073 (F9HE84), Streptococcus pneumoniae PK81 (Q54875), Streptococcus sanguinis SK1087 (F3SHU7), Streptococcus sanguinis SK36 (A3CMW3), Streptococcus pseudopneumoniae IS7493, Streptococcus sanguinis SK330 (F2C6A9), Streptococcus mitis SK1080 (F9HP13), Streptococcus sanguinis SK355 (F3US40), Streptococcus sanguinis SK160 (F0IUS4), Streptococcus mitis NCTC 12261 (A0A380KVU2), Streptococcus oralis SK141 (P96466), Streptococcus sanguinis SK72 (F0I116), Streptococcus sanguinis SK72 (F0I1W6), Streptococcus infantis SK1302 (E1M8Z5), Streptococcus sanguinis SK49 (F3UXX0), Streptococcus infantis SK970 (F9PW76), Streptococcus sanguinis ATCC 29667 (A0A2X3VMP4), Streptococcus sanguinis SK408 (F2CCY5), Streptococcus sanguinis SK115 (F0I7T0), Streptococcus sanguinis SK1057 (F2BS82)
brenda
Shehaj, L.; Choudary, S.K.; Makwana, K.M.; Gallo, M.C.; Murphy, T.F.; Kritzer, J.A.
Small-molecule inhibitors of Haemophilus influenzae IgA1 protease
ACS Infect. Dis.
5
1129-1138
2019
Haemophilus influenzae NTHI
brenda
Gallo, M.C.; Kirkham, C.; Eng, S.; Bebawee, R.S.; Kong, Y.; Pettigrew, M.M.; Tettelin, H.; Murphy, T.F.
Changes in IgA protease expression are conferred by changes in genomes during persistent infection by nontypeable Haemophilus influenzae in chronic obstructive pulmonary disease
Infect. Immun.
86
e00313-18
2018
Haemophilus influenzae NTHI
brenda
Fu, L.; Zhao, J.; Lin, L.; Zhang, Q.; Xu, Z.; Han, L.; Xie, C.; Zhou, R.; Jin, M.; Zhang, A.
Characterization of IgA1 protease as a surface protective antigen of Streptococcus suis serotype 2
Microbes Infect.
18
285-289
2016
Streptococcus suis DAT1 (A0A0Z8E9X6), Streptococcus suis DAT1 SC-19 (A0A0Z8E9X6), Streptococcus suis DAT1 ZYS (A0A0Z8E9X6)
brenda
Kotelnikova, O.; Alliluev, A.; Zinchenko, A.; Zhigis, L.; Prokopenko, Y.; Nokel, E.; Razgulyaeva, O.; Zueva, V.; Tokarskaya, M.; Yastrebova, N.; Gordeeva, E.; Melikhova, T.; Kaliberda, E.; Rumsh, L.
Protective potency of recombinant meningococcal IgA1 protease and its structural derivatives upon animal invasion with meningococcal and pneumococcal infections
Microbes Infect.
21
336-340
2019
Neisseria meningitidis serogroup B, Neisseria meningitidis serogroup B B44/76
brenda
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
Protein Sci.
26
600-610
2017
Streptococcus pneumoniae
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.24.13)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
