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Sequence analysis of the wall‐associated protein precursor of Streptococcus mutans antigen A
Author(s) -
Ferretti J. J.,
Russell R. R. B.,
Dao M. L.
Publication year - 1989
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1989.tb00193.x
Subject(s) - biology , nucleic acid sequence , streptococcus mutans , peptide sequence , gene , cell wall , signal peptide , amino acid , strain (injury) , nucleotide , antigen , microbiology and biotechnology , biochemistry , genetics , bacteria , anatomy
Summary The nucleotide sequence has been determined for the Streptococcus mutans wall‐associated protein A ( wapA ) gene from serotype c strains Ingbritt and GS5. The nucleotide sequence for each wapA gene was virtually identical, although the gene from strain GS5 contained a 24 base pair deletion. A 29 amino acid signal peptide was specified by each wapA gene with a mature protein of 424 amino acids ( M r , 45276) for strain Ingbritt and 416 amino acids ( M r , 44846) for strain GS5. In the C ‐terminal region of the wall‐associated protein A, considerable sequence similarity was found with the membrane anchor region of proteins from other Gram‐positive organisms such as the group A streptococcal M protein and the group G streptococcal IgG binding protein. Adjacent to the proposed membrane anchor is a highly hydrophilic region which may span the cell wall; both sequence data and experimental evidence indicate the existence of a region immediately outside the wall at which proteolytic cleavage occurs to release antigen A of M r 29000 into the culture supernatant. Thus, the wall‐associated protein A is a precursor of the 29000 M r antigen A.