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PROSITE documentation PDOC00293 |
Gram-negative bacteria produce a number of proteins which are secreted into the growth medium by a mechanism that does not require a cleaved N-terminal signal sequence. These proteins, while having different functions, seem [1] to share two properties: they bind calcium and they contain a variable number of tandem repeats consisting of a nine amino acid motif rich in glycine, aspartic acid and asparagine. It has been shown [2] that such a domain is involved in the binding of calcium ions in a parallel β roll structure. The proteins which are currently known to belong to this category are:
We derived a signature pattern from conserved positions in the sequence of the calcium-binding domain.
Note:This pattern is found once in nodO and the extracellular proteases but up to 5 times in some hemolysin/cyclolysins.
Last update:October 1993 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Economou A. Hamilton W.D.O. Johnston A.W. Downie J.A. |
Title | The Rhizobium nodulation gene nodO encodes a Ca2(+)-binding protein that is exported without N-terminal cleavage and is homologous to haemolysin and related proteins. | |
Source | EMBO J. 9:349-354(1990). | |
PubMed ID | 2303029 |
2 | Authors | Baumann U. Wu S. Flaherty K.M. McKay D.B. |
Title | Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. | |
Source | EMBO J. 12:3357-3364(1993). | |
PubMed ID | 8253063 |