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PROSITE documentation PDOC00283Bacterial ice-nucleation proteins octamer repeat
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00283
Some Gram-negative bacteria express proteins that enable them to promote the nucleation of ice at relatively high temperature (above -5 degree Celsius) [1,2,3]. These proteins are localized at the surface of the outer membrane of the bacteria and can cause frost injury to many plant species. The primary structure of these ice-nucleation proteins is highly repetitive. A central repetitive domain represents about 80% of the total sequence. This domain is mainly formed by the repetition of a conserved region of forty eight residues (48-mer). The 48-mers are themselves composed of three blocks of 16 residues (16-mer). The first eight residues of each of these 16-mers are identical. It has been proposed that the repetitive domain may be directly responsible for aligning water molecules in the seed crystal.
Schematic structure of a 48-mer region:
[.........48.residues.repeated.domain..........]
/ / | | \ \
AGYGSTxTagxxssli AGYGSTxTagxxsxlt AGYGSTxTaqxxsxlt
[16.residues...] [16.residues...] [16.residues...]
Last update:
June 1994 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Wolber P. Warren G. |
| Title | Bacterial ice-nucleation proteins. | |
| Source | Trends Biochem. Sci. 14:179-182(1989). | |
| PubMed ID | 2672438 |
| 2 | Authors | Wolber P.K. |
| Source | Adv. Microb. Physiol. 34:205-237(1992). |
| 3 | Authors | Gurian-Sherman D. Lindow S.E. |
| Source | FASEB J. 7:1338-1343(1993). |
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