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Q28488952-5C7D60AA-1E0E-4B0A-A0FA-0BF1475A0C60
Q28488952-5C7D60AA-1E0E-4B0A-A0FA-0BF1475A0C60
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http://www.wikidata.org/entity/statement/Q28488952-5C7D60AA-1E0E-4B0A-A0FA-0BF1475A0C60
Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B
P2860
Q28488952-5C7D60AA-1E0E-4B0A-A0FA-0BF1475A0C60
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28488952-5C7D60AA-1E0E-4B0A-A0FA-0BF1475A0C60
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wasDerivedFrom
0a7edef8bdd9f2b76df8223ad93c300acecf0f22
P2860
The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components.