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Q51026793-2A9F8853-01D8-4283-B2C4-34BA263CF11C
Q51026793-2A9F8853-01D8-4283-B2C4-34BA263CF11C
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http://www.wikidata.org/entity/statement/Q51026793-2A9F8853-01D8-4283-B2C4-34BA263CF11C
Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.
P2860
Q51026793-2A9F8853-01D8-4283-B2C4-34BA263CF11C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q51026793-2A9F8853-01D8-4283-B2C4-34BA263CF11C
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wasDerivedFrom
a0dcfee93a6451b602bab00f9cc42e37ab5f2a59
P2860
The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis