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- W2384169626 abstract "Bioinformatics softwares were used to predict and analyse the biological properties of plnBCD encoded proteins in Lactobacillus paraplantarumL-XM1,the functions of PlnBCD were also predicted.The physical and chemical properties,hydrohobicity,phospholyration sites,conserved domain,secondary structure information of the plnBCD encoded proteins were predicted using RPS-Blast,InterProscan,TMHMM Server,etc..Three-dimensional structure models were constructed using Swiss-Model homology modeling.The results showed that plnB encoded protein was a hydrophobic protein,and located in the plasma membrane,with six transmembrane regions and 21phosphorylation sites,one HATPase_c domain,which was consistent with the basic nature of most histidine protein kinase.α-helix and extended chains were the main secondary structure elements of plnB encoded protein.The spatial model of this protein was consistent with the histidine protein kinase.Both plnCand plnDencoded proteins were hydrophilic proteins,without transmembrane regions,located in the cytoplasm,and both were found with a REC domain and a LytTR domain.Both spatial models of plnC and plnD encoded proteins were similar to the response regulatory protein.Therefore,we predict that proteins encoded by plnBCDof strain L-XM1are components of quorum sensing system.The bioinformatics analysis of plnBCD provide a reference for finding a new quorum sensing system and a deep understanding of the functions of quorum-sensing components." @default.
- W2384169626 created "2016-06-24" @default.
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- W2384169626 date "2014-01-01" @default.
- W2384169626 modified "2023-09-23" @default.
- W2384169626 title "Bioinformatics analysis of the plnBCDgene from Lactobacillus paraplantarum L-XM1" @default.
- W2384169626 hasPublicationYear "2014" @default.
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