(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Paenibacillaceae: NE > Paenibacillus: NE > Paenibacillus amylolyticus: NE
MRKLKLLLMVCMSMVFIFTLPGMGQSLKASAATERTPIVFVHGLTGSDSN
FALIERYLRGEGWSSDELFAIDLPSKAGNQLLNSAAISRFVDDVLRQTGH
SKVHIVAHSMGGANSLYYILNRGGIDKVDKLITLGGANRLTTSRAPDGIR
VTSIYSTSDTIVSPALSRLDGANNISVNLVTHIGLLYNSRVNALIKAALI
E
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MRKLKLLLMVCMSMVFIFTLPGMGQSLKASAATERTPIVFVHGLTGSDSN FALIERYLRGEGWSSDELFAIDLPSKAGNQLLNSAAISRFVDDVLRQTGH SKVHIVAHSMGGANSLYYILNRGGIDKVDKLITLGGANRLTTSRAPDGIR VTSIYSTSDTIVSPALSRLDGANNISVNLVTHIGLLYNSRVNALIKAALI E
The gene encoding a poly(DL-lactic acid) (PLA) depolymerase from Paenibacillus amylolyticus strain TB-13 was cloned and overexpressed in Escherichia coli. The purified recombinant PLA depolymerase, PlaA, exhibited degradation activities toward various biodegradable polyesters, such as poly(butylene succinate), poly(butylene succinate-co-adipate), poly(ethylene succinate), and poly(epsilon-caprolactone), as well as PLA. The monomeric lactic acid was detected as the degradation product of PLA. The substrate specificity toward triglycerides and p-nitrophenyl esters indicated that PlaA is a type of lipase. The gene encoded 201 amino acid residues, including the conserved pentapeptide Ala-His-Ser-Met-Gly, present in the lipases of mesophilic Bacillus species. The identity of the amino acid sequence of PlaA with Bacillus lipases was no more than 45 to 50%, and some of its properties were different from those of these lipases.