(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Enterobacterales: NE > Yersiniaceae: NE > Serratia: NE > Serratia sp. MK1: NE
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 MSMSLSFTSAIAPAAIQPPMVRTQPEPLSSSQPVEASATKAPVATLSQNS LNAQSLLNTLVSEISAAAPAAANQGVTRGQQPQKGDYTLALLAKDVYSTG SQGVEGFNRLSADALLGAGIDPASLQDAASGFQAGIYTDNQQYVLAFAGT NDMRDWLSNVRQATGYDDVQYNQAVSLAKSAKAAFGDALVIAGHSLGGGL AATAALATGTVAVTFNAAGVSDYTLNRMGIDPAAAKQDAQAGGIRRYSEQ YDMLTGTQESTSLIPDAIGHKITLANNDTLSGIDDWRPSKHLDRSLTAHG IDKVISSMAEQKPWEAMANA
Reference
Title: Cloning and expression of the gene encoding phospholipase A1 from Serratia sp. MK1 in Escherichia coli Song JK, Kim MK, Rhee JS Ref: J Biotechnol, 72:103, 1999 : PubMed
The gene encoding extracellular phospholipase A1 of Serratia sp. MK1 was cloned from a genomic DNA library. Formation of transparent halos on the PCY agar plates was used to identify E. coli carrying the phospholipase A1 gene. A 4.2 kb EcoRI fragment was isolated and sequenced. From nucleotide sequences and expression of various plasmids, two open reading frames (plaA and plaS) involved in efficient expression of phospholipase A1 in natural and recombinant host were identified. Extracellular phospholipase A1 activity was identified as the gene product of plaA encoding 321 amino acids with a predicted MW of 33,400. Analysis of the amino acid sequence revealed significant homology (around 70%) to phospholipase A1 of Serratia liquefaciens and Yersinia enterocolitica. The sequence, -Gly-X1-Ser-X2-Gly-, known as a lipase-specific consensus sequence was also found in the bacterial phospholipase A1. PlaS encoding a protein of 224 amino acids showed no enzymatic activity, but might be necessary for the efficient expression of phospholipase A1 in E. coli. To further improve the production of phospholipase A1 as a soluble and active form in E. coli, the effect of some parameters was examined. Surprisingly, a higher yield of soluble and active phospholipase A1 could be obtained under the combined conditions of a lower temperature, an enriched medium, and a lower-strength promoter.
