(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. XJF1: 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 MSLPLSFISTMTPITAASASSLPLQDAIKPVQTDEPQVTKVAVPLPSENS RNAQNLLNSLTRDLSAAVPLAPRLEMSRGQESQQGDYSLALLAKDVYNLT GQGAEGFSRMSDNDLLSVGIDPASLLDAASGLQAGIYSNKQHYVLAFAGT NDMRDWLSNVRQATGYDDVQYNHAVAIAKNAKAAFGDGLVITGHSLGGGL AATAALATGSLAVTFNAAGVSDHTLNRFGINPAAAKQDAESGGIRRYSEQ YDMLTGTQESTSLLPDAIGHKITIANNETLSGTDAWRPSKYLDRSMTAHG IDKVISSMAEQKPWEIKANA
Reference
Title: A novel cold-adapted phospholipase A(1) from Serratia sp. xjF1: Gene cloning, expression and characterization Fu J, Huang H, Meng K, Yuan T, Yao B, Shi Y, Ouyang P Ref: Enzyme Microb Technol, 42:187, 2008 : PubMed
The gene encoding a cold-adapted phospholipase A(1) (PLA(1)) from a psychrotrophic, glacier soil bacterium Serratia sp. xjF1 was cloned by two-step PCR (general PCR and TAIL-PCR). The full-length fragment comprised two open reading frames plA and plS. The gene product of plA encoding 320 amino acids with a molecular weight of 33.8kDa was identified as a phospholipase A(1). Its amino acid sequence exhibited the highest homology to PLA(1) of Serratia marcescens (71%). plS encoded a protein of 251 amino acids, which showed no enzymatic activity. The result of plA expression in Escherichia coli indicated that plS might improve the efficient expression of PLA(1) in E. coli. Furthermore, PLA(1) was functionally expressed in Pichia pastoris, yielding 41.8U/mL in a 3.7L fermentor. The purified recombinant phospholipase A(1) (rPLA(1)) had features typical of cold-adapted enzymes with a temperature optimum of 35 degrees C and a maximum activity of 70% at 10 degrees C. The rate of catalysis was optimal at pH 9.0 and the enzyme could be slightly activated by Ca(2+). This is the first report on gene isolation and expression of cold-adapted PLA(1).
