N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Pseudomonadales: NE > Moraxellaceae: NE > Acinetobacter: NE > Acinetobacter lwoffii: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. Acinetobacter lwoffii SH145: N, E.
Acinetobacter lwoffii NIPH 715: N, E.
Acinetobacter lwoffii CIP 70.31: N, E.
Acinetobacter lwoffii NIPH 512: N, E.
Acinetobacter lwoffii NIPH 478: N, E.
Acinetobacter lwoffii NCTC 5866 = CIP 64.10 = NIPH 512: N, 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 MKFGTVWKYYFTESLLKATIRTPSQLNLAPNALRPVLDQLCRLFPQNPTV QIRPIRLAGVRGEEIKAQASATQLIFHIHGGAFFLGSLNTHRALMTDLAA RTQMQVIHVDYPLAPEHPYPEAIDAIFDVYQALLVQGIKPKDIIISGDSC GANLALALCLRLKQQPELMPSGLILMSPYLDLTLTSESLRFNQKHDALLS IEALQAGIKHYLTDDIQPGDPRVSPLFDDLDGLPPTLVQVGSKEILLDDS KRFREKAEQADVKVHFKLYTGMWHNFQMFNAWFPEAKQALADIAEFAHSL DLD
The est gene encoding an esterase from Acinetobacter lwoffii RAG-1 was cloned into E. coli under the control of the PL promoter of the phage lambda. The N-terminal sequence of the first 20 amino acids of the heterologous expressed esterase corresponded to that obtained from the nucleotide sequence. Antibodies prepared against the over-expressed recombinant esterase in E. coli were used to locate the enzyme primarily in the membrane fractions of A. lwoffii RAG-1. Comparison with homologous proteins from both eukaryotic and prokaryotic organisms suggest that the RAG-1 esterase exhibits sequence motifs characteristic of both serine proteases and of lipases.
Title: Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1 Reddy PG, Allon R, Mevarech M, Mendelovitz S, Sato Y, Gutnick DL Ref: Gene, 76:145, 1989 : PubMed
A putative esterase gene (est) from Acinetobacter calcoaceticus RAG-1 has been cloned into Escherichia coli. Esterase-positive clones exhibited high levels of esterase activity even in intact cells. In addition, expression of the est gene conferred on E. coli the ability to grow on simple triglycerides such as triacetin (TAC). The original esterase-positive plasmid pRA17 carried a 2.2-kb insert from a partial MboI digest of RAG-1 DNA, which gave a single band with RAG-1 DNA following Southern hybridization. By subcloning and sequencing the est gene was found to contain a sequence of 870 bp which could be translated to yield a protein of Mr 32,700. In support of the sequencing results was the finding that when pRA17 was expressed in minicells, a unique peptide of Mr 32,500 was identified. This peptide was not found in minicells transformed with esterase-negative plasmids, such as pRA176, which contained a Tn5 insertion in the est gene. The fact that the production of active esterase depended on the orientation of the est gene within the vector suggested that transcription proceeded from the tet promoter in pBR322.