(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 > Pseudomonadales: NE > Moraxellaceae: NE > Acinetobacter: NE > Acinetobacter calcoaceticus/baumannii complex: NE > Acinetobacter calcoaceticus: 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
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Acinetobacter lwoffii: N, E.
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 QIRPIRLAGVRGEEIKAQASATQLIFHIHGGAFFLGSLNTHRALMTDLAS RTQMQVIHVDYPLAPEHPYPEAIDAIFDVYQALLVQGIKPKDIIISGDSC GANLALALSLRLKQQPELMPSGLILMSPYLDLTLTSESLRFNQKHDALLS IEALQAGIKHYLTDDIQPGDPRVSPLFDDLDGLPPTLVQVGSKEILLDDS KRFREKAEQADVKVHFKLYTGMWNNFQMFNAWFPEAKQALADIAEFATSL DLD
References
Title: Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases Kok RG, Christoffels VM, Vosman B, Hellingwerf KJ Ref: J Gen Microbiol, 139:2329, 1993 : PubMed
Acinetobacter calcoaceticus BD413, when grown in batch culture in nutrient broth, produces both extracellular lipase activity and cell-bound esterase activity during and after the transition between exponential growth and the stationary phase. From a library of A. calcoaceticus DNA in Escherichia coli, plasmids were isolated that enabled E. coli to grow on media with tributyrin as the sole carbon source. Assays with model substrates classified the product of the cloned gene as an esterase. Via deletion analysis, the esterase gene was mapped on a 1.8 kbp chromosomal DNA fragment. This fragment was sequenced and found to contain one open reading frame, termed estA, which encodes a protein of 40.0 kDa. The amino acid sequence of this protein shows homology to a number of lipolytic enzymes, most notably to esterases. Deletion of estA only partially abolished cell-bound esterase activity in A. calcoaceticus, indicating that BD413 forms at least two esterases. Both esterases show the same temporal regulation of expression. beta-Galactosidase activity was measured in strains in which a promoterless lacZ gene was inserted into estA. Induction of lacZ expression in these strains also occurred at the end of exponential growth in batch cultures, indicating that production of the esterase is regulated at the genetic level.
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.
