EC Number   |
Protein Variants |
Reference |
|---|
    2.7.8.B10 | delT2-E60 |
a deletion mutant that is missing residues 260 produces a fully active protein |
727065 |
| 2.7.8.B10 | G59A |
mutation has little if any effect on cardiolipin synthase processing or activity |
727065 |
| 2.7.8.B10 | H113A |
mutation in HKD motif, catalyticlly inactive |
761454 |
| 2.7.8.B10 | H215R |
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin |
-, 726689 |
| 2.7.8.B10 | H215R |
the mutation is associated with adaptation to daptomycin and increases the enzyme activity compared to the wild-type enzyme, Cls447aH215R shows an increase in Vmax from 0.00016 (wild-type) to 0.00026 mM cardiolipin/min/mM protein |
-, 726689 |
| 2.7.8.B10 | H224A/H404A |
mutations inactivate ClsA and compromise transporter ProP localization |
761920 |
| 2.7.8.B10 | H291A |
mutation in HKD motif, catalyticlly inactive |
761454 |
| 2.7.8.B10 | K438R |
a lipolytically inactive form of mclS, O35E.mclS.K438R |
738526 |
| 2.7.8.B10 | L7S/V8S |
an EYMPE epitope tag is introduced into the interior of Cardiolipin synthase. The tagged polypeptide retains the biological properties of wild type enzyme, including full enzymatic activity. Site-directed mutagenesis is used to alter conserved residues in the N-terminal region. An tagged cardiolipin synthase in which Leu7 and Val8 are both replaced by Ser residues retains in vitro activity but loses most of its in vivo activity. The mutant protein has a higher apparent molecular mass than its parent protein. That conserved residues L7 and V8 play a role in polypeptide processing, topology, or both |
727065 |
| 2.7.8.B10 | more |
cardiolipin synthesis is abolished after deleting the last residue, Leu482, in the C-terminal four amino acid residue sequence, Ser-Pro-Ile-Leu, which is highly conserved among bacterial CL synthases. A series of N-terminal, internal, and C-terminal deletion derivatives of ClsA fused to GFP are constructed using plasmid vectors pSG1729 and pSG1154. Construction of a series of GFP-tagged membrane targeting sequence derivatives, GFP-MTS(s), and fusion proteins formed by the C- and N-termini. Integration of the constructed clsA alleles into the amyE locus of wild-type strain 168 and CL-deficient BSF219 strain. Analysis of expression and subcellular localization of the mutant proteins, immunohistochemic detection, overview. The cardiolipin-deficient mutant cells of Bacillus subtilis strain BFS219 is harboring an allele of a defective derivative of clsA. A fusion of GFP to the extreme COOH-terminus does not affect septal localization, i.e. the role in septal localization played by the amphipathic alpha-helices is not affected by GFP-fusion |
-, 739625 |
