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Literature summary for 2.7.8.B10 extracted from

  • Kusaka, J.; Shuto, S.; Imai, Y.; Ishikawa, K.; Saito, T.; Natori, K.; Matsuoka, S.; Hara, H.; Matsumoto, K.
    Septal localization by membrane targeting sequences and a conserved sequence essential for activity at the COOH-terminus of Bacillus subtilis cardiolipin synthase (2016), Res. Microbiol., 167, 202-214.
    View publication on PubMed
Search for more literature for 2.7.8.B10

Cloned(Commentary)

Cloned (Comment) Organism
gene clsA, recombinant expression of wild-type and deletion mutant enzymes in Escherichia coli strain JM109 Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information 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 Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane septal membranes. Recombinant GFP fusion proteins of enzyme ClsA with N-terminal and internal deletions retain septal localization. Enzyme mutants with deletions starting from the C-terminus (Leu482) cease to localize to the septum once the deletion passes the Ile residue at 448, indicating that the sequence responsible for septal localization is confined within a short distance from the C-terminus. Enzyme ClsA contains a specific region responsible for the septal membrane localization Bacillus subtilis 16020
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additional information two sequences, Ile436-Leu450 and Leu466-Leu478, individually form an amphipathic alpha-helix. The configuration is a membrane targeting sequence (MTS), MTS2 and MTS1, respectively. Either one has the ability to affect septal localization, and each of these sequences by itself localizes to the septum Bacillus subtilis
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a phosphatidylglycerol + a phosphatidylglycerol Bacillus subtilis
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 a cardiolipin + glycerol
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 ?
a phosphatidylglycerol + a phosphatidylglycerol Bacillus subtilis 168
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 a cardiolipin + glycerol
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 ?
additional information Bacillus subtilis the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin ?
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 ?
additional information Bacillus subtilis 168 the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin ?
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 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Bacillus subtilis 168
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a phosphatidylglycerol + a phosphatidylglycerol
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 Bacillus subtilis a cardiolipin + glycerol
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 ?
a phosphatidylglycerol + a phosphatidylglycerol
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 Bacillus subtilis 168 a cardiolipin + glycerol
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 ?
additional information the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin Bacillus subtilis ?
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 ?
additional information the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin Bacillus subtilis 168 ?
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 ?

Subunits

Subunits Comment Organism
More the predicted domain structure of Bacillus subtilis major CL synthase, ClsA (482 residues), shows two HKD motif segments (H222-N239, H400-N417). Probable catalytic sites, which are conserved in the PLD superfamily of enzymes, are: in the middle of ClsA and at the N-terminus, a pair of transmembrane alpha-helices (I3-F24 and W34-H56) Bacillus subtilis

Synonyms

Synonyms Comment Organism
cardiolipin synthase
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 Bacillus subtilis
CL synthase
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 Bacillus subtilis
clsA
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 Bacillus subtilis

General Information

General Information Comment Organism
evolution the enzyme belongs to the PLD superfamily of enzymes Bacillus subtilis
additional information the fact that the homologues YwiE and YwjE show almost no detectable cardiolipin synthesis activity in Bacillus subtilis cells under laboratory conditions, although both localize septally, suggests a much stricter consensus motif S-P-(I/L)-L for bacterial CL synthase, that is, the two residues in the middle of the four conserved residues may have to be taken into account for activity Bacillus subtilis