Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.7.8.B10	gene clsA, recombinant expression of wild-type and deletion mutant enzymes in Escherichia coli strain JM109	Bacillus subtilis

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.7.8.B10	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

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
2.7.8.B10	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	-
2.7.8.B10	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	-	-

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.7.8.B10	a phosphatidylglycerol + a phosphatidylglycerol	Bacillus subtilis	-	a cardiolipin + glycerol	-	?
2.7.8.B10	a phosphatidylglycerol + a phosphatidylglycerol	Bacillus subtilis 168	-	a cardiolipin + glycerol	-	?
2.7.8.B10	additional information	Bacillus subtilis	the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin	?	-	?
2.7.8.B10	additional information	Bacillus subtilis 168	the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin	?	-	?
2.7.8.B11	a phosphatidylglycerol + a phosphatidylethanolamine	Escherichia coli	-	a cardiolipin + ethanolamine	-	?
2.7.8.B11	additional information	Escherichia coli	the enzyme homologue ClsC1 (YmdC) uses both phosphatidylethanolamine and phoshatidylglycerol as substrates for cardiolipin synthesis with the assistance of YmdB (ClsC2), the product of a neighboring gene. Enzyme homologue ClsB may also use some phospholipid other than phosphatidylglycerol	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.8.B10	Bacillus subtilis	-	-	-
2.7.8.B10	Bacillus subtilis 168	-	-	-
2.7.8.B11	Escherichia coli	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.7.8.B10	a phosphatidylglycerol + a phosphatidylglycerol	-	Bacillus subtilis	a cardiolipin + glycerol	-	?
2.7.8.B10	a phosphatidylglycerol + a phosphatidylglycerol	-	Bacillus subtilis 168	a cardiolipin + glycerol	-	?
2.7.8.B10	additional information	the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin	Bacillus subtilis	?	-	?
2.7.8.B10	additional information	the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin	Bacillus subtilis 168	?	-	?
2.7.8.B11	a phosphatidylglycerol + a phosphatidylethanolamine	-	Escherichia coli	a cardiolipin + ethanolamine	-	?
2.7.8.B11	additional information	the enzyme homologue ClsC1 (YmdC) uses both phosphatidylethanolamine and phoshatidylglycerol as substrates for cardiolipin synthesis with the assistance of YmdB (ClsC2), the product of a neighboring gene. Enzyme homologue ClsB may also use some phospholipid other than phosphatidylglycerol	Escherichia coli	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.7.8.B10	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

EC Number	Synonyms	Comment	Organism
2.7.8.B10	cardiolipin synthase	-	Bacillus subtilis
2.7.8.B10	CL synthase	-	Bacillus subtilis
2.7.8.B10	clsA	-	Bacillus subtilis
2.7.8.B11	cardiolipin synthase	-	Escherichia coli
2.7.8.B11	ClsC1	-	Escherichia coli
2.7.8.B11	YmdC	-	Escherichia coli

General Information

EC Number	General Information	Comment	Organism
2.7.8.B10	evolution	the enzyme belongs to the PLD superfamily of enzymes	Bacillus subtilis
2.7.8.B10	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

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Release 2023.1 (January 2023)