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evolution
Cafeteria sp.
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Cafeteria sp. Caron contains both, a CLS_cap enzyme homologue, and a CLS_pld homologue
evolution
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Cantina marsupialis contains only a CLS_pld enzyme homologue, no CLS_cap, EC 2.7.8.41, homologue
evolution
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Wobblia lunata contains both, a CLS_cap enzyme homologue, and a CLS_pld homologue
evolution
phylogenetic analysis reveals that gene cls1 is generated through the duplication of gene cls2 after the divergence of the genus Staphylococcus
evolution
-
the enzyme belongs to the PLD superfamily of enzymes
evolution
the enzyme is a member of the PLD superfamily of proteins, the enzyme is conserved among Moraxella catarrhalis isolates
evolution
-
the enzyme belongs to the PLD superfamily of enzymes
-
evolution
-
phylogenetic analysis reveals that gene cls1 is generated through the duplication of gene cls2 after the divergence of the genus Staphylococcus
-
evolution
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Wobblia lunata contains both, a CLS_cap enzyme homologue, and a CLS_pld homologue
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malfunction
Escherichia coli has three cardiolipin synthases. Cardiolipin synthase A encoded by clsA, cardiolipin synthase B encoded by clsB and cardiolipin synthase C, encoded by clsC. Triple deletions of clsA, clsB, and clsC results in the complete depletion of cardiolipin synthase activity in Escherichia coli cells. The double mutant DELTAclsAB mutant still makes cardiolipin in the stationary phase
malfunction
a cls1 mutant is equal to the wild-type in terms of CL accumulation and stress tolerance. But below pH 2.6, the cls1 mutant (i.e. carrying Cls2 alone) cannot produce cardiolipin
malfunction
a cls2 mutant (carrying Cls1 alone) effectively accumulates cardiolipin at pH 2.6 and below
malfunction
cardiolipin-deficient Moraxella catarrhalis exhibits wild-type growth in complete medium and under osmotic stress
malfunction
Alkalihalophilus pseudofirmus
no detectablecardiolipin is found in DELTAclsA mutants, whereas the cardiolipin precursor phosphatidylglycerol is elevated. The DELTAclsB mutant exhibits no significant reduction in cardiolipin, but at pH 7.5, clsB expression is upregulated and appears growth. In the absence of detectable cardiolipin, the alkaliphile shows no significant deficits in non-fermentative growth, respiration-dependent ATP synthesis, or salt tolerance. In long term survival experiments, significant growth defects are found in DELTAclsA strains and the DELTAclsC strain at pH10.5. Both the single DELTAclsA and triple deletion mutants have a significant reduction in NADH dehydrogenase activity
malfunction
-
a cls1 mutant is equal to the wild-type in terms of CL accumulation and stress tolerance. But below pH 2.6, the cls1 mutant (i.e. carrying Cls2 alone) cannot produce cardiolipin
-
malfunction
-
a cls2 mutant (carrying Cls1 alone) effectively accumulates cardiolipin at pH 2.6 and below
-
malfunction
Alkalihalophilus pseudofirmus OF4
-
no detectablecardiolipin is found in DELTAclsA mutants, whereas the cardiolipin precursor phosphatidylglycerol is elevated. The DELTAclsB mutant exhibits no significant reduction in cardiolipin, but at pH 7.5, clsB expression is upregulated and appears growth. In the absence of detectable cardiolipin, the alkaliphile shows no significant deficits in non-fermentative growth, respiration-dependent ATP synthesis, or salt tolerance. In long term survival experiments, significant growth defects are found in DELTAclsA strains and the DELTAclsC strain at pH10.5. Both the single DELTAclsA and triple deletion mutants have a significant reduction in NADH dehydrogenase activity
-
metabolism
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
metabolism
Cafeteria sp.
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
metabolism
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
metabolism
Alkalihalophilus pseudofirmus
the clsA gene plays a major role in cardiolipin biosynthesis
metabolism
Alkalihalophilus pseudofirmus OF4
-
the clsA gene plays a major role in cardiolipin biosynthesis
-
metabolism
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
-
physiological function
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. Gene cls2 encodes a housekeeping-type CL synthase
physiological function
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. The physiological role of cls1 is to synthesize cardiolipin under conditions of acute low-pH stress
physiological function
Alkalihalophilus pseudofirmus
cardiolipin is not essential for oxidative phosphorylation and the non-fermentative growth it supports in alkaliphilic Bacillus pseudofirmus strain OF4, during growth at either pH 7.5 or pH 10.5. Cardiolipin does not seem be a crucial participant in the proton movements on or near the membrane surface from proton-pumping respiratory chain complexes to the F1F0-ATP synthase complex
physiological function
enzyme MclS is responsible for the synthesis of cardiolipin, which is a major component of the Moraxella catarrhalis cell envelope, constituting 5-30% of the total membrane phospholipid. The mclS gene product is not required for optimal growth of Moraxella catarrhalis in vitro. Expression of the mclS gene product impacts the adherence of Moraxella catarrhalis to human epithelial cells. The contribution of mclS to adherence is indirect, possibly by modulating the proper surface display of Moraxella catarrhalis adhesins on the bacterial surface through its CLS activity
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
physiological function
a ClsA mutant has no cardiolipin detected within its membrane, grows normally in vitro, and invades cultured epithelial cells, but it fails to form plaques in epithelial cell monolayers. The ClsA mutant is initially motile within the host cell cytoplasm but forms filaments and loses motility during replication and fails to spread efficiently to neighboring cells
physiological function
a minor decrease of cardiolipin content is observed in the ClsA overexpression strain. Phosphatidylethanolamine and phosphatidylglycerol levels remain unaltered upon overexpression of ClsA. ClsA deletion leads to abolishment of phosphytidylcholine-dependent phosphatidylalcohol formation
physiological function
a modest increase of cardiolipin content is observed in the ClsB overexpression strain. Overexpression of ClsB also leads to an increase of phosphatidylethanolamine from 67% to 79% and a decrease of phosphatidylglycerol content from 31% to 14% of phospholipids. Overexpression of ClsB leads to formation of phosphatidylalcohols whereas levels of phosphatidylalcohols are unaltered in the clsB knockout mutant
physiological function
-
ClsA and proteins YdhP, YjbJ interact with transporter ProP. All three proteins are concentrated at the cell poles, but only ClsA localization was cardiolipin-dependent. ClsA is N-terminally processed and membrane-anchored, with dual, cytoplasmic, catalytic domains
physiological function
ClsB additionally catalyzes an alternative mechanism for phosphatidylglycerol synthesis that is PgsA-independent. The reaction in vivo and in vitro converts phosphatidylethanolamine and glycerol into phosphatidylglycerol. When the growth medium is supplemented with glycerol, the expression ClsB significantly increases phosphatidylglycerol and cardiolipin levels, with the growth deficiency of PgsA null strain also being complemented under such conditions
physiological function
-
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. The physiological role of cls1 is to synthesize cardiolipin under conditions of acute low-pH stress
-
physiological function
-
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. Gene cls2 encodes a housekeeping-type CL synthase
-
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
-
physiological function
Alkalihalophilus pseudofirmus OF4
-
cardiolipin is not essential for oxidative phosphorylation and the non-fermentative growth it supports in alkaliphilic Bacillus pseudofirmus strain OF4, during growth at either pH 7.5 or pH 10.5. Cardiolipin does not seem be a crucial participant in the proton movements on or near the membrane surface from proton-pumping respiratory chain complexes to the F1F0-ATP synthase complex
-
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
-
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
-
additional information
-
daptomycin (DAP) is a cyclic lipopeptide antibiotic, that has demonstrated rapid in vitro bactericidal activity against clinically significant strains of Gram-positive bacteria. DAP inserts into the plasma membrane in a calcium-dependent manner and subsequently disrupts the functional integrity of the cell membrane, altering cell division. DAP forms membrane-associated oligomers on liposomes and bacterial cells, suggesting that it is phosphatidylglycerol-dependent oligomerization of DAP that contributes to its effectiveness in altering membrane homeostasis. Role of Cls and adaptive variants Cls447aR218Q and Cls447aH215R in altering cardiolipin synthesis
additional information
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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
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
-
additional information
-
daptomycin (DAP) is a cyclic lipopeptide antibiotic, that has demonstrated rapid in vitro bactericidal activity against clinically significant strains of Gram-positive bacteria. DAP inserts into the plasma membrane in a calcium-dependent manner and subsequently disrupts the functional integrity of the cell membrane, altering cell division. DAP forms membrane-associated oligomers on liposomes and bacterial cells, suggesting that it is phosphatidylglycerol-dependent oligomerization of DAP that contributes to its effectiveness in altering membrane homeostasis. Role of Cls and adaptive variants Cls447aR218Q and Cls447aH215R in altering cardiolipin synthesis
-
additional information
-
daptomycin (DAP) is a cyclic lipopeptide antibiotic, that has demonstrated rapid in vitro bactericidal activity against clinically significant strains of Gram-positive bacteria. DAP inserts into the plasma membrane in a calcium-dependent manner and subsequently disrupts the functional integrity of the cell membrane, altering cell division. DAP forms membrane-associated oligomers on liposomes and bacterial cells, suggesting that it is phosphatidylglycerol-dependent oligomerization of DAP that contributes to its effectiveness in altering membrane homeostasis. Role of Cls and adaptive variants Cls447aR218Q and Cls447aH215R in altering cardiolipin synthesis
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delT2-E60
a deletion mutant that is missing residues 260 produces a fully active protein
G59A
mutation has little if any effect on cardiolipin synthase processing or activity
H113A
mutation in HKD motif, catalyticlly inactive
H224A/H404A
-
mutations inactivate ClsA and compromise transporter ProP localization
H291A
mutation in HKD motif, catalyticlly inactive
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
K438R
a lipolytically inactive form of mclS, O35E.mclS.K438R
H215R
-
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin
H215R
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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
R218Q
-
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin
R218Q
-
the mutation is associated with adaptation to daptomycin and increases the enzyme activity compared to the wild-type enzyme, Cls447aR218Q shows an increase in Vmax from 0.00016 (wild-type) to 0.00026 mM cardiolipin/min/mM protein
H215R
-
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin
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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
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R218Q
-
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin
-
R218Q
-
the mutation is associated with adaptation to daptomycin and increases the enzyme activity compared to the wild-type enzyme, Cls447aR218Q shows an increase in Vmax from 0.00016 (wild-type) to 0.00026 mM cardiolipin/min/mM protein
-
H215R
-
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin
-
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
-
R218Q
-
mutation results in an 1.6fold increase in Vmax, mutation is associated with adaption to daptomycin
-
R218Q
-
the mutation is associated with adaptation to daptomycin and increases the enzyme activity compared to the wild-type enzyme, Cls447aR218Q shows an increase in Vmax from 0.00016 (wild-type) to 0.00026 mM cardiolipin/min/mM protein
-
additional information
Alkalihalophilus pseudofirmus
construction of three single, DELTAclsA, DELTAclsB, and DELTAclsC, one double, DELTAclsA/B, and one triple, DELTAclsA/B/C, mutants
additional information
Alkalihalophilus pseudofirmus OF4
-
construction of three single, DELTAclsA, DELTAclsB, and DELTAclsC, one double, DELTAclsA/B, and one triple, DELTAclsA/B/C, mutants
-
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
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
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additional information
-
the adaptive mutations Cls447aH215R and Cls447aR218Q are proximal to the phospholipase domain 1 (PLD1) active site and near the putative nucleophile H217. As mutations to Cls are part of a larger genomic adaptation process, increased Cls activity is likely to be highly epistatic with other changes to facilitate DAP resistance. ClsR218Q mutation does not affect DAP susceptibility, supporting the idea that changes to Cls function in a broader context with other adaptive changes, such as alterations in the LiaFRS signaling pathway
additional information
-
the adaptive mutations Cls447aH215R and Cls447aR218Q are proximal to the phospholipase domain 1 (PLD1) active site and near the putative nucleophile H217. As mutations to Cls are part of a larger genomic adaptation process, increased Cls activity is likely to be highly epistatic with other changes to facilitate DAP resistance. ClsR218Q mutation does not affect DAP susceptibility, supporting the idea that changes to Cls function in a broader context with other adaptive changes, such as alterations in the LiaFRS signaling pathway
-
additional information
-
the adaptive mutations Cls447aH215R and Cls447aR218Q are proximal to the phospholipase domain 1 (PLD1) active site and near the putative nucleophile H217. As mutations to Cls are part of a larger genomic adaptation process, increased Cls activity is likely to be highly epistatic with other changes to facilitate DAP resistance. ClsR218Q mutation does not affect DAP susceptibility, supporting the idea that changes to Cls function in a broader context with other adaptive changes, such as alterations in the LiaFRS signaling pathway
-
additional information
cls has about 100 residues at the N-terminus that are missing from the polypeptide specified by the homologous gene f413 (cardiolipin synthase B). The f413 protein catalyzes cardiolipin formation in vitro but not in vivo. Amino acid residues specified by the first 60 codons in cls are not essential for catalytic activity
additional information
cls has about 100 residues at the N-terminus that are missing from the polypeptide specified by the homologous gene f413 (cardiolipin synthase B). The f413 protein catalyzes cardiolipin formation in vitro but not in vivo. Amino acid residues specified by the first 60 codons in cls are not essential for catalytic activity
additional information
-
cls has about 100 residues at the N-terminus that are missing from the polypeptide specified by the homologous gene f413 (cardiolipin synthase B). The f413 protein catalyzes cardiolipin formation in vitro but not in vivo. Amino acid residues specified by the first 60 codons in cls are not essential for catalytic activity
additional information
construction of mclS knockout strains from wild-type Moraxella catarrhalis isolates O35E, O12E, and McGHS1 yielding isogenic mutant strains O35E.mclS, O12E.mclS, and McGHS1.mclS. Wild-type and mutant strains show no differences in growth behaviour
additional information
-
construction of mclS knockout strains from wild-type Moraxella catarrhalis isolates O35E, O12E, and McGHS1 yielding isogenic mutant strains O35E.mclS, O12E.mclS, and McGHS1.mclS. Wild-type and mutant strains show no differences in growth behaviour
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Davlieva, M.; Zhang, W.; Arias, C.A.; Shamoo, Y.
Biochemical characterization of cardiolipin synthase mutations associated with daptomycin resistance in enterococci
Antimicrob. Agents Chemother.
57
289-296
2012
Enterococcus faecalis, Enterococcus faecalis S613, Enterococcus faecium, Enterococcus faecium S447, Enterococcus faecium S613
brenda
Ragolia, L.; Tropp, B.E.
The effects of phosphoglycerides on Escherichia coli cardiolipin synthase
Biochim. Biophys. Acta
1214
323-332
1994
Escherichia coli
brenda
Guo, D.; Tropp, B.E.
A second Escherichia coli protein with CL synthase activity
Biochim. Biophys. Acta
1483
263-274
2000
Escherichia coli (P0A6H8), Escherichia coli (P0AA84), Escherichia coli
brenda
Quigley, B.R.; Tropp, B.E.
E. coli cardiolipin synthase: function of N-terminal conserved residues
Biochim. Biophys. Acta
1788
2107-2113
2009
Escherichia coli (P0A6H8), Escherichia coli
brenda
Burritt, M.F.; Henderson, T.O.
Properties of a membrane-bound cardiolipin synthetase from Lactobacillus plantarum
J. Bacteriol.
123
972-977
1975
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC 8014
brenda
Hiraoka, S.; Nukui, K.; Uetake, N.; Ohta, A.; Shibuya, I.
Amplification and substantial purification of cardiolipin synthase of Escherichia coli
J. Biochem.
110
443-449
1991
Escherichia coli (P0A6H8), Escherichia coli
brenda
Tan, B.K.; Bogdanov, M.; Zhao, J.; Dowhan, W.; Raetz, C.R.; Guan, Z.
Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates
Proc. Natl. Acad. Sci. USA
109
16504-16509
2012
Escherichia coli (P0A6H8), Escherichia coli (P0AA84), Escherichia coli
brenda
Hirschberg, C.B.; Kennedy, E.P.
Mechanism of the enzymatic synthesis of cardiolipin in Escherichia coli
Proc. Natl. Acad. Sci. USA
69
648-651
1972
Escherichia coli
brenda
Ohniwa, R.; Kitabayashi, K.; Morikawa, K.
Alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress
FEMS Microbiol. Lett.
338
141-146
2013
Staphylococcus aureus (A0A0H3JKV8), Staphylococcus aureus (P63801), Staphylococcus aureus, Staphylococcus aureus N315 (A0A0H3JKV8), Staphylococcus aureus N315 (P63801)
brenda
Buskirk, S.W.; Lafontaine, E.R.
Moraxella catarrhalis expresses a cardiolipin synthase that impacts adherence to human epithelial cells
J. Bacteriol.
196
107-120
2014
Moraxella catarrhalis (R4V164), Moraxella catarrhalis
brenda
Liu, J.; Ryabichko, S.; Bogdanov, M.; Fackelmayer, O.J.; Dowhan, W.; Krulwich, T.A.
Cardiolipin is dispensable for oxidative phosphorylation and non-fermentative growth of alkaliphilic Bacillus pseudofirmus OF4
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Alkalihalophilus pseudofirmus (O66043), Alkalihalophilus pseudofirmus OF4 (O66043)
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Noguchi, F.; Tanifuji, G.; Brown, M.; Fujikura, K.; Takishita, K.
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Mol. Phylogenet. Evol.
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Wobblia lunata, Cafeteria sp., no activity in Developayella elegans, no activity in Cafeteria roenbergensis, Cantina marsupialis, Wobblia lunata NIES1015
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Bacillus subtilis, Bacillus subtilis 168
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Jeucken, A.; Helms, J.; Brouwers, J.
Cardiolipin synthases of Escherichia coli have phospholipid class specific phospholipase D activity dependent on endogenous and foreign phospholipids
Biochim. Biophys. Acta
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Escherichia coli (P0A6H8), Escherichia coli (P0AA84)
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Li, C.; Tan, B.K.; Zhao, J.; Guan, Z.
In vivo and in vitro synthesis of phosphatidylglycerol by an Escherichia coli cardiolipin synthase
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Escherichia coli (P0AA84), Escherichia coli
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Rossi, R.; Yum, L.; Agaisse, H.; Payne, S.
Cardiolipin synthesis and outer membrane localization are required for Shigella flexneri virulence
mBio
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Shigella flexneri (Q83RM8), Shigella flexneri
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Romantsov, T.; Gonzalez, K.; Sahtout, N.; Culham, D.E.; Coumoundouros, C.; Garner, J.; Kerr, C.H.; Chang, L.; Turner, R.J.; Wood, J.M.
Cardiolipin synthase A colocalizes with cardiolipin and osmosensing transporter ProP at the poles of Escherichia coli cells
Mol. Microbiol.
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623-638
2018
Escherichia coli
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