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Information on EC 2.3.2.3 - lysyltransferase for references in articles please use BRENDA:EC2.3.2.3Word Map on EC 2.3.2.3
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The enzyme appears in viruses and cellular organisms
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L-lysyl-tRNALys + phosphatidylglycerol = tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
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aminoacyl group transfer
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aminoacyl group transfer
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aminoacyl group transfer
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aminoacyl group transfer
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L-lysyl-tRNALys:phosphatidylglycerol 3-O-lysyltransferase
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Lys-tRNA(Lys) phosphatidylglycerol transferase
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lysophosphatidylglycerol synthetase
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lysyl-transferase-lysyl-tRNA synthetase
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MprF2
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the enzyme encompasses a lysyl-phosphatidylglycerol synthase and a lysyl-phosphatidylglycerol flippase domain
multiple peptide resistance factor protein
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MprF
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MprF
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a membrane protein with both lysylphosphatidylglycerol synthase and flippase activities
MprF protein
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UniProt
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malfunction
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a MprF knockout mutant demonstrates a substantial increase in the phosphatidylglycerol:lysylphosphatidylglycerol ratio of the membrane
metabolism
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the C-terminal domain of the enzyme is responsible for the synthesis of lysylphosphatidylglycerol
physiological function
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MprF2-mediated lysyl-phosphatidylglycerol production confers cationic antimicrobial peptide susceptibility with 6fold decreased daptomycin susceptibility or 4fold decreased gallidermin and nisin susceptibility compared to the Staphylococcus aureus mprF deletion mutant
physiological function
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the mprFgene confers daptomycin resistance
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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enzyme is involved in synthesis of lipids
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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enzyme is involved in synthesis of lipids
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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2'- (not 3'-) deoxy-analogue of phosphatidylglycerol can also act as L-lysyl-acceptor
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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enzyme is involved in synthesis of lipids
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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enzyme is involved in synthesis of lipids
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
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L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
Q2G2M2
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additional information
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anionic surfactant, e.g. sodium-salt of a fatty acid, and high ionic strength lead to activation
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0.056
phosphatidylglycerol
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0.00000072
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supernatant 10000 x g
0.00000143
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cell crude extract
0.00000326
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membrane fraction
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septal membranes
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septal membranes
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an integral membrane protein
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Q65MA9
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46);
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39000
theoretical, MprF(-14) mutant, truncated protein consisting of residues 510-840
48000
theoretical, MprF(-12) mutant, truncated protein consisting of residues 437-840
56000
theoretical, MprF(-10) mutant, truncated protein consisting of residues 363-840
67000
theoretical, MprF(-8) mutant, truncated protein consisting of residues 274-840; theoretical, MprF(-C) mutant, truncated protein consisting of residues 1-586
75000
theoretical, MprF(-6) mutant, truncated protein consisting of residues 219-840
80000
theoretical, MprF(-4) mutant, truncated protein consisting of residues 157-840
88000
theoretical, MprF(-2) mutant, truncated protein consisting of residues 84-840
97000
theoretical, MprF wild-type
100000
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determined by SDS-PAGE
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-20°C, membrane-bound enzyme extracted with organic solvents, t1/2: 3-5 days
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-20°C, native membrane-bound enzyme, several weeks
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membrane fractions are prepared by differential centrifugation
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expressed in a Staphylococcus aureus mprF deletion mutant
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expression in Escherichia coli
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for the construction of lysX deletion and complemented derivative Mycobacterium tuberculosis strains
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into the vector pET33b for expression in Escherichia coli Rosetta2 DE3, C41 and C43 cells
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D546A
MprF(-8) mutant, replacement results in slightly reduced production of lysyl-phosphatidylglycerol, same result is obtained when the mutation is introduced into the full-length MprF protein
D731A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
E624A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
E685A
MprF(-8) mutant, replacement results in strongly reduced production of lysyl-phosphatidylglycerol, same result is obtained when the mutation is introduced into the full-length MprF protein
K547A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
K621A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
K806A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
MprF(-10)
mutant, truncated protein consisting of residues 363-840
MprF(-12)
mutant, truncated protein consisting of residues 437-840
MprF(-14)
mutant, truncated protein consisting of residues 510-840
MprF(-2)
mutant, truncated protein consisting of residues 84-840
MprF(-4)
mutant, truncated protein consisting of residues 157-840
MprF(-6)
mutant, truncated protein consisting of residues 219-840
MprF(-8)
mutant, truncated protein consisting of residues 274-840
MprF(-C)
mutant, truncated protein consisting of residues 1-586
R734A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
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analysis
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a method to obtain a stable enriched membrane fraction containing MprF, and the techniques necessary to quantitatively monitor its activity in vitro and in vivo is reported
medicine
MprF could be a target for new anti-virulence drugs
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Lennarz, W.J.; Bonsen, P.P.M.; Van Deenen, L.L.M.
Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol
Biochemistry
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2307-2312
1967
Staphylococcus aureus
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Nishibori, A.; Kusaka, J.; Hara, H.; Umeda, M.; Matsumoto, K.
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
J. Bacteriol.
187
2163-2174
2005
Bacillus subtilis
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Oku, Y.; Kurokawa, K.; Ichihashi, N.; Sekimizu, K.
Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol
Microbiology
150
45-51
2004
Staphylococcus aureus
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Roy, H.; Ibba, M.
Monitoring Lys-tRNA(Lys) phosphatidylglycerol transferase activity
Methods
44
164-169
2008
Bacillus subtilis
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Maloney, E.; Stankowska, D.; Zhang, J.; Fol, M.; Cheng, Q.J.; Lun, S.; Bishai, W.R.; Rajagopalan, M.; Chatterjee, D.; Madiraju, M.V.
The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides
PLoS Pathog.
5
e1000534
2009
Mycobacterium tuberculosis
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Ernst, C.M.; Staubitz, P.; Mishra, N.N.; Yang, S.J.; Hornig, G.; Kalbacher, H.; Bayer, A.S.; Kraus, D.; Peschel, A.
The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion
PLoS Pathog.
5
e1000660
2009
Staphylococcus aureus (Q2G2M2)
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Slavetinsky, C.J.; Peschel, A.; Ernst, C.M.
Alanyl-phosphatidylglycerol and lysyl-phosphatidylglycerol are translocated by the same MprF flippases and have similar capacities to protect against the antibiotic daptomycin in Staphylococcus aureus
Antimicrob. Agents Chemother.
56
3492-3497
2012
Clostridium perfringens
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Rubio, A.; Moore, J.; Varoglu, M.; Conrad, M.; Chu, M.; Shaw, W.; Silverman, J.A.
LC-MS/MS characterization of phospholipid content in daptomycin-susceptible and -resistant isolates of Staphylococcus aureus with mutations in mprF
Mol. Membr. Biol.
29
1-8
2012
Staphylococcus aureus
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