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Information on EC 2.3.2.3 - lysyltransferase
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EC Tree
2.3.2.3 lysyltransferaseSpecify your search results
Word Map
- 2.3.2.3
- aureus
- phospholipid
-
lysinylated
-
methicillin-resistant
-
daptomycin
-
lysyl-phosphatidylglycerol
-
aminoacylate
-
regulon
- phosphatidylethanolamine
-
teichoic
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
mprf protein, lpg synthetase, mprf flippase, lysx protein, lysyl-pg synthase, phosphatidylglycerol lysyltransferase, mprf2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LysX
lysyl-PG synthase
MprF
MprF protein
MprF2
-
the enzyme encompasses a lysyl-phosphatidylglycerol synthase and a lysyl-phosphatidylglycerol flippase domain
phosphatidylglycerol lysyltransferase
RimK-related lysine biosynthesis protein
Rv1640c
Tk0278
TkLysX
MprF
-
a membrane protein with both lysylphosphatidylglycerol synthase and flippase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysyl-tRNALys + phosphatidylglycerol = tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
aminoacyl group transfer
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-lysyl-tRNALys:phosphatidylglycerol 3-O-lysyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
37257-20-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
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
-
enzyme is involved in synthesis of lipids
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
Bacillus subtilis Marburg / DSM 10 / ATCC 6051
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enzyme is involved in synthesis of lipids
-
-
?
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
-
-
-
-
?
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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2'- (not 3'-) deoxy-analogue of phosphatidylglycerol can also act as L-lysyl-acceptor
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?
additional information
?
-
enzyme LysX from Thermococcus kodakarensis catalyzes the conjugation of enzyme LysW with either alpha-aminoadipate (AAA) or glutamate
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-
-
additional information
?
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the enzyme LysX also forms LysW-gamma-(alpha-aminoadipate) (LysW-gamma-AAA) from alpha-amino adipate (AAA) and glutamate as substrates and ligates both compounds with TK0279, the amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW
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-
-
additional information
?
-
enzyme LysX from Thermococcus kodakarensis catalyzes the conjugation of enzyme LysW with either alpha-aminoadipate (AAA) or glutamate
-
-
-
additional information
?
-
the enzyme LysX also forms LysW-gamma-(alpha-aminoadipate) (LysW-gamma-AAA) from alpha-amino adipate (AAA) and glutamate as substrates and ligates both compounds with TK0279, the amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW
-
-
-
additional information
?
-
enzyme LysX from Thermococcus kodakarensis catalyzes the conjugation of enzyme LysW with either alpha-aminoadipate (AAA) or glutamate
-
-
-
additional information
?
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the enzyme LysX also forms LysW-gamma-(alpha-aminoadipate) (LysW-gamma-AAA) from alpha-amino adipate (AAA) and glutamate as substrates and ligates both compounds with TK0279, the amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
-
-
-
?
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
-
enzyme is involved in synthesis of lipids
-
-
?
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
Bacillus subtilis Marburg / DSM 10 / ATCC 6051
-
enzyme is involved in synthesis of lipids
-
-
?
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
-
-
-
?
additional information
?
-
enzyme LysX from Thermococcus kodakarensis catalyzes the conjugation of enzyme LysW with either alpha-aminoadipate (AAA) or glutamate
-
-
-
additional information
?
-
enzyme LysX from Thermococcus kodakarensis catalyzes the conjugation of enzyme LysW with either alpha-aminoadipate (AAA) or glutamate
-
-
-
additional information
?
-
enzyme LysX from Thermococcus kodakarensis catalyzes the conjugation of enzyme LysW with either alpha-aminoadipate (AAA) or glutamate
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
2 magnesium atoms are located in the active site of the enzyme
phosphate
1 phosphate is located in the active site of the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
anionic surfactant, e.g. sodium-salt of a fatty acid, and high ionic strength lead to activation
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Pyrococcus kodakaraensis strain KOD1
UniProt
brenda
i.e. Pyrococcus kodakaraensis strain KOD1
UniProt
brenda
diverse clinical isolates from China
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the lysX gene is differentially expressed among Mycobacterium tuberculosis strains 37 (strains H37Rv, H37Ra, Beijing, Beijing4P, MDR, and 5186)
brenda
additional information
-
the lysX gene is differentially expressed among Mycobacterium tuberculosis strains 37 (strains H37Rv, H37Ra, Beijing, Beijing4P, MDR, and 5186)
-
brenda
additional information
-
the lysX gene is differentially expressed among Mycobacterium tuberculosis strains 37 (strains H37Rv, H37Ra, Beijing, Beijing4P, MDR, and 5186)
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
according to the presence of IS6110 insertion in the NTF region, the Beijing genotype is currently divided into two subtypes. The ancient subtype is characterized with the intact NTF region, whereas modern subtype strains demonstrate the presentation of IS6110 insertion in the NTF region. The latter subtype strains can also be discriminated by the polymorphisms of mutT genes. Modern subtype is designated to Beijing monophyletic groups 3 (Bj-MG3), whereas ancient subtype is further subdivided into Bj-MG1 and Bj-MG2 based on the RD181 deletion. The strains of modern subtype constitute the majority of Beijing genotype in most regions and demonstrate an increased virulent phenotype
evolution
the enzyme belongs to the LysX family of enzymes. Analysis of the mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities, overview. Substrate recognition mechanism in LysX family proteins. The lysX homologues in the lysine biosynthetic gene cluster encode enzymes that possess the signature motif (Tyr175, Ile185, Thr196, and Asn250-Ala251) for the LysX/ArgX bifunctional enzyme
evolution
-
the enzyme belongs to the LysX family of enzymes. Analysis of the mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities, overview. Substrate recognition mechanism in LysX family proteins. The lysX homologues in the lysine biosynthetic gene cluster encode enzymes that possess the signature motif (Tyr175, Ile185, Thr196, and Asn250-Ala251) for the LysX/ArgX bifunctional enzyme
-
evolution
-
according to the presence of IS6110 insertion in the NTF region, the Beijing genotype is currently divided into two subtypes. The ancient subtype is characterized with the intact NTF region, whereas modern subtype strains demonstrate the presentation of IS6110 insertion in the NTF region. The latter subtype strains can also be discriminated by the polymorphisms of mutT genes. Modern subtype is designated to Beijing monophyletic groups 3 (Bj-MG3), whereas ancient subtype is further subdivided into Bj-MG1 and Bj-MG2 based on the RD181 deletion. The strains of modern subtype constitute the majority of Beijing genotype in most regions and demonstrate an increased virulent phenotype
-
evolution
-
the enzyme belongs to the LysX family of enzymes. Analysis of the mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities, overview. Substrate recognition mechanism in LysX family proteins. The lysX homologues in the lysine biosynthetic gene cluster encode enzymes that possess the signature motif (Tyr175, Ile185, Thr196, and Asn250-Ala251) for the LysX/ArgX bifunctional enzyme
-
evolution
-
according to the presence of IS6110 insertion in the NTF region, the Beijing genotype is currently divided into two subtypes. The ancient subtype is characterized with the intact NTF region, whereas modern subtype strains demonstrate the presentation of IS6110 insertion in the NTF region. The latter subtype strains can also be discriminated by the polymorphisms of mutT genes. Modern subtype is designated to Beijing monophyletic groups 3 (Bj-MG3), whereas ancient subtype is further subdivided into Bj-MG1 and Bj-MG2 based on the RD181 deletion. The strains of modern subtype constitute the majority of Beijing genotype in most regions and demonstrate an increased virulent phenotype
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malfunction
-
a MprF knockout mutant demonstrates a substantial increase in the phosphatidylglycerol:lysylphosphatidylglycerol ratio of the membrane
malfunction
a Mycobacterium avium lysX mutant strain undergoes a transition in phenotype by switching the carbon metabolism to beta-oxidation of fatty acids, along with accumulation of lipid inclusions. Proteins associated with intracellular survival are upregulated in the lysX mutant, even during extracellular growth, preparing bacteria for the conditions occurring inside host cells. In line with this, the lysX mutant exhibits enhanced intracellular growth in human-blood-derived monocytes
malfunction
-
gain-of-function mutations in the phospholipid flippase MprF confer specific daptomycin resistance, although the T345A mutation does not alter lysyl-phosphatidylglycerol (LysPG) synthesis, LysPG translocation, or the Staphylococcus aureus cell surface charge. MprF-mediated DAP-resistance relies on a functional flippase domain and is restricted to daptomycin and a related cyclic lipopeptide antibiotic, friulimicin B. Daptomycin-resistant (DAP-R) Staphylococcus aureus mutants emerge during therapy, featuring isolates which in most cases possess point mutations in the mprF gene. T345A is a naturally occuring single nucleotide polymorphism (SNP) that can reproducibly cause daptomycin resistance, the mutation leads to weakened intramolecular domain interactions of MprF, suggesting that daptomycin and friulimicin resistance-conferring mutations may alter the substrate range of the MprF flippase to directly translocate these lipopeptide antibiotics or other membrane components with crucial roles in the activity of these antimicrobials
malfunction
identification of lysX mutants, Beijing and modern Beijing strains, genotyping, overview. Beijing family is a genotype of Mycobacterium tuberculosis that is disseminated worldwide predominating throughout East Asia, the former Soviet Union and South Africa. This family has a common spoligotype signature and lack of the region of difference (RD) 105. Clinical and epidemiological studies demonstrate that Beijing genotype strains are associated with high levels of bacterial resistance to drugs and enhanced ability to cause disease, contributing to increased transmissibility and rapid progression from infection to active disease. Evaluation of the virulence of Beijing genotype strains shows a wide range of virulence phenotypes
malfunction
-
a Mycobacterium avium lysX mutant strain undergoes a transition in phenotype by switching the carbon metabolism to beta-oxidation of fatty acids, along with accumulation of lipid inclusions. Proteins associated with intracellular survival are upregulated in the lysX mutant, even during extracellular growth, preparing bacteria for the conditions occurring inside host cells. In line with this, the lysX mutant exhibits enhanced intracellular growth in human-blood-derived monocytes
-
malfunction
-
identification of lysX mutants, Beijing and modern Beijing strains, genotyping, overview. Beijing family is a genotype of Mycobacterium tuberculosis that is disseminated worldwide predominating throughout East Asia, the former Soviet Union and South Africa. This family has a common spoligotype signature and lack of the region of difference (RD) 105. Clinical and epidemiological studies demonstrate that Beijing genotype strains are associated with high levels of bacterial resistance to drugs and enhanced ability to cause disease, contributing to increased transmissibility and rapid progression from infection to active disease. Evaluation of the virulence of Beijing genotype strains shows a wide range of virulence phenotypes
-
malfunction
-
identification of lysX mutants, Beijing and modern Beijing strains, genotyping, overview. Beijing family is a genotype of Mycobacterium tuberculosis that is disseminated worldwide predominating throughout East Asia, the former Soviet Union and South Africa. This family has a common spoligotype signature and lack of the region of difference (RD) 105. Clinical and epidemiological studies demonstrate that Beijing genotype strains are associated with high levels of bacterial resistance to drugs and enhanced ability to cause disease, contributing to increased transmissibility and rapid progression from infection to active disease. Evaluation of the virulence of Beijing genotype strains shows a wide range of virulence phenotypes
-
metabolism
-
the C-terminal domain of the enzyme is responsible for the synthesis of lysylphosphatidylglycerol
metabolism
significance of lysX in the metabolism and virulence of the environmental pathogen Mycobacterium avium hominissuis
metabolism
the enzyme LysX is involved in the lysine biosynthesis pathway. The conversion from alpha-aminoadipate (AAA) to lysine, is accomplished by five enzymes: LysX, LysZ, LysY, LysJ, and LysK, using the amino group carrier protein LysW. The alpha-amino group of AAA is modified with LysW by LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW. LysW-gamma-AAA thus synthesized is then transferred to subsequent biosynthetic enzymes to be converted to LysW-gamma-lysine by phosphorylation, reduction, and amination steps. In the final step, LysW-gamma-lysine is recognized by LysK, a carboxypeptidase, resulting in the release of lysine. LysW contains many acidic amino acid residues for electrostatic interactions with each enzyme, and, thus, functions as an amino group carrier protein for efficient lysine biosynthesis
metabolism
-
the enzyme LysX is involved in the lysine biosynthesis pathway. The conversion from alpha-aminoadipate (AAA) to lysine, is accomplished by five enzymes: LysX, LysZ, LysY, LysJ, and LysK, using the amino group carrier protein LysW. The alpha-amino group of AAA is modified with LysW by LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW. LysW-gamma-AAA thus synthesized is then transferred to subsequent biosynthetic enzymes to be converted to LysW-gamma-lysine by phosphorylation, reduction, and amination steps. In the final step, LysW-gamma-lysine is recognized by LysK, a carboxypeptidase, resulting in the release of lysine. LysW contains many acidic amino acid residues for electrostatic interactions with each enzyme, and, thus, functions as an amino group carrier protein for efficient lysine biosynthesis
-
metabolism
-
significance of lysX in the metabolism and virulence of the environmental pathogen Mycobacterium avium hominissuis
-
metabolism
-
the enzyme LysX is involved in the lysine biosynthesis pathway. The conversion from alpha-aminoadipate (AAA) to lysine, is accomplished by five enzymes: LysX, LysZ, LysY, LysJ, and LysK, using the amino group carrier protein LysW. The alpha-amino group of AAA is modified with LysW by LysX, forming an isopeptide bond between the alpha-amino group of AAA and gamma-carboxyl group of the glutamate residue at the C terminus of LysW. LysW-gamma-AAA thus synthesized is then transferred to subsequent biosynthetic enzymes to be converted to LysW-gamma-lysine by phosphorylation, reduction, and amination steps. In the final step, LysW-gamma-lysine is recognized by LysK, a carboxypeptidase, resulting in the release of lysine. LysW contains many acidic amino acid residues for electrostatic interactions with each enzyme, and, thus, functions as an amino group carrier protein for efficient lysine biosynthesis
-
physiological function
-
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
-
enzyme MprF is a bifunctional bacterial resistance protein that synthesizes the positively charged lipid lysyl-phosphatidylglycerol (LysPG) and translocates it subsequently from the inner membrane leaflet to the outer membrane leaflet. MprF links lysine to negatively charged phosphatidylglycerol (PG) and translocates the resulting positively charged lysyl-PG (LysPG) to the outer leaflet of the cytoplasmic membrane (CM), resulting in electrostatic repulsion of cationic antimicrobial peptides (CAMPs), including human defensins and bacterial lantibiotics
physiological function
in comparison with Gram-negative bacteria, Gram-positive bacteria in general have much less zwitterionic phosphatidylethanolamine. They are known for producing aminoacylated phosphatidylglycerol (PG), especially positively charged L-lysyl-PG, which is catalyzed by lysyl-PG synthase MprF. Enzyme MprF appears to have a broad range of specificity for L-aminoacyl transfer RNAs. Lipids from Bacillus subtilis are extremely abundant in lysyl-PG and somewhat rich in alanyl-PG. It appears that N-succinylation of lipids in Bacillus subtilis strain 168 is specific to lysyl-PG but not alanyl-PG
physiological function
lysyl-phosphatidylglycerol is one of the components of the mycobacterial membrane that contributes to the resistance to cationic antimicrobial peptides, a host-induced frontline defense against invading pathogens. Its production is catalyzed by LysX, a bifunctional protein with lysyl transferase and lysyl transfer RNA synthetase activity
physiological function
Mycobacterium tuberculosis (Mtb) has developed mechanisms to avoid antimicrobial peptides (AMPs) activity, for instance lysX adds lysine residues to surface phospholipids changing their net charge, leading to the repelling of the AMPs. In the presence of AMPs, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. Ability of Mtb to replicate intracellularly is directly correlated to the level of lysX expression showing that the amount of lysX produced by the bacterial cell is an important variable for the modulation of Mtb virulence. Gene expression of AMPs during in vivo infection of BALB/c mice, overview
physiological function
the lysine connection with phosphatidylglycerol (PG) may alter the Mycobacterium tuberculosis surface charge, and consequently decrease the bacterial vulnerability to antimicrobial action of the immune cells. PG lysinylation plays an important role in maintaining an optimal membrane potential for Mycobacterium tuberculosis and promoting the survival of pathogen upon infection
physiological function
-
in comparison with Gram-negative bacteria, Gram-positive bacteria in general have much less zwitterionic phosphatidylethanolamine. They are known for producing aminoacylated phosphatidylglycerol (PG), especially positively charged L-lysyl-PG, which is catalyzed by lysyl-PG synthase MprF. Enzyme MprF appears to have a broad range of specificity for L-aminoacyl transfer RNAs. Lipids from Bacillus subtilis are extremely abundant in lysyl-PG and somewhat rich in alanyl-PG. It appears that N-succinylation of lipids in Bacillus subtilis strain 168 is specific to lysyl-PG but not alanyl-PG
-
physiological function
-
lysyl-phosphatidylglycerol is one of the components of the mycobacterial membrane that contributes to the resistance to cationic antimicrobial peptides, a host-induced frontline defense against invading pathogens. Its production is catalyzed by LysX, a bifunctional protein with lysyl transferase and lysyl transfer RNA synthetase activity
-
physiological function
-
the lysine connection with phosphatidylglycerol (PG) may alter the Mycobacterium tuberculosis surface charge, and consequently decrease the bacterial vulnerability to antimicrobial action of the immune cells. PG lysinylation plays an important role in maintaining an optimal membrane potential for Mycobacterium tuberculosis and promoting the survival of pathogen upon infection
-
physiological function
-
Mycobacterium tuberculosis (Mtb) has developed mechanisms to avoid antimicrobial peptides (AMPs) activity, for instance lysX adds lysine residues to surface phospholipids changing their net charge, leading to the repelling of the AMPs. In the presence of AMPs, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. Ability of Mtb to replicate intracellularly is directly correlated to the level of lysX expression showing that the amount of lysX produced by the bacterial cell is an important variable for the modulation of Mtb virulence. Gene expression of AMPs during in vivo infection of BALB/c mice, overview
-
physiological function
-
the lysine connection with phosphatidylglycerol (PG) may alter the Mycobacterium tuberculosis surface charge, and consequently decrease the bacterial vulnerability to antimicrobial action of the immune cells. PG lysinylation plays an important role in maintaining an optimal membrane potential for Mycobacterium tuberculosis and promoting the survival of pathogen upon infection
-
physiological function
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Mycobacterium tuberculosis (Mtb) has developed mechanisms to avoid antimicrobial peptides (AMPs) activity, for instance lysX adds lysine residues to surface phospholipids changing their net charge, leading to the repelling of the AMPs. In the presence of AMPs, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. Ability of Mtb to replicate intracellularly is directly correlated to the level of lysX expression showing that the amount of lysX produced by the bacterial cell is an important variable for the modulation of Mtb virulence. Gene expression of AMPs during in vivo infection of BALB/c mice, overview
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additional information
crystal structure analysis revealing the mechanism of substrate recognition of alpha-aminoadipate substrate by LysX and structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis Active site structure and reaction mechanism, structure-function analysis, detailed overview. ADP, a phosphate ion, two magnesium atoms, and the C-terminus of TkLysW-gamma-AAA are located in the active site of TkLysX
additional information
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crystal structure analysis revealing the mechanism of substrate recognition of alpha-aminoadipate substrate by LysX and structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis Active site structure and reaction mechanism, structure-function analysis, detailed overview. ADP, a phosphate ion, two magnesium atoms, and the C-terminus of TkLysW-gamma-AAA are located in the active site of TkLysX
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additional information
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crystal structure analysis revealing the mechanism of substrate recognition of alpha-aminoadipate substrate by LysX and structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis Active site structure and reaction mechanism, structure-function analysis, detailed overview. ADP, a phosphate ion, two magnesium atoms, and the C-terminus of TkLysW-gamma-AAA are located in the active site of TkLysX
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Show AA Sequence and Transmembrane Helices (8561 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
67000
theoretical, MprF(-8) mutant, truncated protein consisting of residues 274-840
67000
theoretical, MprF(-C) mutant, truncated protein consisting of residues 1-586
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with product LysW-gamma-AAA, hanging drop vapor diffusion method, method screening and subsequent optimization, mixing of 7.5 mg/ml enzyme, 2.5 mg/ml TkLysW, 10 mM AMP-PNP, 10 mM alpha-aminoadipate (AAA), or 50 mM glutamate, and 10 mM MgSO4 with crystallization solution containing 20% v/v 2-methyl-2,4-pentanediol, 6.6% w/v PEG 3350, 0.066 M imidazole, pH 6.5, and 0.132 M ammonium sulfate, 20°C, X-ray diffraction stucture determination and analysis at 2.18 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I701T
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
I420N
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naturally occuring single nucleotide polymorphism (SNP) that does not alter daptomycin resistance and the lysyl-phosphatidylglycerol synthesizing activity
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
L826F
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naturally occuring single nucleotide polymorphism (SNP) that does not alter daptomycin resistance and the lysyl-phosphatidylglycerol synthesizing activity
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
P314L
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naturally occuring single nucleotide polymorphism (SNP) that does not alter daptomycin resistance, but slightly enhances the lysyl-phosphatidylglycerol synthesizing activity
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
S295L
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naturally occuring single nucleotide polymorphism (SNP) that causes a slight daptomycin resistance and slightly enhances the lysyl-phosphatidylglycerol synthesizing activity
S337L
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naturally occuring single nucleotide polymorphism (SNP) that does not alter daptomycin resistance and the lysyl-phosphatidylglycerol synthesizing activity
T345A
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naturally occuring single nucleotide polymorphism (SNP) that can reproducibly cause strong, clinically relevant daptomycin resistance, the mutation leads to weakened intramolecular domain interactions of MprF, suggesting that daptomycin and friulimicin resistance-conferring mutations may alter the substrate range of the MprF flippase to directly translocate these lipopeptide antibiotics or other membrane components with crucial roles in the activity of these antimicrobials. MprF point mutation T345A causes cross-resistance only to daptomycin and the related lipopeptide antibiotic friulimicin B
V351E
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naturally occuring single nucleotide polymorphism (SNP) that causes a strong, clinically relevant daptomycin resistance and slightly reduced lysyl-phosphatidylglycerol synthesizing activity
additional information
I701T
naturally occuring mutation in gene lysX, involved in Bejing genotype, the Ile701Thr mutation can affect the protein function
I701T
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naturally occuring mutation in gene lysX, involved in Bejing genotype, the Ile701Thr mutation can affect the protein function
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I701T
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naturally occuring mutation in gene lysX, involved in Bejing genotype, the Ile701Thr mutation can affect the protein function
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additional information
genotyping of gene lysX, Beijing and modern Beijing strains are idetified. Mutations at codon 995 (Pro CCG to Pro CCA) and 701 (Ile ATT to Thr ACT) in lysX gene (Rv1640c), are specific markers for Beijing and modern Beijing strains, respectively. Determination of a mutation at codon 809 (CGA to CGG), and a mutation at codon 885 (ATC to ATT). Beijing and modern Beijing strains are observed and used to develop a MAS-PCR method for identifying isolates of these genotypes
additional information
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genotyping of gene lysX, Beijing and modern Beijing strains are idetified. Mutations at codon 995 (Pro CCG to Pro CCA) and 701 (Ile ATT to Thr ACT) in lysX gene (Rv1640c), are specific markers for Beijing and modern Beijing strains, respectively. Determination of a mutation at codon 809 (CGA to CGG), and a mutation at codon 885 (ATC to ATT). Beijing and modern Beijing strains are observed and used to develop a MAS-PCR method for identifying isolates of these genotypes
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additional information
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genotyping of gene lysX, Beijing and modern Beijing strains are idetified. Mutations at codon 995 (Pro CCG to Pro CCA) and 701 (Ile ATT to Thr ACT) in lysX gene (Rv1640c), are specific markers for Beijing and modern Beijing strains, respectively. Determination of a mutation at codon 809 (CGA to CGG), and a mutation at codon 885 (ATC to ATT). Beijing and modern Beijing strains are observed and used to develop a MAS-PCR method for identifying isolates of these genotypes
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