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IUBMB Comments The enzyme is a dimeric complex consisting of an ATP-binding protein (FakA) and a fatty acid-binding protein (FakB). The first step in the reaction is the binding of FakB (with a bound fatty acid) to FakA. The fatty acid bound to FakB is then phosphorylated by FakA, and the fatty acyl phosphate-bound FakB is released from the complex. In the presence of an exchangeable fatty acid pool in the cell membrane, the fatty acy phosphate bound to FakB exchanges with a fatty acid to regenerate the substrate for FakA. The system is widespread in Gram-positive bacteria, with most strains possessing a single FakA protein along with multiple FakB subunits that differ in their specificity towards fatty acid substrates.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
a fatty acyl phosphate
Synonyms
fa kinase, fatty acid kinase, fakb2, fakab,
more
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branched-chain fatty acid kinase
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short chain fatty acid kinase
acetate kinase
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ACK
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FA kinase
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FAK
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fakA
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fakA
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FakA provides the ATP binding domain and interacts with two distinct FakB protein to produce acyl phosphate
fakA
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gene name, originally named vfrB
fakA
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the ATP-binding protein phosphorylates the fatty acid bound to FakB
fakA
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FakA provides the ATP binding domain and interacts with two distinct FakB protein to produce acyl phosphate
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FakAB
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fakB
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fakB
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FakB is a fatty acid binding protein. FakB1 selectively binds saturated fatty acids whereas FakB2 prefers unsaturated fatty acids
fakB
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FakB is a fatty acid binding protein. FakB1 selectively binds saturated fatty acids whereas FakB2 prefers unsaturated fatty acids
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fatty acid kinase A
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fatty acid kinase A
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short chain fatty acid kinase
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short chain fatty acid kinase
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VfrB
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formerly named
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a fatty acyl phosphate-[fatty acid-binding protein] + a fatty acid = a fatty acyl phosphate + a fatty acid-[fatty acid-binding protein]
(1b)
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ATP + a fatty acid = ADP + a fatty acyl phosphate
overall reaction
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ATP + a fatty acid-[fatty acid-binding protein] = ADP + a fatty acyl phosphate-[fatty acid-binding protein]
(1a)
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ATP:fatty acid 1-phosphotransferase
The enzyme is a dimeric complex consisting of an ATP-binding protein (FakA) and a fatty acid-binding protein (FakB). The first step in the reaction is the binding of FakB (with a bound fatty acid) to FakA. The fatty acid bound to FakB is then phosphorylated by FakA, and the fatty acyl phosphate-bound FakB is released from the complex. In the presence of an exchangeable fatty acid pool in the cell membrane, the fatty acy phosphate bound to FakB exchanges with a fatty acid to regenerate the substrate for FakA. The system is widespread in Gram-positive bacteria, with most strains possessing a single FakA protein along with multiple FakB subunits that differ in their specificity towards fatty acid substrates.
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ATP + 2-methylbutyrate
ADP + 2-methylbutyryl phosphate
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-
-
-
?
ATP + acetate
ADP + acetyl phosphate
ATP + butyrate
ADP + butyryl phosphate
ATP + heptanoate
ADP + heptanoyl phosphate
22% activity compared to acetate
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-
?
ATP + hexanoate
ADP + hexanoyl phosphate
38% activity compared to acetate
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-
?
ATP + isobutyrate
ADP + isobutyryl phosphate
ATP + isovalerate
ADP + isovaleryl phosphate
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-
-
-
?
ATP + myristic acid
ADP + myristyl phosphate
ATP + octanoate
ADP + octanoyl phosphate
8.4% activity compared to acetate
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-
?
ATP + oleate
ADP + oleyl phosphate
ATP + oleic acid
ADP + oleyl phosphate
ATP + propionate
ADP + propionyl phosphate
ATP + valerate
ADP + valeryl phosphate
CTP + isobutyrate
CDP + isobutyryl phosphate
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103% activity compared to ATP
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?
GTP + isobutyrate
GDP + isobutyryl phosphate
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70% activity compared to ATP
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?
ITP + isobutyrate
IDP + isobutyryl phosphate
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68% activity compared to ATP
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?
UTP + isobutyrate
UDP + isobutyryl phosphate
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78% activity compared to ATP
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?
additional information
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ATP + acetate
ADP + acetyl phosphate
100% activity
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?
ATP + acetate
ADP + acetyl phosphate
100% activity
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?
ATP + butyrate
ADP + butyryl phosphate
59.5% activity compared to acetate
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?
ATP + butyrate
ADP + butyryl phosphate
59.5% activity compared to acetate
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?
ATP + butyrate
ADP + butyryl phosphate
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-
-
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?
ATP + isobutyrate
ADP + isobutyryl phosphate
26.7% activity compared to acetate
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?
ATP + isobutyrate
ADP + isobutyryl phosphate
26.7% activity compared to acetate
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?
ATP + isobutyrate
ADP + isobutyryl phosphate
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100% activity
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?
ATP + myristic acid
ADP + myristyl phosphate
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-
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?
ATP + myristic acid
ADP + myristyl phosphate
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?
ATP + oleate
ADP + oleyl phosphate
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?
ATP + oleate
ADP + oleyl phosphate
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?
ATP + oleate
ADP + oleyl phosphate
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?
ATP + oleic acid
ADP + oleyl phosphate
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?
ATP + oleic acid
ADP + oleyl phosphate
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-
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?
ATP + propionate
ADP + propionyl phosphate
93.3% activity compared to acetate
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?
ATP + propionate
ADP + propionyl phosphate
93.3% activity compared to acetate
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?
ATP + propionate
ADP + propionyl phosphate
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-
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?
ATP + valerate
ADP + valeryl phosphate
43.3% activity compared to acetate
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?
ATP + valerate
ADP + valeryl phosphate
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?
additional information
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the enzyme shows broad substrate specificity for primary fatty acids of varying lengths (C2-C8)
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additional information
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the enzyme shows broad substrate specificity for primary fatty acids of varying lengths (C2-C8)
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additional information
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the enzyme shows broad substrate specificity for primary fatty acids of varying lengths (C2-C8)
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additional information
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no activity with acetate
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additional information
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the enzyme does not phosphorylate SaeS or SaeR
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additional information
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the enzyme does not phosphorylate SaeS or SaeR
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ATP + oleic acid
ADP + oleyl phosphate
ATP + oleic acid
ADP + oleyl phosphate
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?
ATP + oleic acid
ADP + oleyl phosphate
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-
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?
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Mg2+
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96% activity in the presence of 4 mM Mg2+ as compared to Mn2+
Mg2+
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20 mM used in assay conditions
Mn2+
10 mM used in assay conditions. The enzyme exhibits about 25% higher specific activity with manganese as a cofactor compared to magnesium
Mn2+
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100% activity in the presence of 4 mM Mn2+
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Ca2+
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complete inhibition at 4 mM Ca2+
Co2+
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65% residual activity in the presence of 4 mM
Cu2+
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58% residual activity in the presence of 4 mM
K+
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complete inhibition at 4 mM K+
Na+
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complete inhibition at 4 mM Na+
Zn2+
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42% residual activity in the presence of 4 mM
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Blister
A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction.
Breast Neoplasms
Progesterone receptor enhances breast cancer cell motility and invasion via extranuclear activation of focal adhesion kinase.
Infections
Acyl-chain selectivity and physiological roles of Staphylococcus aureus fatty acid-binding proteins.
Infections
Staphylococcus aureus Fatty Acid Kinase FakA Modulates Pathogenesis during Skin Infection via Proteases.
Lung Neoplasms
Vimentin regulates lung cancer cell adhesion through a VAV2-Rac1 pathway to control focal adhesion kinase activity.
Neoplasms
Regulation of focal adhesion turnover by ErbB signalling in invasive breast cancer cells.
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10.8
2-methylbutyrate
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at pH 7.5 and 30°C
53.9
acetate
at pH 5.7 and 37°C
9.5
Isovalerate
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at pH 7.5 and 30°C
1.8
ATP
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with isobutyrate as cosubstrate, at pH 7.5 and 30°C
3.1
ATP
with acetate as cosubstrate, at pH 5.7 and 37°C
16.9
Butyrate
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at pH 7.5 and 30°C
24.5
Butyrate
at pH 5.7 and 37°C
4.3
Isobutyrate
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at pH 7.5 and 30°C
109
Isobutyrate
at pH 5.7 and 37°C
14.3
propionate
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at pH 7.5 and 30°C
25.8
propionate
at pH 5.7 and 37°C
12.5
valerate
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at pH 7.5 and 30°C
14.2
valerate
at pH 5.7 and 37°C
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177
acetate
at pH 5.7 and 37°C
250
ATP
with acetate as cosubstrate, at pH 5.7 and 37°C
118
Butyrate
at pH 5.7 and 37°C
65.4
Isobutyrate
at pH 5.7 and 37°C
172
propionate
at pH 5.7 and 37°C
80.2
valerate
at pH 5.7 and 37°C
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3.3
acetate
at pH 5.7 and 37°C
80.5
ATP
with acetate as cosubstrate, at pH 5.7 and 37°C
4.8
Butyrate
at pH 5.7 and 37°C
0.6
Isobutyrate
at pH 5.7 and 37°C
6.7
propionate
at pH 5.7 and 37°C
5.6
valerate
at pH 5.7 and 37°C
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0.031
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mutant enzyme T61A, at pH 7.5 and 37°C
0.034
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mutant enzyme S93A, at pH 7.5 and 37°C
0.053
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mutant enzyme H266A, at pH 7.5 and 37°C
0.497
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mutant enzyme R202A, at pH 7.5 and 37°C
54.5
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wild type enzyme, at pH 7.5 and 37°C
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6 - 8.5
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more than 80% activity between pH 6.0 and 8.5
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51
activity declines sharply at temperatures above 51°C, with 44% and 12% of activity remaining at 60°C and 67°C, respectively
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UniProt
brenda
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UniProt
brenda
spirochete MA-2
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brenda
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brenda
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brenda
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brenda
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malfunction
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a DELTAfakA mutant is hypervirulent during skin infection, and the hypervirulence is dependent on alpha-hemolysin
malfunction
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the absence of the enzyme leads to altered acetate metabolism and altered redox balance, as well as a change in intracellular amino acids
malfunction
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transductants mutated in fakA gene exhibit elevated biofilm formation
malfunction
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transductants mutated in fakA gene exhibit elevated biofilm formation
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malfunction
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a DELTAfakA mutant is hypervirulent during skin infection, and the hypervirulence is dependent on alpha-hemolysin
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metabolism
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the enzyme activates SaeRS-dependent virulence factor production by lowering inhibitory fatty acid levels. Thus, the enzyme plays a role in cellular lipid homeostasis by activating fatty acid for incorporation into phospholipid, and it indirectly regulates SaeRS signaling by maintaining a low intracellular fatty acid pool
metabolism
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the enzyme is important for maintaining the composition and properties of the phospholipid membrane in the presence of exogenous fatty acids, impacting overall cell physiology
metabolism
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the enzyme is specific for leucine, isoleucine, and valine fermentation
metabolism
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the enzyme is important for maintaining the composition and properties of the phospholipid membrane in the presence of exogenous fatty acids, impacting overall cell physiology
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metabolism
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the enzyme activates SaeRS-dependent virulence factor production by lowering inhibitory fatty acid levels. Thus, the enzyme plays a role in cellular lipid homeostasis by activating fatty acid for incorporation into phospholipid, and it indirectly regulates SaeRS signaling by maintaining a low intracellular fatty acid pool
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physiological function
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the enzyme is essential for phospholipid synthesis and also impacts the transcription of numerous virulence factors, as a negative regulator of biofilm formation in Staphylococcus aureus strain USA300
physiological function
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the enzyme modulates pathogenesis during skin infection via proteases SspAB and aureolysin
physiological function
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the enzyme plays a significant role in virulence factor regulation and skin infections. The enzyme is responsible for phosphorylating exogenous fatty acids and incorporating them into the Staphylococcus aureus phospholipid bilayer
physiological function
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the enzyme is essential for phospholipid synthesis and also impacts the transcription of numerous virulence factors, as a negative regulator of biofilm formation in Staphylococcus aureus strain USA300
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physiological function
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the enzyme modulates pathogenesis during skin infection via proteases SspAB and aureolysin
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Q3IYF1_CERS4
Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)
396
0
41860
TrEMBL
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240000
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FakA, gel filtration
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?
x * 47000, SDS-PAGE
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x * 47000, SDS-PAGE
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x * 35000, subunit FakB2, SDS-PAGE
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x * 66000, subunit FakA, SDS-PAGE
homodimer
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FakA, analytical ultracentrifugation
homodimer
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FakA, analytical ultracentrifugation
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subunit FakB2 bound to oleate, sitting drop vapor diffusion method, using 0.1 M citrate, pH 5.5, 20% (w/v) PEG 3000
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H266A
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the 1000fold less active mutant shows a reduced thermal denaturation temperature compared to the wild type enzyme
S93A
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the 1000fold less active mutant shows a reduced thermal denaturation temperature compared to the wild type enzyme
T61A
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the 1000fold less active mutant shows a reduced thermal denaturation temperature compared to the wild type enzyme
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45 - 60
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25% loss of activity after 30 min at 45°C, complete loss of activity after 30 min at 60°C
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-50°C, crude cell extract, 2 months, no loss of activity
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5°C, purified enzyme, 48 h, no loss of activity
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DEAE-cellulose column chromatography and Sephacryl S-300 gel filtration
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HisTrap column chromatography
Ni-NTA column chromatography
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Ni-NTA column chromatography and Superdex 75 gel filtration
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) Rosetta-2 cells
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Bachochin, M.J.; Van Allen, M.; Barber, R.D.
Characterization of a Rhodobacter sphaeroides primary fatty acid kinase
Arch. Microbiol.
203
861-864
2021
Cereibacter sphaeroides (Q3IYF1), Cereibacter sphaeroides, Cereibacter sphaeroides ATH 2.4.1 (Q3IYF1)
brenda
Sabirova, J.S.; Hernalsteens, J.P.; De Backer, S.; Xavier, B.B.; Moons, P.; Turlej-Rogacka, A.; De Greve, H.; Goossens, H.; Malhotra-Kumar, S.
Fatty acid kinase A is an important determinant of biofilm formation in Staphylococcus aureus USA300
BMC Genomics
16
861
2015
Staphylococcus aureus, Staphylococcus aureus USA300
brenda
Ridder, M.J.; Daly, S.M.; Triplett, K.D.; Seawell, N.A.; Hall, P.R.; Bose, J.L.
Staphylococcus aureus fatty acid kinase FakA modulates pathogenesis during skin infection via proteases
Infect. Immun.
88
e00163-20
2020
Staphylococcus aureus, Staphylococcus aureus USA300
brenda
Harwood, C.S.; Canale-Parola, E.
Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a spirochete
J. Bacteriol.
152
246-254
1982
Spirochaetales
brenda
DeMars, Z.; Bose, J.L.
Redirection of metabolism in response to fatty acid kinase in Staphylococcus aureus
J. Bacteriol.
200
e00345-18
2018
Staphylococcus aureus
brenda
DeMars, Z.; Singh, V.K.; Bose, J.L.
Exogenous fatty acids remodel Staphylococcus aureus lipid composition through fatty acid kinase
J. Bacteriol.
202
e00128-20
2020
Staphylococcus aureus, Staphylococcus aureus USA300
brenda
Broussard, T.; Miller, D.; Jackson, P.; Nourse, A.; White, S.; Rock, C.
Biochemical roles for conserved residues in the bacterial fatty acid-binding protein family
J. Biol. Chem.
291
6292-6303
2016
Staphylococcus aureus
brenda
Ericson, M.E.; Subramanian, C.; Frank, M.W.; Rock, C.O.
Role of fatty acid kinase in cellular lipid homeostasis and SaeRS-dependent virulence factor expression in Staphylococcus aureus
mBio
8
e00988-17
2017
Staphylococcus aureus, Staphylococcus aureus USA300
brenda
Parsons, J.B.; Frank, M.W.; Jackson, P.; Subramanian, C.; Rock, C.O.
Incorporation of extracellular fatty acids by a fatty acid kinase-dependent pathway in Staphylococcus aureus
Mol. Microbiol.
92
234-245
2014
Staphylococcus aureus, Staphylococcus aureus RN4220
brenda
Parsons, J.B.; Broussard, T.C.; Bose, J.L.; Rosch, J.W.; Jackson, P.; Subramanian, C.; Rock, C.O.
Identification of a two-component fatty acid kinase responsible for host fatty acid incorporation by Staphylococcus aureus
Proc. Natl. Acad. Sci. USA
111
10532-10537
2014
Staphylococcus aureus, Staphylococcus aureus USA300
brenda
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