2.7.8.43	evolution	ethanolamine transferases are members of the YhjW/YjdB/YijP superfamily	734476	
2.7.8.43	evolution	LptA is a member of the lipopolysaccharide transport protein (Lpt) family	752134	
2.7.8.43	evolution	the eptC gene (locus tag Cj0256) is clustered in a family of inner-membrane metalloenzymes (COG2194) containing a fivehelix transmembrane domain and a periplasmic catalytic domain that is currently grouped in the sulfatase family	-, 739786	
2.7.8.43	malfunction	a mutant LptA protein unable to form oligomers has an altered affinity for LPS	752134	
2.7.8.43	malfunction	a pbgP/pmrC double mutant resembled a pmrA mutant both in its lipid A profile and in its susceptibility to polymyxin B, mutation of the pmrC gene results in lipid A that lacks phosphoethanolamine. The inactivation of both the pmrC and pbgP genes in the polymyxin B-resistant pmrA505 genetic background reduces polymyxin B resistance to the levels of the pmrA null mutant	734064	
2.7.8.43	malfunction	although Salmonella lipid A is more prevalently modified with L-4-aminoarabinose, loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA, and LpxT-dependent lipid A modification is not restored in the DELTAeptA mutant. LpxT catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface	-, 723212	
2.7.8.43	malfunction	deletion of colR and of eptA results in loss of Zn2+-induced phosphatidylethanolamine modification of Pseudomonas aeruginosa lipid A. colR deletion mutant complementation restores Zn2+-dependent eptAPa transcription by more than fourfold	739106	
2.7.8.43	malfunction	deletion of gene cj0256 results in the loss of phosphoethanolamine modification of lipid A and sensitivity to CAMPs, polymyxin B. Cj0256 mutants show decreased motility and greatly reduced flagella production. Interruption of cj0256 results in the absence of pEtN modifications on lipid A as well as FlgG. The cj0256 mutant showed a 20fold increase in sensitivity to the cationic antimicrobial peptide, polymyxin B, as well as a decrease in motility	735157	
2.7.8.43	malfunction	deletion of two putative PEA transferase genes in Haemophilus ducreyi increases susceptibility to HBD-3	-, 735018	
2.7.8.43	malfunction	disruption of gene lptA leads to a approximately 10fold decrease in Neisseria meningitidis adhesion to four kinds of human endothelial and epithelial cell lines. Complementation with the lptA gene in the DELTAlptA mutant restores wild-type adherence	733962	
2.7.8.43	malfunction	eptA mutants show a 20fold decrease in polymyxin B resistanc. Overexpression of LpxT in trans in Escherichia coli strain WD101 results in loss of phosphoethanolamine modification and compromised WD101 polymyxin resistance	723212	
2.7.8.43	malfunction	in N-minimal media under Mg2+-limiting conditions to activate the PhoP/PhoQ two-component regulatory system, Salmonella typhimurium PhoP induces activation of PmrA, leading to increased substitution of lipid A phosphate groups with L-4-aminoarabinose and phosphoethanolamine. The mutant strain produces a lipopolysaccharide with an approximate 10fold decrease in the amount of myristate. The lipid myristoylation has an effect on the polymyxin resistance	-, 734151	
2.7.8.43	malfunction	in three enzyme mutant strains, no phosphoethanolamine residues are included in the lipid A region of the lipopolysacchride and there is no further phosphorylation of lipid A beyond one additional phosphate species	734062	
2.7.8.43	malfunction	JSG435 carries a mutant pmrA locus allele (pmrA505) that results in high level polymyxin resistance, probably due to constitutive expression of PmrA/PmrB-activated genes	-, 734706	
2.7.8.43	malfunction	lipid A modification is observed in strain BAA894 when the 1-phosphate residue of lipid A is removed, but disappears when the 4'-phosphate residue of lipid A was removed. When gene ESA_RS16430, the orthologous gene of Escherichia coli pmrA, is deleted in Cronobacter sakazakii strain BAA894, this phosphoethanolamine modification of lipid A is still observed, suggesting that this modification is not regulated by the PmrA-PmrB system. Compared to the wild-type strain BAA894, the ESA_RS09200 deletion mutant shows decreased resistance to cationic antimicrobial peptides, increased recognition by TLR4/MD2, and decreased ability to invade and persist in mammalian cells. Phosphoethanolamine modification of lipid A reduces recognition and killing by the host innate immune system. Analysis of mammalian cell invasion abilities of mutants using human enterocyte-like epithelial Caco-2 cells, overview	-, 738476	
2.7.8.43	malfunction	loss of phosphoethanolamine from lipid A diminishes binding of the complement regulatory protein C4b binding protein (C4BP) to the FA19 porin B (PorB), providing a molecular basis to explain the susceptibility of an lptA null strain of FA19 to killing by normal human serum. Loss of phosphoethanolamine from lipid A also affects binding of the alternative pathway regulator factor H to PorB of some strains, e.g. strains 252 and 1291, but not of strains FA1090 and 273. Complementation of lptA null strains with lptA restores C4BP binding, decreased C4b deposition, and increased resistance to killing by normal human serum	733965	
2.7.8.43	malfunction	loss of phosphoethanolamine substitution from the lipid A component of lipooligosaccharide, due to insertional inactivation of lptA, results in increased gonococcal susceptibility to polymyxin B. Loss of phosphoethanolamine attached to lipid A at 4' position renders strain FA19 susceptible to complement killing. Serum killing of the lptA mutant occurs through the classical complement pathway. Both serum and polymyxin B resistance as well as phosphoethanolamine decoration of lipid A are restored in the lptA-null mutant by complementation with wild-type lptA	-, 733963	
2.7.8.43	malfunction	loss of the enzyme activity increases bacterial sensitivity to killing by human complement and cationic antimicrobial peptides, lptA mutant Neisseria gonorrhoeae is significantly more sensitive to killing by human neutrophils	-, 733635	
2.7.8.43	malfunction	phenotypes of mutants of PmrA-dependent genes pbgE2 and pbgE3, overview	-, 734198	
2.7.8.43	malfunction	point mutations in the PmrA/B two-component system lead to colistin resistance	733107	
2.7.8.43	malfunction	strains lacking gene eptC show decreased commensal colonization of chick ceca and reduced colonization of BALB/cByJ mice compared to wild-type strains	-, 733966	
2.7.8.43	malfunction	the eptC-deficient Campylobacter jejuni strain shows a dramatic decrease in resistance to polymyxin B when compared with wild-type, indicating a loss of phosphoethanolamine modification of the lipid A backbone. Campylobacter strains expressing site-directed FlgG mutants show defects in motility arise directly from the loss of phophoethanolamine modification of FlgG, phenotypes, overview	-, 734190	
2.7.8.43	malfunction	the phenotypes of Neisseria meningitidis strains lacking LptB, LptC, LptH (homologue of Escherichia coli LptA), LptF, and LptG are identical to those lacking LptD or MsbA, i.e. the knockout mutants are viable but leaky and produce only very little LPS, which is not present at the cell surface	-, 752031	
2.7.8.43	malfunction	WD101, a polymyxin-resistant Escherichia coli K-12 strain, contains a mutation in the pmrA (basR) gene resulting in a pmrAC phenotype promoting polymyxin resistance	734151	
2.7.8.43	malfunction	wild-type Neisseria gonorrhoeae strain FA1090 has a survival advantage relative to a PEA transferase A (lptA) mutant in the human urethral-challenge and murine lower genital tract infection models. Purified lipooligosaccharide containing lipid A devoid of the phosphoethanolamine modification and an lptA mutant of strain FA19 induce significantly lower levels of NF-kappaB in human embryonic kidney Toll-like receptor 4 (TLR4) cells and murine embryonic fibroblasts than wild-type lipooligosaccharide of the parent strain. Vaginal proinflammatory cytokines and chemokines are not elevated in female mice infected with the isogenic lptA mutant, in contrast to mice infected with the wild-type and complemented lptA mutant bacteria. lptA mutant bacteria are more susceptible to human and murine cathelicidins due to increased binding by these peptides and that the differential induction of NF-kappaB by wild-type and unmodified lipid A is more pronounced in the presence of cationic antimicrobial peptides. Wild-type but not lptA mutant gonococci induce a proinflammatory response during infection	-, 738368	
2.7.8.43	metabolism	Hp0021 is the structural gene for the lipid A 1-phosphatase and is required for removal of the 1-phosphate group from mature lipid A in an in vitro assay system	734148	
2.7.8.43	metabolism	PmrA is activated under Mg2+ limiting growth conditions or upon exposure to cationic antimicrobial peptides. Under these conditions PmrA activation is mediated by a second two-component system, PhoP/PhoQ. activation of PhoP in Salmonella induces the synthesis of PmrD, which regulates PmrA activity post-transcriptionally by preventing dephosphorylation of PmrA	-, 723212	
2.7.8.43	metabolism	the development of a moderate level of colistin resistance in Acinetobacter baumannii requires distinct genetic events, including (i) at least one point mutation in pmrB, (ii) upregulation of pmrAB, and (iii) expression of pmrC, which lead to addition of phosphoethanolamine to lipid A	733107	
2.7.8.43	metabolism	the PmrA-activated pmrC gene encodes an inner membrane protein that is required for the incorporation of phosphoethanolamine into lipid A and for polymyxin B resistance. The pbg operon and the pmrC genes are solely responsible for PmrA-regulated polymyxin B resistance, but the pmrC gene is dispensable for resistance to Fe3+	734064	
2.7.8.43	metabolism	the PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B, while the PmrA-regulated STM4118 (cptA) gene is necessary for the addition of phosphoethanolamine to the lipopolysacchride core, which is not affected by PmrC, overview. The PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B	-, 734067	
2.7.8.43	metabolism	the polymyxin-resistant phenotype is primarily under the control of the PmrA/PmrB two-component regulatory system that is activated during growth under conditions of low pH, high Fe3+, and in a PhoP/PhoQ-dependent manner during Mg2+ starvation	734151	
2.7.8.43	metabolism	the two-component regulatory system PmrA/PmrB controls in part the modifications of the Salmonella enterica serovar Typhimurium lipopolysaccharide with the addition of 4-aminoarabinose to the lipid A and phosphoethanolamine to the lipid A and core in response to the in vivo environment	-, 734067	
2.7.8.43	metabolism	two unlinked PmrA/PmrB-regulated loci, designated pmrE and pmrF, are identified as necessary for resistance of the organism to polymyxin B and for the addition of aminoarabinose to lipid A. Genes immediately flanking this putative operon are also regulated by PmrA/PmrB and/or have been associated with Salmonella typhimurium polymyxin resistance	-, 734706	
2.7.8.43	metabolism	under PmrA regulator activation, the expression of wzzfepE and wzzst genes is induced, and their products are required to determine the O-antigen chain length. Wzzst protein is necessary to maintain the balance of 4-aminoarabinose and phosphoethanolamine lipid A modifications. The interaction of the PmrA-dependent pbgE2 and pbgE3 gene products is important for the formation of the short O-antigen region, protein Wzzst is unable to interact with itself or with the PbgE2 or PbgE3 protein	-, 734198	
2.7.8.43	additional information	analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview	734476	
2.7.8.43	additional information	homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview	-, 734476	
2.7.8.43	additional information	identification of identify zinc-ligand residues, a putative nucleophile and conserved active-site residues required for in vivo activity from the crystal structure, active-site architecture of cEptC, overview	-, 739786	
2.7.8.43	physiological function	a 6-residue-requiring zinc-binding/catalytic motif is essential for MCR2-mediated colistin resistance. The transmembrane regions TM2 and TM1 play a critical role in MCR2-mediated colistin resistance, catalytic activity depends on the correct location of MCR2 in bacterial periplasm	761797	
2.7.8.43	physiological function	Cronobacter sakazakii modifies its lipid A structure through the enzyme to avoid recognition by the host immune cells. Gene ESA_RS09200, encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system. The enzyme is active in cells grown at pH 5.0, not pH 7.0. Gene ESA_RS09200, but not ESA_RS16425, is required for phosphoethanolamine addition to the lipid A in strain BAA894	-, 738476	
2.7.8.43	physiological function	enzyme LptA is required for phosphoethanolamine modification of lipid A and contributes to resistance of the organism against the human antimicrobial peptides alpha-defensin and beta-defensin, mechanism of resistance to alpha-defensins, overview. Gene lptA is not required for survival in vivo	735018	
2.7.8.43	physiological function	enzyme PmrA is required for production of lipid A species with one or two phosphoethanolamine or 4-amino-4-deoxy-L-arabinose substituents. PmrA is not needed for the incorporation of 2-hydroxymyristate or palmitate into lipid A	-, 734138	
2.7.8.43	physiological function	EptA-dependent lipid A modification is required for resistance to polymyxin B, EptA plays a dominant role in polymyxin resistance. Enzyme PmrA is not involved in transcription of LpxT, which catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface. LpxT-dependent lipid A modification is regulated post-translationally. The regulation does not occur at the level of transcription, but rather following the assembly of LpxT into the inner membrane. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A, which is critical for Escherichia coli to resist the bactericidal activity of polymyxin	723212	
2.7.8.43	physiological function	EptA-dependent lipid A modification is required for resistance to polymyxin B. Expression of EptA (PmrC) is under the control of PmrA/PmrB	-, 723212	
2.7.8.43	physiological function	expression in Escherichia coli leads to 4fold increase in resistance to antibiotics colistin and polymyxin B. In addition to the catalytoc domain, the N-terminal transmembrane regions are required to confer drug resistance in the cell	760257	
2.7.8.43	physiological function	gene product of ESA_RS09200 in Cronobacter sakazakii encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system. phosphoethanolamine modification of lipid A reduces recognition and killing by the host innate immune system	-, 761356	
2.7.8.43	physiological function	Gram-negative bacteria survive harmful environmental stressors by modifying their outer membrane. Much of this protection is afforded upon remodeling of the lipid A region of the major surface molecule lipopolysaccharide. Addition of cationic substituents, such as 4-amino-4-deoxy-L-arabinose (L-Ara4N) and phosphoethanolamine (pEtN) at the lipid A phosphate groups, is often induced in response to specific environmental flux stabilizing the outer membrane. ColR specifically induces pEtN addition to lipid A in lieu of L-Ara4N when Zn2+ is present	739106	
2.7.8.43	physiological function	in Shigella flexneri serotype X and 4a variants called Xv and 4av, respectively, O-antigen modification with phosphoethanolamine (PEtN) is identified, which is encoded by a plasmid-borne gene lpt-O for a PEtN-transferase and confers the monoclonal antibody IV-1(MASF IV-1) determinant to the bacteria. A correlation between the serotype-specific PEtN modification pattern and the lpt-O variation in different serotypes: lpt-ORII in serotype Xv is better tuned for phosphorylation of RhaII and lpt-ORIII in serotypes Yv and 4av for phosphorylation of RhaII	740516	
2.7.8.43	physiological function	LptA functions to transport lipopolysaccharide (LPS) through the periplasm to the outer leaflet of the outer membrane after ABC transporter MsbA flips LPS across the inner membrane. It is hypothesized that LPS binds to LptA to cross the periplasm and that the acyl chains of LPS bind to the central pocket of LptA	752134	
2.7.8.43	physiological function	LptA is important for Neisseria gonorrhoeae defence against non-oxidative components produced by polymorphonuclear leukocytes, PMNs. Infection of humans with Neisseria gonorrhoeae is marked by an influx of neutrophils to the site of infection. Enzyme LptA-catalysed modification of lipooligosaccharide enhances gonococcal defence against human neutrophils and enhances survival of the bacteria from the human inflammatory response during acute gonorrhoea. Three mechanisms underlie the increased sensitivity of lptA mutant bacteria to neutrophils: (i) lptA mutant bacteria are more likely to reside in mature phagolysosomes than LptA expressing bacteria, (ii) lptA mutant bacteria are more sensitive to killing by components found in neutrophil granules, including CAP37/azurocidin, human neutrophil peptide 1 and the serine protease cathepsin G, (iii) lptA mutant bacteria are more susceptible to killing by antimicrobial components that are exocytosed from neutrophils, including those decorating neutrophil extracellular traps	-, 733635	
2.7.8.43	physiological function	minimum inhibitory concentrations of polymyxin B and colistin for the wild-type are twice as high as those for the mutant lacking the eptA gene	-, 762389	
2.7.8.43	physiological function	modification of lipooligosaccharide with phosphoethanolamine by enzyme LptA enhances meningococcal adhesion to human endothelial and epithelial cells in unencapsulated Neisseria meningitidis. LptA does not directly act as an adhesin molecule. Enzyme LptA-mediated adhesion may be masked when meningococci are encapsulated	733962	
2.7.8.43	physiological function	modification of the 1-phosphate group of Helicobacter pylori lipid A requires two enzymatic steps	734148	
2.7.8.43	physiological function	phosphatidylethanolamine is transferred to lipid A by EptA homologue, PetL, and is transferred to galactose by a phosphatidylethanolamine transferase that is unique to Pasteurella multocida called PetG. The presence of a functional petL and petK, which iis responsible for PEtn addition to the single Kdo molecul, an therefore the presence of phosphatidylethanolamine on lipid A and Kdo1, i essential for resistance to the antimicrobial peptide cathelicidin-2. An enzyme inactivation mutant grows similar to wild-type	-, 761244	
2.7.8.43	physiological function	phosphoethanolamine modification of lipid A in colistin-resistant variants of Acinetobacter baumannii, e.g. strain ATCC 19606, is mediated by the pmrAB two-component regulatory system	733107	
2.7.8.43	physiological function	phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro. The PEA transferase genes confer resistance to alpha and beta-defensins but not to cathelicidin or human serum. Genes lptA is not required for survival in vivo	-, 735018	
2.7.8.43	physiological function	phosphoethanolamine-lipid A contributes to serum resistance by modulating factor H binding	733965	
2.7.8.43	physiological function	PmrAB is the global regulatory system that controls lipopolysaccharide modification, leading to a coordinate regulation of 4-aminoarabinose incorporation and O-antigen chain length to respond against the host defense mechanisms. The PmrAB two-component system consists of the PmrA response regulator and the PmrB sensor, which is able to sense Fe3+, activating the system. The PmrAB two-component system activation promotes a remodeling of lipid A and the core region by addition of 4-aminoarabinose and/or phosphoethanolamine. These PmrA-dependent activities are produced by activation of ugd, pbgPE, pmrC, cpta, and pmrG transcription. Lipid A profiles from wild-type and mutant strains, overview	-, 734198	
2.7.8.43	physiological function	the addition of PEA to lipid A by lipid A PEA transferase, LptA, is a major mechanism for resistance to polymyxin in Neisseria meningitidis since this species does not synthesize 4-aminoarabinose. The neisserial lipooligosaccharide phosphoethanolamine transferase A is required for resistance to polymyxin	734476	
2.7.8.43	physiological function	the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue	-, 734190	
2.7.8.43	physiological function	the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue. The enzyme also catalyzes the addition of phosphoethanolamine to the first heptose sugar of the inner core oligosaccharide of lipooligosaccharide, a fourth enzymatic target. Modification of Campylobacter jejuni lipid A with phosphoethanolamine results in increased recognition by the human Toll-like receptor 4-myeloid differentiation factor 2 complex, along with providing resistance to relevant mammalian and avian antimicrobial peptides (i.e., defensins). Modification of surface structures with phosphoethanolamine by EptC is key to its ability to promote commensalism in an avian host and to survive in the mammalian gastrointestinal environment. Modification of FlgG is required for efficient flagellar production and motility	-, 733966	
2.7.8.43	physiological function	the enzyme is involved in lipopolysaccharide (LPS) transport. LptA binds lipid A, it might act as a chaperone, assisting the amphipathic LPS molecules to pass through the aqueous periplasm. LptB, LptC, LptF, LptG, and LptH(LptA) are essential components of the LPS transport system in the important model organism for outer membrane biogenesis, Neisseria meningitidis, as they are in Escherichia coli. LptA binds to LptC but not to LptE	-, 752031	
2.7.8.43	physiological function	the enzyme is required for substitution of osmoregulated periplasmic glucans by phosphoethanolamine	740134	
2.7.8.43	physiological function	the enzyme is responsible for the transfer of phosphoethanolamine residues to the lipid A in several Neisseria meningitidis strains. In all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview	734062	
2.7.8.43	physiological function	the enzyme modifies two periplasmic targets, a membrane lipid A and a flagellar protein. It is required for efficient motility and flagella production	735157	
2.7.8.43	physiological function	the enzyme phosphoethanolamine transferase A is involved in the addition of phosphoethanolamine moieties to lipid A	-, 733017	
2.7.8.43	physiological function	the enzyme regulates the modification of phosphate moieties of lipid A, which may be substituted with L-4-aminoarabinose or phosphoethanolamine groups	-, 734151	
2.7.8.43	physiological function	the enzyme regulates the modification of phosphate moieties of lipid A, which may be substituted with L-4-aminoarabinose or phosphoethanolamine groups. The enzyme also regulates the catalysis of periplasmic addition of L-4-aminoarabinose to lipid A through glycosyltransferase L-4-aminoarabinose transferase (ArnT)	734151	
2.7.8.43	physiological function	the foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine. Modifying lipid A with phosphoethanolamine promotes cationic antimicrobial peptide resistance. Modifications of the Campylobacter jejuni surface structures with phosphoethanolamine promote flagellar assembly, motility, cationic antimicrobial peptide resistance and host intestinal colonization	-, 739786	
2.7.8.43	physiological function	the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit, functional significance of LptA oligomerization and LptC. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the outer membrane by periplasmic LptA. The LptB2FG tetramer extracts LPS from the outer leaflet of the inner membrane and provides the energy to drive LPS transport through an ATPase-dependent mechanism. LptA provides a continuous LPS binding surface that conveys it to the outer membrane. Mechanism of the LPS (lipopolysaccharide) transport (Lpt) system, specific LPS interactions with LptA and LptC, LptC is the intermediate between the inner membrane complex and LptA, overview	750867	
2.7.8.43	physiological function	the paradigm of resistance to antibiotic colistin mediated by ethanolamine phosphotransferase in Shewanella algae MARS 14. Resistance to colistin in Shewanella algae MARS 14 is associated with overexpression of enzyme EptA (27fold increase), which plays a crucial role in the arrangement of outer membrane lipopolysaccharide	-, 740532	
2.7.8.43	physiological function	the PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B	-, 734067	
2.7.8.43	physiological function	the PmrA/PmrB regulatory system of Salmonella enterica controls the modification of lipid A with aminoarabinose and phosphoethanolamine, the PmrA-dependent modification of lipid A with aminoarabinose and phosphoethanolamine is responsible for PmrA-regulated polymyxin B resistance	734064	
2.7.8.43	physiological function	the two-component regulatory system PmrA/PmrB controls in part the modifications of the Salmonella enterica serovar Typhimurium lipopolysaccharide with the addition of 4-aminoarabinose to the lipid A and phosphoethanolamine to the lipid A and core in response to the in vivo environment	-, 734067	
2.7.8.43	physiological function	wild-type Neisseria gonorrhoeae strain FA1090 has a survival advantage relative to a PEA transferase A (lptA) mutant in the human urethral-challenge and murine lower genital tract infection models. Wild-type lipid A stimulates the humanTLR4-MD2-CD14 complex	-, 738368