|Function||lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase|
|Domain Trusted Cutoff||297.80|
|Domain Noise Cutoff||248.25|
|Mainrole Category||Cell envelope|
|Subrole Category||Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides|
|Gene Ontology Term||GO:0008415: acyltransferase activity molecular_function|
| ||GO:0009245: lipid A biosynthetic process biological_process|
|Entry Date||May 24 2004 3:54PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This model represents a narrow clade of acyltransferases, nearly all of which transfer a lauroyl group to KDO2-lipid IV-A, a lipid A precursor; these proteins are termed lipid A biosynthesis lauroyl acyltransferase, HtrB. An exception is a closely related paralog of E. coli HtrB, LpxP, which acts in cold shock conditions by transferring a palmitoleoyl rather than lauroyl group to the lipid A precursor. Members of this family are homologous to the family of acyltransferases responsible for the next step in lipid A biosynthesis.|
RT An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C.
RA Vorachek-Warren MK, Carty SM, Lin S, Cotter RJ, Raetz CR.
RL J Biol Chem. 2002 Apr 19;277(16):14186-93|
|Genome Property||GenProp0204: KDO(2)-lipid A (Re LPS) biosynthesis and delivery (HMM)|
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