| Accession | TIGR02207 |
| Name | lipid_A_htrB |
| Function | lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase |
| Gene Symbol | lpxL |
| Trusted Cutoff | 297.80 |
| Domain Trusted Cutoff | 297.80 |
| Noise Cutoff | 248.25 |
| Domain Noise Cutoff | 248.25 |
| Isology Type | subfamily |
| EC Number | 2.3.1.- |
| HMM Length | 303 |
| 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 |
| Author | Haft DH |
| 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. |
| References | RM 11830594
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) |
