lpxE

Lipid A 1-phosphatase

445 amino acids

Removes the 1-phosphate group from lipid A species. Absence of phosphate groups in lipid A renders the bacteria resistant to host-derived cationic antimicrobial peptides (CAMP) and allowing it to camouflage itself from the host innate immune response.

49.486 kDa

MNRESFLLLLVLLFALPLHLQASSPCNNMADTTCISDSAKMFPPAIGVYHVKPMKNTLRHSLPLVAASLLTFNVDDNIRELRFTGAGSFHTKIDNVSQLVPLMAQLSMRGFGYKGRSKSWGKMLVSDALGMALMGGMVNAGKYSFGRLRPDGTAANSYPSGHTATAFACATLFHLEYGSRSPWYSVAGYTVASFTGISRIVNNRHWASDVLCGAAVGILVGELGYWISDLIFRDPTGYNYKLTKKQEGTLESMVISLSTGNRYINRQMDFEGKTVERTDAFGMNLKTTFNPSFARWVRIGLQFSVSTEKQKGLTRERPAKVFVAPAISLGLSAGVEWHPWQRASVWAEILPSILFRTDFTNAQDKPDEMSSKLHRRSSFQPAFQVGVAYRVSDHMGIEAHAGYQLGEAVYHLMEETSTWSIIKKRATVPYRGFEFAVGLQFYPFR

lpxE

Lipid A 1-phosphatase

244 amino acids

Removes the 1-phosphate group from (tetraacyl) lipid A species, has no requirement for the Kdo(2) moiety of lipid A. Has no 4'-phosphatase activity. Reduces sensitivity of S.meliloti strain 1021 to the cationic antimicrobial peptide (CAMP) polymyxin B.

Belongs to the lipid A LpxE 1-phosphatase family.

26.99 kDa

MRAFWASLDRRWRRSGVGMPPLRWQACLFVTLNAVILSMLLFDAPIGASKAPAPVKHLGELLTGFGDSAWLIYTSILLFFQGRAGYKLLKTARSKAQALYVSWIGAYLFFTVVFSGLLANLLKRAIGRARPDHFHDYGMFSFAPFSGHSAFESFPSGHSTTVGAFFAAFALLFPRYRVAFIACAIWLGMTRVMVGAHYPSDVIAGLAFGAWFSLLTAIVFARCGLLFKLAPDGWPLAKRLFRTA

lpxE

Lipid A 1-phosphatase

232 amino acids

Probably removes the 1-phosphate moiety from lipid A species. Does not seem to act on other membrane components, nor does it dephosphorylate the 4'-phosphate group of lipid A and/or lipid A precursors.

Belongs to the lipid A LpxE 1-phosphatase family.

25.297 kDa

MPPLRWQACLFITINAVALSMLLFDAPVGASERPAAVKELGELLTGFGDSAWLICISILLFFQGKAGYKLLKTARSKAQALYVSWIGAYLFTTVVFSGLLANLLKRAIGRARPDHFHDYGMFSFTPFSGHAAFESFPSGHSTTVGAFFAAFALLFPRYRVAFIACAIWLGMTRVMVGAHYPSDVIAGLAFGGWFSLLTAIVYARCGLLFKLAPDGWPLAKRLFPDIEKPGAL

lpxE

Lipid A 1-phosphatase

191 amino acids

Removes the 1-phosphate group from tetra- and probably hexaacylated lipid A species (PubMed:16740959). Absence of the 1-phosphate group renders the bacteria partially resistant to host-derived cationic antimicrobial peptides (CAMP), allowing it to camouflage itself from the host innate immune response, and plays a role in the long-term colonization of the host's stomach (PubMed:22216004).

Belongs to the lipid A LpxE 1-phosphatase family.

21.151 kDa

MKKFLFKQKFCESLPKSFSKTLLALSLGLILLGVFIPFPKVPKHQSVPLALHFTEHYARFIPTILSVAIPLIQRDAVGLFQVANASIATTFLTHATKRALNHVTINDQRLGERPYGGNFNMPSGHSSMVGLAVAFLMRRYSVKKYLWLLPLIPLTMLARIYLDMHTIGAVLAGLGTGMLCVGLFTSPKNLN

lpxE

Lipid A 1-phosphatase

190 amino acids

Removes the 1-phosphate group from tetra- and probably hexaacylated lipid A species, has no requirement for the Kdo moiety of lipid A (PubMed:15489235). Has no 4'-phosphatase activity (PubMed:15489235, PubMed:16740959). Has no activity on phospholipids (phosphatidylglycerol, phosphatidylethanolamine or cardiolipin). This enzyme has to act before EptA can attach phosphoethanolamine to the 1-position of lipid A (PubMed:16740959). Absence of the 1-phosphate group renders the bacteria partially resistant to host-derived cationic antimicrobial peptides (CAMP), allowing it to camouflage itself from the host innate immune response, and plays a role in the long-term colonization of the host's stomach (By similarity).

Belongs to the lipid A LpxE 1-phosphatase family.

21.183 kDa

MKKFLFKQKFCESLPKSFSKTLLALSLGLILLGIFAPFPKVPKQPSVPLMFHFTEHYARFIPTILSVAIPLIQRDAVGLFQVANASIATTLLTHTTKRALNHVTINDQRLGERPYGGNFNMPSGHSSMVGLAVAFLMRRYSFKKYFWLLPLVPLTMLARIYLDMHTIGAVLTGLGVGMLCVSLFTSPKKP