KINtaro Database
FAMILY: LepB_N (PKLF000027)
Description
LepB_N kinase possesses lipid 4-kinase activity. Legionella pneumophila employs Lepb_N to manipulate host membrane trafficking to facilitate the maturation of the Legionella-containing vacuole (LCV) via specific conversion of PtdIns3Ps (phosphatidylinositol 3-phosphate) into PtdIns(3,4)P2s (phosphatidylinositol 3,4-bisphosphate) (located on LCV) [PMID: 27941800].
Origin
phmmer: 0.0001;
database: nr;
sequence_cutoff: 100aa;
clustering: cdhit: 90%;
catalytic residues: D166 replaced by Serine, but at the three-dimensional level, a histidine residue (H154) in LepB_N occupies the position corresponding to D166, based on - collapsed family logo, 3D structure model, PDB (4JW1) FATCAT structural pairwise alignment with 4JW1, 1ATP, 1O6Y and 6PWD, PMID: 27941800
Structure
PKL domain
HMM Model
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Sequences
Aligned domain sequences
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Unaligned domain sequences
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Full sequences
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Description
LepB_N kinase possesses lipid 4-kinase activity. Legionella pneumophila employs Lepb_N to manipulate host membrane trafficking to facilitate the maturation of the Legionella-containing vacuole (LCV) via specific conversion of PtdIns3Ps (phosphatidylinositol 3-phosphate) into PtdIns(3,4)P2s (phosphatidylinositol 3,4-bisphosphate) (located on LCV) [PMID: 27941800].
Origin
phmmer: 0.0001; database: nr; sequence_cutoff: 100aa; clustering: cdhit: 90%; catalytic residues: D166 replaced by Serine, but at the three-dimensional level, a histidine residue (H154) in LepB_N occupies the position corresponding to D166, based on - collapsed family logo, 3D structure model, PDB (4JW1) FATCAT structural pairwise alignment with 4JW1, 1ATP, 1O6Y and 6PWD, PMID: 27941800
Structure
PKL domain
HMM Model
WebLogo