A0Q4N6 · LPXF_FRATN
- ProteinLipid A 4'-phosphatase
- GenelpxF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids222 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Removes the 4'-phosphate moiety from lipid IV(A) (a tetraacylated precursor of lipid A) and from pentaacylated lipid A, but not from hexaacylated lipid A (as is found in E.coli). Does not dephosphorylate phosphatidic acid, phosphatidylglycerophosphate, or the 1-phosphate group of lipid A and lipid A precursors. Its expression in E.coli confers resistance to the cationic antimicrobial peptide (CAMP) polymyxin B (PubMed:16467300).
Plays a critical role in the ability of the bacteria to avoid the host's innate immune system, especially the bactericidal action of CAMPs, although whether it is CAMP-sensitivity or increased sensitivity to the immune system is not clear (PubMed:17360489).
Plays a critical role in the ability of the bacteria to avoid the host's innate immune system, especially the bactericidal action of CAMPs, although whether it is CAMP-sensitivity or increased sensitivity to the immune system is not clear (PubMed:17360489).
Miscellaneous
In Francisella lipid A is mono-phosphorylated at position 1- and tetraacylated, it lacks the 4'-phosphate residue found in E.coli (PubMed:17263332, PubMed:17360489).
More than 90% of lipid A is in a free form that lacks core oligosaccharide and O-antigen (PubMed:17360489).
More than 90% of lipid A is in a free form that lacks core oligosaccharide and O-antigen (PubMed:17360489).
Pathway
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | hydrolase activity | |
Biological Process | lipid A biosynthetic process | |
Biological Process | lipopolysaccharide biosynthetic process | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipid A 4'-phosphatase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Thiotrichales > Francisellaceae > Francisella
Accessions
- Primary accessionA0Q4N6
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Note: Activity depends on msbA function when expressed in E.coli, strongly suggesting this protein acts in the periplasm (MsbA flips the lipopolysaccharide precursor across the cell inner membrane).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-3 | Cytoplasmic | ||||
Sequence: MAR | ||||||
Transmembrane | 4-24 | Helical; Name=1 | ||||
Sequence: FHIILGLVVCFFAWIFFLIFP | ||||||
Topological domain | 25-58 | Periplasmic | ||||
Sequence: NLDIQFAGHFYNSSAHQFIGGYDGFLGFLHWFAR | ||||||
Transmembrane | 59-79 | Helical; Name=2 | ||||
Sequence: FFPIFFSIIVILFLLGSLFID | ||||||
Topological domain | 80-87 | Cytoplasmic | ||||
Sequence: KFKIKYRK | ||||||
Transmembrane | 88-108 | Helical; Name=3 | ||||
Sequence: AIFFIAVCLWIGPGLVVNYVF | ||||||
Topological domain | 109-144 | Periplasmic | ||||
Sequence: KDHWGRPRPVMVEQFNGDKIFQPPFVISSQCDKNCS | ||||||
Transmembrane | 145-165 | Helical; Name=4 | ||||
Sequence: FVCGDASMGFWLFAFMPLLAT | ||||||
Topological domain | 166-169 | Cytoplasmic | ||||
Sequence: RKKK | ||||||
Transmembrane | 170-190 | Helical; Name=5 | ||||
Sequence: LVAFIAAVVAGGGLGLMRMSQ | ||||||
Topological domain | 191-193 | Periplasmic | ||||
Sequence: GGH | ||||||
Transmembrane | 194-214 | Helical; Name=6 | ||||
Sequence: FFSDVVFCGIFVYISTWVVYA | ||||||
Topological domain | 215-222 | Cytoplasmic | ||||
Sequence: LMYRKKEY |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Lipid A retains the 4'-phosphate group (giving bi-phosphorylated lipid A) and a 3'-hydroxyacyl chain not usually seen in wild-type cells. Cells grow more slowly in liquid culture and are more sensitive to the CAMP polymyxin B. Bacteria are avirulent upon infection of C57BL/6 mice, the natural host of this bacterium; they do not colonize mouse spleen. Upon mouse intraperitoneal injection induces pro-inflammatory cytokine IL-6 and monocyte chemoattractant protein 1 and keratinocyte-derived chemokine, two potent chemoattractants; bacterial viability decreases about 100-fold.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000432495 | 1-222 | Lipid A 4'-phosphatase | |||
Sequence: MARFHIILGLVVCFFAWIFFLIFPNLDIQFAGHFYNSSAHQFIGGYDGFLGFLHWFARFFPIFFSIIVILFLLGSLFIDKFKIKYRKAIFFIAVCLWIGPGLVVNYVFKDHWGRPRPVMVEQFNGDKIFQPPFVISSQCDKNCSFVCGDASMGFWLFAFMPLLATRKKKLVAFIAAVVAGGGLGLMRMSQGGHFFSDVVFCGIFVYISTWVVYALMYRKKEY |
Structure
Sequence
- Sequence statusComplete
- Length222
- Mass (Da)25,552
- Last updated2007-01-09 v1
- Checksum15B8850E5BD330E3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ364143 EMBL· GenBank· DDBJ | ABC96319.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000439 EMBL· GenBank· DDBJ | ABK89201.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP009633 EMBL· GenBank· DDBJ | AJI61280.1 EMBL· GenBank· DDBJ | Genomic DNA |