LPXE_HELPJ
ID LPXE_HELPJ Reviewed; 191 AA.
AC Q9ZN40;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Lipid A 1-phosphatase {ECO:0000303|PubMed:15489235};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxE {ECO:0000303|PubMed:22216004}; OrderedLocusNames=jhp_0019;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
RN [2]
RP FUNCTION.
RC STRAIN=J99 / ATCC 700824;
RX PubMed=15489235; DOI=10.1074/jbc.m406480200;
RA Tran A.X., Karbarz M.J., Wang X., Raetz C.R., McGrath S.C., Cotter R.J.,
RA Trent M.S.;
RT "Periplasmic cleavage and modification of the 1-phosphate group of
RT Helicobacter pylori lipid A.";
RL J. Biol. Chem. 279:55780-55791(2004).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, STRUCTURE OF LIPID A, AND ANTIBIOTIC
RP RESISTANCE.
RC STRAIN=J99 / ATCC 700824;
RX PubMed=16740959; DOI=10.1128/jb.00146-06;
RA Tran A.X., Whittimore J.D., Wyrick P.B., McGrath S.C., Cotter R.J.,
RA Trent M.S.;
RT "The lipid A 1-phosphatase of Helicobacter pylori is required for
RT resistance to the antimicrobial peptide polymyxin.";
RL J. Bacteriol. 188:4531-4541(2006).
RN [4]
RP FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, STRUCTURE OF LIPID A, AND
RP ANTIBIOTIC RESISTANCE.
RC STRAIN=B128, J99 / ATCC 700824, and X47;
RX PubMed=22216004; DOI=10.1371/journal.ppat.1002454;
RA Cullen T.W., Giles D.K., Wolf L.N., Ecobichon C., Boneca I.G., Trent M.S.;
RT "Helicobacter pylori versus the host: remodeling of the bacterial outer
RT membrane is required for survival in the gastric mucosa.";
RL PLoS Pathog. 7:E1002454-E1002454(2011).
CC -!- FUNCTION: Removes the 1-phosphate group from tetra- and probably
CC hexaacylated lipid A species (PubMed:16740959). Absence of the 1-
CC phosphate group renders the bacteria partially resistant to host-
CC derived cationic antimicrobial peptides (CAMP), allowing it to
CC camouflage itself from the host innate immune response, and plays a
CC role in the long-term colonization of the host's stomach
CC (PubMed:22216004). {ECO:0000269|PubMed:16740959,
CC ECO:0000269|PubMed:22216004, ECO:0000305|PubMed:15489235}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000269|PubMed:22216004, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:O24866}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of 1-phosphate tetraacylated lipid
CC A, unlike strain 26695 no hexaacylated lipid A is detected
CC (PubMed:16740959, PubMed:22216004). 16-fold to 25-fold decrease in
CC resistance to CAMP polymyxin B (PMB) (PubMed:16740959,
CC PubMed:22216004). Increased cell-surface binding of CAMP, 2-fold
CC decrease in resistance to endogenous antibacterial peptide Hp (rplA).
CC Lipopolysaccharide (LPS) from this strain induces the human innate
CC immune response via Toll-like receptor 4 (TLR4) 2-fold in cultured
CC cells (similar effects are seen with mouse cells, has no effect on
CC TLR2-mediated induction). No changes in O-antigen or motility.
CC Decreased ability to colonize C57BL/6J mouse stomachs (using mouse-
CC adapted H.pylori strains B128 and X47). A double lpxE-lpxF mutant
CC accumulates 1-, 4'-bisphosphate hexaacylated lipid A, has 1000-fold
CC decrease in resistance to PMB (a similar reduction in resistance is
CC seen for other human-derived CAMPs), a 70-fold decrease in resistance
CC to endogenous antibacterial peptide Hp, induces the innate immune
CC response via TLR4 10-fold, loss of colonization of C57BL/6J mouse
CC stomachs (strains B128 and X47) (PubMed:22216004).
CC {ECO:0000269|PubMed:16740959, ECO:0000269|PubMed:22216004}.
CC -!- MISCELLANEOUS: In this organism most lipid A is tetraacylated without a
CC phosphate group at the 4'-position and a phosphoethanolamine residue at
CC the 1-position. {ECO:0000269|PubMed:16740959,
CC ECO:0000269|PubMed:22216004}.
CC -!- SIMILARITY: Belongs to the lipid A LpxE 1-phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001439; AAD05601.1; -; Genomic_DNA.
DR PIR; A71985; A71985.
DR RefSeq; WP_000713927.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZN40; -.
DR SMR; Q9ZN40; -.
DR STRING; 85963.jhp_0019; -.
DR EnsemblBacteria; AAD05601; AAD05601; jhp_0019.
DR KEGG; hpj:jhp_0019; -.
DR PATRIC; fig|85963.30.peg.1023; -.
DR eggNOG; COG0671; Bacteria.
DR OMA; FNMPSGH; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IMP:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Hydrolase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..191
FT /note="Lipid A 1-phosphatase"
FT /id="PRO_0000432489"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
SQ SEQUENCE 191 AA; 21151 MW; 964EC50B9BACE7C7 CRC64;
MKKFLFKQKF CESLPKSFSK TLLALSLGLI LLGVFIPFPK VPKHQSVPLA LHFTEHYARF
IPTILSVAIP LIQRDAVGLF QVANASIATT FLTHATKRAL NHVTINDQRL GERPYGGNFN
MPSGHSSMVG LAVAFLMRRY SVKKYLWLLP LIPLTMLARI YLDMHTIGAV LAGLGTGMLC
VGLFTSPKNL N
