LPXF_HELPJ
ID LPXF_HELPJ Reviewed; 198 AA.
AC Q9ZJ31;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Lipid A 4'-phosphatase {ECO:0000303|PubMed:22216004};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxF {ECO:0000303|PubMed:22216004}; OrderedLocusNames=jhp_1487;
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, 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 4'-phosphate group from tetra- and hexaacylated
CC lipid A species, has no 1-phosphatase or Kdo hydrolase activity.
CC Absence of the 4'-phosphate group renders the bacteria resistant to
CC host-derived cationic antimicrobial peptides (CAMP), allowing it to
CC camouflage itself from the host innate immune response, and plays a
CC critical role in the long-term colonization of the host's stomach.
CC {ECO:0000269|PubMed:22216004}.
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:A0Q4N6}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Loss of Kdo(2)-lipid A 4'-phosphatase activity,
CC accumulation of 4'-phosphate hexaacylated lipid A. 360-fold decrease in
CC resistance to cationic antimicrobial peptide (CAMP) polymyxin B (PMB),
CC increased cell-surface binding of CAMP, 20-fold decrease in resistance
CC to endogenous antibacterial peptide Hp (rplA). Lipopolysaccharide (LPS)
CC from the deleted strain induces the human innate immune response via
CC Toll-like receptor 4 (TLR4) 6-fold in cultured cells (similar effects
CC are seen with mouse cells, has no effect on TLR2-mediated induction).
CC Almost complete loss of colonization of C57BL/6J mouse stomach (using
CC mouse-adapted H.pylori strains B128 and X47). No changes in O-antigen
CC or cell motility. A double lpxE-lpxF mutant accumulates 1-, 4'-
CC bisphosphate hexaacylated lipid A, has 1000-fold decrease in resistance
CC to PMB (a similar reduction in resistance is seen for other human-
CC derived CAMPs), a 70-fold decrease in resistance to endogenous
CC antibacterial peptide Hp, induces the innate immune response via TLR4
CC 10-fold, complete loss of colonization of C57BL/6J mouse stomachs
CC (strains B128 and X47). {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:22216004}.
CC -!- SIMILARITY: Belongs to the lipid A LpxF 4'-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD07061.1; -; Genomic_DNA.
DR PIR; A71801; A71801.
DR RefSeq; WP_000734125.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZJ31; -.
DR SMR; Q9ZJ31; -.
DR STRING; 85963.jhp_1487; -.
DR EnsemblBacteria; AAD07061; AAD07061; jhp_1487.
DR KEGG; hpj:jhp_1487; -.
DR PATRIC; fig|85963.30.peg.1054; -.
DR eggNOG; COG0671; Bacteria.
DR OMA; AFSNAHK; -.
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..198
FT /note="Lipid A 4'-phosphatase"
FT /id="PRO_0000432496"
FT TRANSMEM 143..165
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 198 AA; 21864 MW; 07D5136A5AD58E62 CRC64;
MKKLKGLFLS LLLWVYPLKS EPINEGAYIL EEIGDVLRFL PIFVGTVSLA MRDYRGLGEL
AVGTLVTQGV IYGLKGAFST AHKDGARVGF AKRPCCNSWR GMPSGHAGGA FSAAGFVYYR
YGWKPALPVI ALAILTDTSR VVAGQHTILQ VTIGSLIAWG FAYLFTSRYK PKRWMLYPEI
SSDFKGSSRY GVGFSYQW
