LPXE_HELPY
ID LPXE_HELPY Reviewed; 190 AA.
AC O24866; Q1PDD4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Lipid A 1-phosphatase {ECO:0000303|PubMed:15489235};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxE {ECO:0000303|PubMed:15489235};
GN OrderedLocusNames=HP_0021, C694_00100;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP STRUCTURE OF LIPID A.
RC STRAIN=ATCC 700392 / 26695;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RA Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA Kostrjukova E., Govorun V.;
RT "Draft genome of Helicobacter pylori.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBSTRATE SPECIFICITY, PATHWAY, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, STRUCTURE OF LIPID A, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=ATCC 700392 / 26695, Cp20-84, Hp7-91, and Hsp110-93;
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).
CC -!- FUNCTION: Removes the 1-phosphate group from tetra- and probably
CC hexaacylated lipid A species, has no requirement for the Kdo moiety of
CC lipid A (PubMed:15489235). Has no 4'-phosphatase activity
CC (PubMed:15489235, PubMed:16740959). Has no activity on phospholipids
CC (phosphatidylglycerol, phosphatidylethanolamine or cardiolipin). This
CC enzyme has to act before EptA can attach phosphoethanolamine to the 1-
CC position of lipid A (PubMed:16740959). Absence of the 1-phosphate group
CC renders the bacteria partially resistant to host-derived cationic
CC antimicrobial peptides (CAMP), allowing it to camouflage itself from
CC the host innate immune response, and plays a role in the long-term
CC colonization of the host's stomach (By similarity).
CC {ECO:0000250|UniProtKB:Q9ZN40, ECO:0000269|PubMed:15489235,
CC ECO:0000269|PubMed:16740959}.
CC -!- COFACTOR:
CC Note=Does not require divalent cations. {ECO:0000269|PubMed:15489235};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0, activity is seen from pH 5.5 to 8.0.
CC {ECO:0000269|PubMed:15489235};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000305|PubMed:16740959}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:15489235,
CC ECO:0000305|PubMed:16740959}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Activity depends on msbA function when expressed in
CC E.coli, strongly suggesting this protein acts in the periplasm (MsbA
CC flips the lipopolysaccharide precursor across the inner cell membrane).
CC {ECO:0000269|PubMed:15489235}.
CC -!- DISRUPTION PHENOTYPE: Lipid A retains the 1-phosphate group; none of
CC the lipid A species have the usual phosphoethanolamine residue at the
CC 1-position as the enzyme responsible (EptA) cannot act on a
CC phosphorylated residue. In strain 26695 95% is hexaacylated (16 to 18
CC carbons in length) with both 1- and 4'-phosphate groups, 5% is
CC tetraacylated with only 1-phosphate. In 4 other strains (Cp20-84, Hp7-
CC 91, Hsp110-93 and J99) only the 1-phosphate tetraacylated species is
CC seen. Over 1250-fold decrease (strain 26695) or 10-fold decrease
CC (strain Hp7-91) in resistance to cationic antimicrobial peptide (CAMP)
CC polymyxin B (PMB); strain 26695 is probably more sensitive because it
CC has a more negatively charged cell surface and thus binds more CAMP. In
CC strain Hp7-91 upon exposure to PMB the cells round into a coccoid form,
CC the outer membrane forms ruffles, invaginates and in some cases the
CC periplasmic region increases in volume. {ECO:0000269|PubMed:16740959}.
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:15489235,
CC ECO:0000269|PubMed:16740959}.
CC -!- SIMILARITY: Belongs to the lipid A LpxE 1-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; DQ447324; ABE02821.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07094.1; -; Genomic_DNA.
DR EMBL; CP003904; AFV41241.1; -; Genomic_DNA.
DR PIR; E64522; E64522.
DR RefSeq; NP_206823.1; NC_000915.1.
DR RefSeq; WP_000713906.1; NC_018939.1.
DR AlphaFoldDB; O24866; -.
DR IntAct; O24866; 2.
DR STRING; 85962.C694_00100; -.
DR PaxDb; O24866; -.
DR EnsemblBacteria; AAD07094; AAD07094; HP_0021.
DR KEGG; heo:C694_00100; -.
DR KEGG; hpy:HP_0021; -.
DR PATRIC; fig|85962.47.peg.20; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_1426205_0_0_7; -.
DR OMA; FNMPSGH; -.
DR PhylomeDB; O24866; -.
DR BioCyc; MetaCyc:HP_RS00125-MON; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000429; 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; IDA:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Hydrolase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..190
FT /note="Lipid A 1-phosphatase"
FT /id="PRO_0000432490"
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 190 AA; 21183 MW; FE300DFD237655AD CRC64;
MKKFLFKQKF CESLPKSFSK TLLALSLGLI LLGIFAPFPK VPKQPSVPLM FHFTEHYARF
IPTILSVAIP LIQRDAVGLF QVANASIATT LLTHTTKRAL NHVTINDQRL GERPYGGNFN
MPSGHSSMVG LAVAFLMRRY SFKKYFWLLP LVPLTMLARI YLDMHTIGAV LTGLGVGMLC
VSLFTSPKKP
