LPXE_PORG3
ID LPXE_PORG3 Reviewed; 445 AA.
AC B2RLI7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Lipid A 1-phosphatase {ECO:0000303|PubMed:19552698};
DE EC=3.1.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=lpxE {ECO:0000305}; Synonyms=PG1773 {ECO:0000303|PubMed:19552698};
GN OrderedLocusNames=PGN_1713;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND LIPID A STRUCTURE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=19552698; DOI=10.1111/j.1462-5822.2009.01349.x;
RA Coats S.R., Jones J.W., Do C.T., Braham P.H., Bainbridge B.W., To T.T.,
RA Goodlett D.R., Ernst R.K., Darveau R.P.;
RT "Human Toll-like receptor 4 responses to P. gingivalis are regulated by
RT lipid A 1- and 4'-phosphatase activities.";
RL Cell. Microbiol. 11:1587-1599(2009).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=A7436;
RX PubMed=24478080; DOI=10.1128/iai.01136-13;
RA Zenobia C., Hasturk H., Nguyen D., Van Dyke T.E., Kantarci A.,
RA Darveau R.P.;
RT "Porphyromonas gingivalis lipid A phosphatase activity is critical for
RT colonization and increasing the commensal load in the rabbit ligature
RT model.";
RL Infect. Immun. 82:650-659(2014).
CC -!- FUNCTION: Removes the 1-phosphate group from lipid A species. Absence
CC of phosphate groups in lipid A renders the bacteria resistant to host-
CC derived cationic antimicrobial peptides (CAMP) and allowing it to
CC camouflage itself from the host innate immune response.
CC {ECO:0000269|PubMed:19552698}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No longer responds to changes in hemin, decreased
CC removal of 1-phosphate from lipid A species. Accumulates bi-
CC phosphorylated pentaacyl and tetraacyl 1-phosphate lipid A species.
CC Lipopolysaccharide (LPS) from this strain is a mild inducer of the
CC human innate immune response via Toll-like receptor 4 (TLR4) in
CC cultured HEK293 cells; double lpxE-lpxF mutants are more potent than
CC either single mutant. No change in resistance to the cationic
CC antimicrobial peptide (CAMP) polymyxin B. Double lpxE-lpxF mutants
CC accumulate multiple mono- and bi-phosphorylated lipid A species
CC (PubMed:19552698). Unable to colonize rabbit periodontium, a model for
CC periodontal disease (PubMed:24478080). {ECO:0000269|PubMed:19552698,
CC ECO:0000269|PubMed:24478080}.
CC -!- MISCELLANEOUS: When grown in low hemin conditions the major lipid A
CC species are non-phosphorylated tetraacyl and 4'-phosphate pentaacyl
CC lipid A, while under high hemin conditions the major lipid A species
CC are non-phosphorylated tetraacyl and 1-phosphate tetraacyl lipid A
CC (hemin is protoporphyrin IX containing Fe(3+) with a chloride ligand
CC (CHEBI:50385) involved in the change from healthy to diseased gums).
CC {ECO:0000269|PubMed:19552698}.
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DR EMBL; AP009380; BAG34232.1; -; Genomic_DNA.
DR RefSeq; WP_012458477.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RLI7; -.
DR STRING; 431947.PGN_1713; -.
DR EnsemblBacteria; BAG34232; BAG34232; PGN_1713.
DR GeneID; 29256877; -.
DR KEGG; pgn:PGN_1713; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_615168_0_0_10; -.
DR OMA; ETSTWSI; -.
DR BioCyc; PGIN431947:G1G2V-1921-MON; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0042597; C:periplasmic space; 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 InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Periplasm; Signal; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..445
FT /note="Lipid A 1-phosphatase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432491"
SQ SEQUENCE 445 AA; 49486 MW; 7EF55ADC3794E1CD CRC64;
MNRESFLLLL VLLFALPLHL QASSPCNNMA DTTCISDSAK MFPPAIGVYH VKPMKNTLRH
SLPLVAASLL TFNVDDNIRE LRFTGAGSFH TKIDNVSQLV PLMAQLSMRG FGYKGRSKSW
GKMLVSDALG MALMGGMVNA GKYSFGRLRP DGTAANSYPS GHTATAFACA TLFHLEYGSR
SPWYSVAGYT VASFTGISRI VNNRHWASDV LCGAAVGILV GELGYWISDL IFRDPTGYNY
KLTKKQEGTL ESMVISLSTG NRYINRQMDF EGKTVERTDA FGMNLKTTFN PSFARWVRIG
LQFSVSTEKQ KGLTRERPAK VFVAPAISLG LSAGVEWHPW QRASVWAEIL PSILFRTDFT
NAQDKPDEMS SKLHRRSSFQ PAFQVGVAYR VSDHMGIEAH AGYQLGEAVY HLMEETSTWS
IIKKRATVPY RGFEFAVGLQ FYPFR
