LPXF_PORG3
ID LPXF_PORG3 Reviewed; 236 AA.
AC B2RI48;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Lipid A 4'-phosphatase {ECO:0000303|PubMed:19552698};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxF {ECO:0000305}; Synonyms=PG1587 {ECO:0000303|PubMed:19552698};
GN OrderedLocusNames=PGN_0524;
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, LIPID A STRUCTURE, AND ANTIBIOTIC
RP RESISTANCE.
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 FUNCTION, DISRUPTION PHENOTYPE, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=20657724; DOI=10.4248/ijos.09062;
RA Coats S.R., To T.T., Jain S., Braham P.H., Darveau R.P.;
RT "Porphyromonas gingivalis resistance to polymyxin B is determined by the
RT lipid A 4'-phosphatase, PGN_0524.";
RL Int. J. Oral Sci. 1:126-135(2009).
RN [4]
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 4'-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 allows it to
CC camouflage itself from the host innate immune response
CC (PubMed:19552698, PubMed:20657724). Removal of the 4'-phosphate may be
CC required to generate the substrate for deacylation of the pentaacyl
CC lipid A to the tetraccylated lipid A species (PubMed:19552698).
CC {ECO:0000269|PubMed:19552698, ECO:0000269|PubMed:20657724}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:A0Q4N6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No longer responds to changes in hemin, decreased
CC removal of 4'-phosphate from lipid A species. Accumulates pentaacylated
CC 4'-phosphate lipid A with concomitant loss of the usual non-
CC phosphorylated tetraacylated lipid A. Lipopolysaccharide (LPS) or
CC bacteria from this strain are a somewhat potent inducer of the human
CC innate immune response via Toll-like receptor 4 (TLR4) in cultured
CC HEK293 cells; double lpxE-lpxF mutants are more potent. Loss of
CC resistance to the cationic antimicrobial peptide (CAMP) polymyxin B.
CC Double lpxE-lpxF mutants accumulate multiple mono- and bi-
CC phosphorylated lipid A species (PubMed:19552698, PubMed:20657724).
CC Unable to colonize rabbit periodontium, a model for periodontal disease
CC (PubMed:24478080). {ECO:0000269|PubMed:19552698,
CC ECO:0000269|PubMed:20657724, 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}.
CC -!- SIMILARITY: Belongs to the lipid A LpxF 4'-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AP009380; BAG33043.1; -; Genomic_DNA.
DR AlphaFoldDB; B2RI48; -.
DR STRING; 431947.PGN_0524; -.
DR EnsemblBacteria; BAG33043; BAG33043; PGN_0524.
DR KEGG; pgn:PGN_0524; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_072573_10_0_10; -.
DR OMA; FYSAHAS; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000008842; 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 SMART; SM00014; acidPPc; 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..236
FT /note="Lipid A 4'-phosphatase"
FT /id="PRO_0000432499"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
SQ SEQUENCE 236 AA; 27362 MW; B10E4E5A73B2D105 CRC64;
MEYILEVERN LFLTLNGVQH PLLDGFFYLI SAKWTWVIMS IAFLFFLFYK KPTKEALFIV
GAVLLSVLIC DQLSSSFFKP FFARFRPSHH PDFIDYVKTV YGYRGGKYGF ISGHTTNYIS
LALFTSRIFR NKFYTWTIWS VVALVIYSRI YIGVHFITDI IPGIAVGLIV GHFVYKVYLY
ARSRWLGASC PAHPSAVYAG DSIRLWTLSL IGFVFAMLCM SRQLTEILQY YVFLLF
