ID   LPXE_RHIL3              Reviewed;         244 AA.
AC   Q1MA49; Q6UEE4;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Lipid A 1-phosphatase {ECO:0000303|PubMed:12869541};
DE            EC=3.1.-.- {ECO:0000305};
GN   Name=lpxE {ECO:0000303|PubMed:12869541}; OrderedLocusNames=RL4708;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY,
RP   PATHWAY, SUBCELLULAR LOCATION, AND EXPRESSION IN E.COLI AND S.MELILOTI
RP   1021.
RC   STRAIN=3841;
RX   PubMed=12869541; DOI=10.1074/jbc.m305830200;
RA   Karbarz M.J., Kalb S.R., Cotter R.J., Raetz C.R.;
RT   "Expression cloning and biochemical characterization of a Rhizobium
RT   leguminosarum lipid A 1-phosphatase.";
RL   J. Biol. Chem. 278:39269-39279(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
RN   [3]
RP   LIPID A STRUCTURE.
RC   STRAIN=3841;
RX   PubMed=16513742; DOI=10.1128/jb.188.6.2126-2133.2006;
RA   Vedam V., Kannenberg E., Datta A., Brown D., Haynes-Gann J.G.,
RA   Sherrier D.J., Carlson R.W.;
RT   "The pea nodule environment restores the ability of a Rhizobium
RT   leguminosarum lipopolysaccharide acpXL mutant to add 27-hydroxyoctacosanoic
RT   acid to its lipid A.";
RL   J. Bacteriol. 188:2126-2133(2006).
CC   -!- FUNCTION: Removes the 1-phosphate group from (tetraacyl) lipid A
CC       species, has no requirement for the Kdo(2) moiety of lipid A. Has no
CC       4'-phosphatase activity. Reduces sensitivity of S.meliloti strain 1021
CC       to the cationic antimicrobial peptide (CAMP) polymyxin B.
CC       {ECO:0000269|PubMed:12869541}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000305|PubMed:12869541}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:12869541}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- MISCELLANEOUS: In this strain lipid A lacks phosphate groups, and both
CC       tetra- and pentaacylated species exist. {ECO:0000269|PubMed:16513742,
CC       ECO:0000305|PubMed:12869541}.
CC   -!- SIMILARITY: Belongs to the lipid A LpxE 1-phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AY371492; AAQ72478.1; -; Genomic_DNA.
DR   EMBL; AM236080; CAK10191.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1MA49; -.
DR   SMR; Q1MA49; -.
DR   STRING; 216596.RL4708; -.
DR   EnsemblBacteria; CAK10191; CAK10191; RL4708.
DR   KEGG; rle:RL4708; -.
DR   eggNOG; COG0671; Bacteria.
DR   HOGENOM; CLU_072573_6_0_5; -.
DR   OMA; VSWIGAY; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000006575; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
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   Cell inner membrane; Cell membrane; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..244
FT                   /note="Lipid A 1-phosphatase"
FT                   /id="PRO_0000432493"
FT   TRANSMEM        28..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   244 AA;  26990 MW;  DD24EEE9B90C0A4E CRC64;
     MRAFWASLDR RWRRSGVGMP PLRWQACLFV TLNAVILSML LFDAPIGASK APAPVKHLGE
     LLTGFGDSAW LIYTSILLFF QGRAGYKLLK TARSKAQALY VSWIGAYLFF TVVFSGLLAN
     LLKRAIGRAR PDHFHDYGMF SFAPFSGHSA FESFPSGHST TVGAFFAAFA LLFPRYRVAF
     IACAIWLGMT RVMVGAHYPS DVIAGLAFGA WFSLLTAIVF ARCGLLFKLA PDGWPLAKRL
     FRTA