ID   LPXE_RHIEC              Reviewed;         232 AA.
AC   Q2K2U9;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Lipid A 1-phosphatase {ECO:0000303|PubMed:20153447};
DE            EC=3.1.-.- {ECO:0000305};
GN   Name=lpxE {ECO:0000303|PubMed:20153447}; OrderedLocusNames=RHE_CH04094;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND LIPID A STRUCTURE.
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=20153447; DOI=10.1016/j.bbalip.2010.02.001;
RA   Ingram B.O., Sohlenkamp C., Geiger O., Raetz C.R.;
RT   "Altered lipid A structures and polymyxin hypersensitivity of Rhizobium
RT   etli mutants lacking the LpxE and LpxF phosphatases.";
RL   Biochim. Biophys. Acta 1801:593-604(2010).
CC   -!- FUNCTION: Probably removes the 1-phosphate moiety from lipid A species.
CC       Does not seem to act on other membrane components, nor does it
CC       dephosphorylate the 4'-phosphate group of lipid A and/or lipid A
CC       precursors. {ECO:0000305|PubMed:20153447}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:O24866}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Lipid A contains a monophosphate group at
CC       position 1. Retains 4'-dephosphorylase activity on Kdo(2)-lipid IV(A).
CC       Increased sensitivity to the cationic antimicrobial peptide (CAMP)
CC       polymyxin B (PMB) but not other several other antibiotics. A double
CC       lpxE-lpxF mutant contains lipid A bi-phosphorylated at positions 1- and
CC       4'- and has greater sensitivity to PMB that either single mutant. No
CC       visible effect on free-living bacteria, or on nitrogen fixation upon
CC       nodulation of P.vulgaris. {ECO:0000269|PubMed:20153447}.
CC   -!- MISCELLANEOUS: In this strain lipid A lacks phosphate groups, instead
CC       contains a galacturonic acid moiety at position-4' in place of the
CC       monophosphate group found in E.coli. {ECO:0000305|PubMed:20153447}.
CC   -!- SIMILARITY: Belongs to the lipid A LpxE 1-phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000133; ABC92837.1; -; Genomic_DNA.
DR   RefSeq; WP_011427275.1; NC_007761.1.
DR   AlphaFoldDB; Q2K2U9; -.
DR   SMR; Q2K2U9; -.
DR   STRING; 347834.RHE_CH04094; -.
DR   EnsemblBacteria; ABC92837; ABC92837; RHE_CH04094.
DR   KEGG; ret:RHE_CH04094; -.
DR   eggNOG; COG0671; Bacteria.
DR   HOGENOM; CLU_072573_6_0_5; -.
DR   OMA; VSWIGAY; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001936; 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   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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..232
FT                   /note="Lipid A 1-phosphatase"
FT                   /id="PRO_0000432492"
FT   TRANSMEM        10..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   232 AA;  25297 MW;  C462E8AF0EDFA939 CRC64;
     MPPLRWQACL FITINAVALS MLLFDAPVGA SERPAAVKEL GELLTGFGDS AWLICISILL
     FFQGKAGYKL LKTARSKAQA LYVSWIGAYL FTTVVFSGLL ANLLKRAIGR ARPDHFHDYG
     MFSFTPFSGH AAFESFPSGH STTVGAFFAA FALLFPRYRV AFIACAIWLG MTRVMVGAHY
     PSDVIAGLAF GGWFSLLTAI VYARCGLLFK LAPDGWPLAK RLFPDIEKPG AL