LPXF_RHILE
ID LPXF_RHILE Reviewed; 233 AA.
AC Q1WDN2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Lipid A 4'-phosphatase {ECO:0000303|PubMed:16467300};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxF {ECO:0000303|PubMed:16467300};
OS Rhizobium leguminosarum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=384;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=16467300; DOI=10.1074/jbc.m600435200;
RA Wang X., McGrath S.C., Cotter R.J., Raetz C.R.;
RT "Expression cloning and periplasmic orientation of the Francisella novicida
RT lipid A 4'-phosphatase LpxF.";
RL J. Biol. Chem. 281:9321-9330(2006).
RN [2]
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 4'-phosphate moiety from lipid IV(A) (a
CC tetraacylated precursor of lipid A). {ECO:0000269|PubMed:16467300}.
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 -!- MISCELLANEOUS: In R.leguminosarum strain 3841 lipid A lacks phosphate
CC groups, and both tetra- and pentaacylated species exist; the same is
CC probably true of this strain. {ECO:0000269|PubMed:16513742,
CC ECO:0000305|PubMed:16467300}.
CC -!- SIMILARITY: Belongs to the lipid A LpxF 4'-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; DQ364144; ABC96320.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1WDN2; -.
DR SMR; Q1WDN2; -.
DR STRING; 936136.ARRT01000006_gene2597; -.
DR eggNOG; COG0671; Bacteria.
DR UniPathway; UPA00973; -.
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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..233
FT /note="Lipid A 4'-phosphatase"
FT /id="PRO_0000432498"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2..22
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..60
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..149
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..200
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 201..221
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 25479 MW; B6EF86B59ACA214F CRC64;
MLLFWMWWAL LAVFRAFPGI DIYFSQLFFV GADCDATAAA GNICGGFPYR DVAAFDLLRT
VFFRLPYVVA IVMVWKLVEC YQQHGATFNA ERAQKLKVAL GTLLIGPVLL VNVVLKEHWG
RPRPIQTDIF GGALHFAEAG SLAGKCVSNC SFVSGEAASA GWLFCLLLFV PKSLRYAVAA
PLAAISILTP AMRLSFGAHY LSDVVLGWLS SLVVFAALLA LTESQQHQKN SEI
