LPXT_ECOLI
ID LPXT_ECOLI Reviewed; 237 AA.
AC P76445; Q2MAR1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Lipid A 1-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000305};
DE EC=2.7.4.29 {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000269|PubMed:18047581};
DE AltName: Full=Kdo(2)-lipid A phosphotransferase {ECO:0000305};
DE AltName: Full=Undecaprenyl pyrophosphate:lipid A 1-phosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000305};
GN Name=lpxT {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000303|PubMed:18047581};
GN Synonyms=yeiU; OrderedLocusNames=b2174, JW2162;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [4]
RP FUNCTION AS AN UNDECAPRENYL-PYROPHOSPHATE PHOSPHATASE, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17660416; DOI=10.1099/mic.0.2007/006312-0;
RA Tatar L.D., Marolda C.L., Polischuk A.N., van Leeuwen D., Valvano M.A.;
RT "An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in
RT undecaprenyl phosphate recycling.";
RL Microbiology 153:2518-2529(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18047581; DOI=10.1111/j.1365-2958.2007.06044.x;
RA Touze T., Tran A.X., Hankins J.V., Mengin-Lecreulx D., Trent M.S.;
RT "Periplasmic phosphorylation of lipid A is linked to the synthesis of
RT undecaprenyl phosphate.";
RL Mol. Microbiol. 67:264-277(2008).
RN [6]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-190.
RX PubMed=20384697; DOI=10.1111/j.1365-2958.2010.07150.x;
RA Herrera C.M., Hankins J.V., Trent M.S.;
RT "Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A
RT promoting resistance to antimicrobial peptides.";
RL Mol. Microbiol. 76:1444-1460(2010).
CC -!- FUNCTION: Involved in the modification of the lipid A domain of
CC lipopolysaccharides (LPS). Transfers a phosphate group from
CC undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1-
CC diphosphate. Contributes to the recycling of undecaprenyl phosphate
CC (C55-P) (PubMed:18047581). In vitro, has low undecaprenyl-diphosphate
CC phosphatase activity (PubMed:17660416). {ECO:0000269|PubMed:17660416,
CC ECO:0000269|PubMed:18047581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + di-trans,octa-cis-
CC undecaprenyl diphosphate = (Kdo)2-lipid A 1-diphosphate + di-
CC trans,octa-cis-undecaprenyl phosphate; Xref=Rhea:RHEA:45468,
CC ChEBI:CHEBI:58405, ChEBI:CHEBI:58540, ChEBI:CHEBI:60392,
CC ChEBI:CHEBI:85271; EC=2.7.4.29; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01945, ECO:0000269|PubMed:18047581};
CC -!- ACTIVITY REGULATION: Inhibited by BasR. This regulation does not occur
CC at the level of transcription, but rather following the assembly of
CC LpxT into the inner membrane. {ECO:0000269|PubMed:20384697}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Significant activity is observed from pH 5.5 to pH
CC 7.5. {ECO:0000269|PubMed:18047581};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01945,
CC ECO:0000269|PubMed:18047581}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01945, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:17660416}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000269|PubMed:17660416}.
CC Note=Transferase activity takes place on the periplamic side of the
CC inner membrane. {ECO:0000255|HAMAP-Rule:MF_01945,
CC ECO:0000269|PubMed:18047581}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in the production of
CC LPS containing only the bis-phosphorylated lipid A species.
CC {ECO:0000269|PubMed:18047581}.
CC -!- MISCELLANEOUS: In E.coli, lipid A contains typically a monophosphate
CC unit at positions 1 and 4' (bis-phosphorylated lipid A). However, one-
CC third of the lipid A contains an unsubstituted diphosphate unit at
CC position 1 (lipid A 1-diphosphate). {ECO:0000305|PubMed:18047581}.
CC -!- SIMILARITY: Belongs to the LpxT phosphotransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000305}.
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DR EMBL; U00096; AAC75235.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76645.1; -; Genomic_DNA.
DR RefSeq; NP_416679.4; NC_000913.3.
DR RefSeq; WP_000594599.1; NZ_LN832404.1.
DR AlphaFoldDB; P76445; -.
DR SMR; P76445; -.
DR BioGRID; 4260460; 4.
DR STRING; 511145.b2174; -.
DR jPOST; P76445; -.
DR PaxDb; P76445; -.
DR PRIDE; P76445; -.
DR EnsemblBacteria; AAC75235; AAC75235; b2174.
DR EnsemblBacteria; BAE76645; BAE76645; BAE76645.
DR GeneID; 66673929; -.
DR GeneID; 946693; -.
DR KEGG; ecj:JW2162; -.
DR KEGG; eco:b2174; -.
DR PATRIC; fig|1411691.4.peg.62; -.
DR EchoBASE; EB3828; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_102925_0_0_6; -.
DR InParanoid; P76445; -.
DR OMA; RSFPGDH; -.
DR PhylomeDB; P76445; -.
DR BioCyc; EcoCyc:G7146-MON; -.
DR BioCyc; MetaCyc:G7146-MON; -.
DR BRENDA; 2.7.4.29; 2026.
DR UniPathway; UPA00030; -.
DR PRO; PR:P76445; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IDA:EcoCyc.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IDA:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01945; Lipid_A_LpxT; 1.
DR InterPro; IPR032908; LpxT.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..237
FT /note="Lipid A 1-diphosphate synthase"
FT /id="PRO_0000169160"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17660416"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01945"
FT TOPO_DOM 27..62
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17660416"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01945"
FT TOPO_DOM 84..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17660416"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01945"
FT TOPO_DOM 112..145
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17660416"
FT TOPO_DOM 167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17660416"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01945"
FT TOPO_DOM 189..194
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17660416"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01945"
FT TOPO_DOM 216..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:17660416"
FT MUTAGEN 190
FT /note="H->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:20384697"
SQ SEQUENCE 237 AA; 26759 MW; A27F9560A1417D09 CRC64;
MIKNLPQIVL LNIVGLALFL SWYIPVNHGF WLPIDADIFY FFNQKLVESK AFLWLVALTN
NRAFDGCSLL AMGMLMLSFW LKENAPGRRR IVIIGLVMLL TAVVLNQLGQ ALIPVKRASP
TLTFTDINRV SELLSVPTKD ASRDSFPGDH GMMLLIFSAF MWRYFGKVAG LIALIIFVVF
AFPRVMIGAH WFTDIIVGSM TVILIGLPWV LLTPLSDRLI TFFDKSLPGK NKHFQNK
