ID A0A285JTD2_9ENTR Unreviewed; 235 AA.
AC A0A285JTD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Lipid A 1-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01945};
DE EC=2.7.4.29 {ECO:0000256|HAMAP-Rule:MF_01945};
DE AltName: Full=Kdo(2)-lipid A phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01945};
DE AltName: Full=Undecaprenyl pyrophosphate:lipid A 1-phosphate phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01945};
GN Name=lpxT {ECO:0000256|HAMAP-Rule:MF_01945};
GN ORFNames=SAMN02744775_01003 {ECO:0000313|EMBL:SNY63538.1};
OS Enterobacter sp. CC120223-11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY63538.1, ECO:0000313|Proteomes:UP000219512};
RN [1] {ECO:0000313|EMBL:SNY63538.1, ECO:0000313|Proteomes:UP000219512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY63538.1,
RC ECO:0000313|Proteomes:UP000219512};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|HAMAP-Rule:MF_01945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + di-trans,octa-
CC cis-undecaprenyl diphosphate = an alpha-D-Kdo-(2->4)-alpha-D-Kdo-
CC (2->6)-lipid A 1-diphosphate + di-trans,octa-cis-undecaprenyl
CC phosphate; Xref=Rhea:RHEA:74291, ChEBI:CHEBI:58405,
CC ChEBI:CHEBI:60392, ChEBI:CHEBI:176431, ChEBI:CHEBI:193150;
CC EC=2.7.4.29; Evidence={ECO:0000256|HAMAP-Rule:MF_01945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00000759};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01945}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01945}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01945}. Note=Transferase activity takes place on the periplamic
CC side of the inner membrane. {ECO:0000256|HAMAP-Rule:MF_01945}.
CC -!- SIMILARITY: Belongs to the LpxT phosphotransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_01945}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OBEF01000003; SNY63538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285JTD2; -.
DR OrthoDB; 8477781at2; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000219512; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:InterPro.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01610; PAP2_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
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 PANTHER; PTHR14969:SF53; LIPID A 1-DIPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW Kinase {ECO:0000313|EMBL:SNY63538.1};
KW Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01945};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01945};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01945}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT DOMAIN 94..210
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 235 AA; 26469 MW; 652E2D598414CAFB CRC64;
MKTRLPLVLL LNIAGLALFM SWYLPANHGA WFGLDSGIFH FFNQGLADSR AYVWFLAITN
NRAFDGCSLL AMGCLMLSFW LKEDAQGRRR IIIIGLVMLL AAVIINQLAQ HLMPVKRASP
SLFFPDVYRV SDLLHISTKD ASKDSFPGDH GMMLLIFSTF MWRYFGLRAF IIALIISVVF
AFPRVMIGAH WFTDIAVGSL TAVLIGIPWI LLTPLSDKTI ALFDRYLPTT KSHKK
//
