ID E6WG34_PANSA Unreviewed; 235 AA.
AC E6WG34;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 OrderedLocusNames=Pat9b_2658 {ECO:0000313|EMBL:ADU69958.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU69958.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU69958.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU69958.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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 -!- 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; CP002433; ADU69958.1; -; Genomic_DNA.
DR RefSeq; WP_013509813.1; NC_014837.1.
DR AlphaFoldDB; E6WG34; -.
DR STRING; 592316.Pat9b_2658; -.
DR KEGG; pao:Pat9b_2658; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_102925_0_0_6; -.
DR OrthoDB; 8477781at2; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000001624; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 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 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..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 53..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01945"
FT TRANSMEM 152..179
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 95..210
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 235 AA; 26657 MW; 9C05017ED56A5CB4 CRC64;
MRASRLFTIL LLNVLGVVIF FSWYLPPDHG FWFGLDKAIF FGFNDQMVVH HGFAILVAIT
NFRGFDLVSL LAMGLLYLWF WRRETPPGRR RMLAIGITML LTAVVLNQLG HLLPVQHVSP
TLFFENVHRV SELTGIPAKD ASSNSFPGDH GMMLIIFACF MWRYFGFRPF LLGLVIVVVF
GLPRVMAGAH WFTDIAVGSL SVVLVGLSWW LLTPASDKLV NWLYRTLPGK YKPQA
//
