ID A0A1Q5U8P7_9GAMM Unreviewed; 234 AA.
AC A0A1Q5U8P7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=Xentx_00501 {ECO:0000313|EMBL:OKP08829.1};
OS Xenorhabdus thuongxuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP08829.1, ECO:0000313|Proteomes:UP000186277};
RN [1] {ECO:0000313|EMBL:OKP08829.1, ECO:0000313|Proteomes:UP000186277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30TX1 {ECO:0000313|EMBL:OKP08829.1,
RC ECO:0000313|Proteomes:UP000186277};
RA Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp. nov.,
RT isolated from Steinernema species.";
RL Submitted (SEP-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKP08829.1}.
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DR EMBL; MKGR01000002; OKP08829.1; -; Genomic_DNA.
DR RefSeq; WP_074018695.1; NZ_MKGR01000002.1.
DR AlphaFoldDB; A0A1Q5U8P7; -.
DR OrthoDB; 8477781at2; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000186277; Unassembled WGS sequence.
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..110
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 92..210
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 234 AA; 26652 MW; 4923D5FD112B22CA CRC64;
MTRSHPLAIF ILNIFGIALF LSWYLPENHG FWFHIDSAIF YFFNEKLLPG SNFALFVAIA
NIRAFDIISL LCMGLLYYSA FRKQDYAGKR RLFMIGLVML ISAVIINQIG HQIPVSRPSP
TLTFENVNRI NEMTSWHTKD ASKDSFPGDH GLMLLIFSSF ILRYISRSAF CIALLIMVAF
ALPRIMAGAH WFTDIAVGSL SLTLIGMSWV LLTPLSDIMA TWLDKKLPHI RRDN
//