ID B7N5D8_ECOLU Unreviewed; 237 AA.
AC B7N5D8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=yeiU {ECO:0000313|EMBL:CAR13697.1};
GN Synonyms=lpxT {ECO:0000256|HAMAP-Rule:MF_01945};
GN OrderedLocusNames=ECUMN_2511 {ECO:0000313|EMBL:CAR13697.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR13697.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) + di-
CC trans,octa-cis-undecaprenyl diphosphate = (Kdo)2-lipid A 1-
CC diphosphate + di-trans,octa-cis-undecaprenyl phosphate;
CC Xref=Rhea:RHEA:45468, ChEBI:CHEBI:58405, ChEBI:CHEBI:58540,
CC ChEBI:CHEBI:60392, ChEBI:CHEBI:85271; EC=2.7.4.29;
CC 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}.
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DR EMBL; CU928163; CAR13697.1; -; Genomic_DNA.
DR RefSeq; WP_001297918.1; NC_011751.1.
DR RefSeq; YP_002413225.1; NC_011751.1.
DR AlphaFoldDB; B7N5D8; -.
DR STRING; 585056.ECUMN_2511; -.
DR KEGG; eum:ECUMN_2511; -.
DR PATRIC; fig|585056.7.peg.2693; -.
DR HOGENOM; CLU_102925_0_0_6; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000007097; 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..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 237 AA; 26758 MW; 94A94E0D1797A661 CRC64;
MIKNLPQIVL LNIVGLALFL SWYIPVNHGF WLPIDADIFY FFNQKLVESK AFLWLVALTN
NRAFDGCSLL AMGMLMLSFW LKENAPGRRR IVIIGLVMLL TAVVLNQLGQ ALIPVKRASP
TLTFTNINRV SELLSVPTKD ASRDSFPGDH GMMLLIFSAF MWRYFGKVAG LIALIIFVVF
AFPRVMIGAH WFTDIIVGSM TVILIGLPWV LLTPLSDRLI TFFDKSLPGK NKHFQNK
//
