ID   LPXL_ECO57              Reviewed;         306 AA.
AC   P0ACV1; P24187;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Lipid A biosynthesis lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942};
DE            EC=2.3.1.241 {ECO:0000255|HAMAP-Rule:MF_01942};
DE   AltName: Full=Kdo(2)-lipid IV(A) lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942};
GN   Name=lpxL {ECO:0000255|HAMAP-Rule:MF_01942}; Synonyms=htrB, waaM;
GN   OrderedLocusNames=Z1690, ECs1432;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the transfer of laurate from lauroyl-acyl carrier
CC       protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid
CC       IV(A). {ECO:0000255|HAMAP-Rule:MF_01942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + dodecanoyl-[ACP]
CC         = dodecanoyl-(Kdo)2-lipid IVA + holo-[ACP]; Xref=Rhea:RHEA:28442,
CC         Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:60365,
CC         ChEBI:CHEBI:61524, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264;
CC         EC=2.3.1.241; Evidence={ECO:0000255|HAMAP-Rule:MF_01942};
CC   -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-
CC       lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step
CC       3/4. {ECO:0000255|HAMAP-Rule:MF_01942}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01942}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01942}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01942}.
CC   -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01942}.
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DR   EMBL; AE005174; AAG55800.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34855.1; -; Genomic_DNA.
DR   PIR; D85667; D85667.
DR   PIR; H90807; H90807.
DR   RefSeq; NP_309459.1; NC_002695.1.
DR   RefSeq; WP_000183364.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0ACV1; -.
DR   SMR; P0ACV1; -.
DR   STRING; 155864.EDL933_1630; -.
DR   EnsemblBacteria; AAG55800; AAG55800; Z1690.
DR   EnsemblBacteria; BAB34855; BAB34855; ECs_1432.
DR   GeneID; 66670679; -.
DR   GeneID; 912457; -.
DR   KEGG; ece:Z1690; -.
DR   KEGG; ecs:ECs_1432; -.
DR   PATRIC; fig|386585.9.peg.1533; -.
DR   eggNOG; COG1560; Bacteria.
DR   HOGENOM; CLU_049421_1_1_6; -.
DR   OMA; WRIERWF; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00360; UER00485.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008913; F:lauroyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07984; LPLAT_LABLAT-like; 1.
DR   HAMAP; MF_01942; Lipid_A_LpxL_LpxP; 1.
DR   InterPro; IPR004960; LipA_acyltrans.
DR   InterPro; IPR011920; Lipid_A_LpxL_LpxP.
DR   PANTHER; PTHR30606; PTHR30606; 1.
DR   Pfam; PF03279; Lip_A_acyltrans; 1.
DR   PIRSF; PIRSF026649; MsbB; 1.
DR   TIGRFAMs; TIGR02207; lipid_A_htrB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW   Stress response; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..306
FT                   /note="Lipid A biosynthesis lauroyltransferase"
FT                   /id="PRO_0000201775"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01942"
FT   MOTIF           132..137
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01942"
SQ   SEQUENCE   306 AA;  35407 MW;  AEA70A5EB10653B5 CRC64;
     MTNLPKFSTA LLHPRYWLTW LGIGVLWLVV QLPYPVIYRL GCGLGKLALR FMKRRAKIVH
     RNLELCFPEM SEQERRKMVV KNFESVGMGL METGMAWFWP DRRIARWTEV IGMEHIRDVQ
     AQKRGILLVG IHFLTLELGA RQFGMQEPGI GVYRPNDNPL IDWLQTWGRL RSNKSMLDRK
     DLKGMIKALK KGEVVWYAPD HDYGPRSSVF VPLFAVEQAA TTTGTWMLAR MSGACLVPFV
     PRRKPDGKGY QLIMLPPECS PPLDDAETTA AWMNKVVEKC IMMAPEQYMW LHRRFKTRPE
     GVPSRY