AC   MF_01942;
DC   Protein; auto
TR   HAMAP; MF_01942; -; 1; level=0
XX
Names: Lipid_A_LpxL_LpxP
XX
ID   LPXL
case <OC:Escherichia>
DE   RecName: Full=Lipid A biosynthesis lauroyltransferase;
DE            EC=2.3.1.241;
DE   AltName: Full=Kdo(2)-lipid IV(A) lauroyltransferase;
else
DE   RecName: Full=Lipid A biosynthesis acyltransferase;
DE            EC=2.3.1.241;
DE   AltName: Full=Kdo(2)-lipid IV(A) acyltransferase;
end case
GN   Name=lpxL;
XX
case <OC:Escherichia>
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA (E. coli) +
CC         dodecanoyl-[ACP] = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-
CC         lipid IVA (E. coli) + holo-[ACP]; Xref=Rhea:RHEA:28442, Rhea:RHEA-
CC         COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:60365, ChEBI:CHEBI:61524,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:65264; EC=2.3.1.241;
else
CC   -!- FUNCTION: Catalyzes the transfer of an acyl chain from an acyl-[acyl-
CC       carrier-protein] (ACP) to a Kdo(2)-lipid IV(A) to form a Kdo(2)-(acyl)-
CC       lipid IV(A).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-
CC         lipid IVA = an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)-lipid IVA +
CC         holo-[ACP]; Xref=Rhea:RHEA:69396, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:14125, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651,
CC         ChEBI:CHEBI:176429, ChEBI:CHEBI:176430; EC=2.3.1.241;
end case
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.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family.
XX
DR   Pfam; PF03279; Lip_A_acyltrans; 1; trigger=no
DR   NCBIfam; TIGR02207; lipid_A_htrB; 1; trigger=no
DR   PIRSF; PIRSF026649; MsbB; 1; trigger=no
DR   General; Transmembrane; -; 1; trigger=yes
XX
KW   Acyltransferase
KW   Cell inner membrane
KW   Cell membrane
KW   Lipopolysaccharide biosynthesis
KW   Membrane
KW   Transferase
KW   Transmembrane
KW   Transmembrane helix
XX
case <OC:Escherichia>
GO   GO:0008913; F:lauroyltransferase activity
else
GO   GO:0016746; F:acyltransferase activity
end case
GO   GO:0036104; P:Kdo2-lipid A biosynthetic process
GO   GO:0005886; C:plasma membrane
XX
FT   From: LPXL_ECOLI (P0ACV0)
FT   MOTIF           132..137
FT                   /note="HXXXXD motif"
FT   Condition: H-x-x-x-x-[DE]
XX
Size: 260-360;
Related: MF_01943!;
Template: P0ACV0;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: The associated profile (MF_01942) matches LpxL and LpxP, but the annotation rule is specific for LpxL.
 See MF_01943 for LpxP annotation.
XX
# Revision 1.8 2023/06/01
//