AC MF_00837; DC Protein; auto TR HAMAP; MF_00837; -; 1; level=0 XX Names: PagP_transferase XX ID PAGP case DE RecName: Full=Lipid A palmitoyltransferase PagP; DE EC=2.3.1.251; else DE RecName: Full=Lipid A acyltransferase PagP; DE EC=2.3.1.251; end case DE AltName: Full=Lipid A acylation protein; DE Flags: Precursor; GN Name=pagP; XX case CC -!- FUNCTION: Transfers a palmitate residue from the sn-1 position of a CC phospholipid to the N-linked hydroxymyristate on the proximal unit of CC lipid A or its precursors. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid A CC (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid CC A; Xref=Rhea:RHEA:46864, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369, CC ChEBI:CHEBI:87048, ChEBI:CHEBI:134257; EC=2.3.1.251; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA CC = a 2-acyl-sn-glycero-3-phosphocholine + lipid IIB; CC Xref=Rhea:RHEA:46872, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369, CC ChEBI:CHEBI:86226, ChEBI:CHEBI:87058; EC=2.3.1.251; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA CC (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + lipid IVB (E. CC coli); Xref=Rhea:RHEA:46868, ChEBI:CHEBI:57875, ChEBI:CHEBI:58603, CC ChEBI:CHEBI:77369, ChEBI:CHEBI:87049; EC=2.3.1.251; else CC -!- FUNCTION: Transfers a fatty acid residue from the sn-1 position of a CC phospholipid to the N-linked hydroxyfatty acid chain on the proximal CC unit of lipid A or its precursors. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a lipid A = a 2- CC acyl-sn-glycero-3-phosphocholine + a hepta-acyl lipid A; CC Xref=Rhea:RHEA:74275, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, CC ChEBI:CHEBI:193141, ChEBI:CHEBI:193142; EC=2.3.1.251; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a lipid IIA = a 2- CC acyl-sn-glycero-3-phosphocholine + a lipid IIB; Xref=Rhea:RHEA:74283, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, ChEBI:CHEBI:193144, CC ChEBI:CHEBI:193145; EC=2.3.1.251; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a lipid IVA = a 2- CC acyl-sn-glycero-3-phosphocholine + a lipid IVB; Xref=Rhea:RHEA:74279, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, ChEBI:CHEBI:176425, CC ChEBI:CHEBI:193143; EC=2.3.1.251; end case CC -!- SUBUNIT: Homodimer. case CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. end case case not CC -!- SUBCELLULAR LOCATION: Cell outer membrane. end case CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family. XX DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 0-1; trigger=yes DR Pfam; PF07017; PagP; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX KW Acyltransferase KW Cell outer membrane KW Membrane KW Signal KW Transferase XX case GO GO:0016416; F:O-palmitoyltransferase activity else GO GO:0016746; F:acyltransferase activity end case GO GO:0009245; P:lipid A biosynthetic process XX FT From: PAGP_ECOLI (P37001) FT ACT_SITE 58 FT Condition: H FT ACT_SITE 101 FT Condition: D FT ACT_SITE 102 FT Condition: S FT SITE 67 FT /note="Role in lipopolysaccharide recognition" FT Condition: K FT SITE 172 FT /note="Role in the phospholipid gating" FT Condition: Y XX Size: 160-240; Related: None; Template: P37001; Q8XBR9; Q8ZR06; Q7WFT9; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.11 2023/01/26 //