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HAMAP rule MF_00837

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_00837
Accession MF_00837
Dates 26-OCT-2011 (Created)
3-SEP-2024 (Last updated, Version 13)
Name PagP_transferase
Scope(s) Bacteria
Pseudomonadota
Template(s) P37001 (PAGP_ECOLI); Q8XBR9 (PAGP_ECO57); Q8ZR06 (PAGP_SALTY); Q7WFT9 (PAGP_BORBR); [ Recover all ]
Triggered by HAMAP; MF_00837 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PAGP
case <OC:Escherichia>
Protein name RecName: Full=Lipid A palmitoyltransferase PagP;
                 EC=2.3.1.251;
else
Protein name RecName: Full=Lipid A acyltransferase PagP;
                 EC=2.3.1.251;
end case
Protein name AltName: Full=Lipid A acylation protein;
                 Flags: Precursor;
Gene name Name=pagP;

Comments [?]

case <OC:Escherichia>
FUNCTIONTransfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
CATALYTIC ACTIVITY Reaction=lipid A (E. coli) + a 1-hexadecanoyl-2-acyl-sn-glycero-3- phosphocholine = hepta-acyl lipid A (E. coli) + a 2-acyl-sn-glycero- 3-phosphocholine; Xref=Rhea:RHEA:46864, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369, ChEBI:CHEBI:87048, ChEBI:CHEBI:134257; EC=2.3.1.251;
CATALYTIC ACTIVITY Reaction=lipid IIA + a 1-hexadecanoyl-2-acyl-sn-glycero-3- phosphocholine = lipid IIB + a 2-acyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:46872, ChEBI:CHEBI:57875, ChEBI:CHEBI:77369, ChEBI:CHEBI:86226, ChEBI:CHEBI:87058; EC=2.3.1.251;
CATALYTIC ACTIVITY Reaction=lipid IVA (E. coli) + a 1-hexadecanoyl-2-acyl-sn-glycero-3- phosphocholine = lipid IVB (E. coli) + a 2-acyl-sn-glycero-3- phosphocholine; Xref=Rhea:RHEA:46868, ChEBI:CHEBI:57875, ChEBI:CHEBI:58603, ChEBI:CHEBI:77369, ChEBI:CHEBI:87049; EC=2.3.1.251;
else
FUNCTIONTransfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors.
CATALYTIC ACTIVITY Reaction=a lipid A + a 1,2-diacyl-sn-glycero-3-phosphocholine = a hepta-acyl lipid A + a 2-acyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:74275, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, ChEBI:CHEBI:193141, ChEBI:CHEBI:193142; EC=2.3.1.251;
CATALYTIC ACTIVITY Reaction=a lipid IIA + a 1,2-diacyl-sn-glycero-3-phosphocholine = a lipid IIB + a 2-acyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:74283, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, ChEBI:CHEBI:193144, ChEBI:CHEBI:193145; EC=2.3.1.251;
CATALYTIC ACTIVITY Reaction=a lipid IVA + a 1,2-diacyl-sn-glycero-3-phosphocholine = a lipid IVB + a 2-acyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:74279, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875, ChEBI:CHEBI:176425, ChEBI:CHEBI:193143; EC=2.3.1.251;
end case
SUBUNITHomodimer.
case <Feature:PS51257>
SUBCELLULAR LOCATIONCell outer membrane; Lipid-anchor.
end case
case not <Feature:PS51257>
SUBCELLULAR LOCATIONCell outer membrane.
end case
SIMILARITYBelongs to the lipid A palmitoyltransferase family.

Keywords [?]

Acyltransferase
Cell outer membrane
Membrane
Signal
Transferase

Gene Ontology [?]

case <OCellular component:Escherichia>
GO:0016416; Molecular function:O-palmitoyltransferase activity
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0016746; Molecular function:acyltransferase activity
end case
GO:0009245; Biological process:lipid A biosynthetic process

Cross-references [?]

PROSITE PS51257; PROKAR_LIPOPROTEIN; 0-1;
Pfam PF07017; PagP; 1;
General Signal; -; 1;

Features [?]

From: PAGP_ECOLI (P37001)
Key From To Description Tag Condition FTGroup
ACT_SITE 58 58 H
ACT_SITE 101 101 D
ACT_SITE 102 102 S
SITE 67 67 /note="Role in lipopolysaccharide recognition" K
SITE 172 172 /note="Role in the phospholipid gating" Y

Additional information [?]

Size range 160-240 amino acids
Related rules None
Fusion Nter: None Cter: None



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