PAGP_LEGPN
ID PAGP_LEGPN Reviewed; 186 AA.
AC Q93K12;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Lipid A palmitoyltransferase PagP {ECO:0000255|HAMAP-Rule:MF_00837};
DE EC=2.3.1.251 {ECO:0000255|HAMAP-Rule:MF_00837};
DE AltName: Full=Lipid A acylation protein {ECO:0000255|HAMAP-Rule:MF_00837};
DE Flags: Precursor;
GN Name=pagP {ECO:0000255|HAMAP-Rule:MF_00837};
GN Synonyms=rcp {ECO:0000303|PubMed:11401964};
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=130b / Wadsworth / Serogroup 1;
RX PubMed=8641790; DOI=10.1128/iai.64.3.842-848.1996;
RA O'Connell W.A., Hickey E.K., Cianciotto N.P.;
RT "A Legionella pneumophila gene that promotes hemin binding.";
RL Infect. Immun. 64:842-848(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN CAMP RESISTANCE,
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RC STRAIN=130b / Wadsworth / Serogroup 1;
RX PubMed=11401964; DOI=10.1128/iai.69.7.4276-4286.2001;
RA Robey M., O'Connell W., Cianciotto N.P.;
RT "Identification of Legionella pneumophila rcp, a pagP-like gene that
RT confers resistance to cationic antimicrobial peptides and promotes
RT intracellular infection.";
RL Infect. Immun. 69:4276-4286(2001).
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 (By similarity). Confers resistance to
CC cationic antimicrobial peptides (CAMPs). Promotes the ability of
CC L.pneumophila to replicate and/or survive in macrophages. Important for
CC ability to kill macrophages and to promote the virulence
CC (PubMed:11401964). {ECO:0000255|HAMAP-Rule:MF_00837,
CC ECO:0000269|PubMed:11401964}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
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;
CC Xref=Rhea:RHEA:46868, ChEBI:CHEBI:57875, ChEBI:CHEBI:58603,
CC ChEBI:CHEBI:77369, ChEBI:CHEBI:87049; EC=2.3.1.251;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00837};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00837}.
CC -!- DISRUPTION PHENOTYPE: Mutant is impaired in stationary-phase survival
CC in low-Mg(2+) medium and shows decreased resistance to different
CC structural classes of CAMPs compared to the wild type. Mutations reduce
CC both the numbers of bacteria recovered during intracellular infection
CC and their cytopathic capacity for U937 macrophages. The mutant is also
CC more defective for lung colonization of A/J mice.
CC {ECO:0000269|PubMed:11401964}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43385; AAK52070.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93K12; -.
DR SMR; Q93K12; -.
DR STRING; 91892.BIZ52_00125; -.
DR GO; GO:0009279; C:cell outer membrane; ISS:UniProtKB.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; ISS:UniProtKB.
DR HAMAP; MF_00837; PagP_transferase; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR009746; Peptid-resist/lipidA_acyl_PagP.
DR Pfam; PF07017; PagP; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell outer membrane; Membrane; Signal; Transferase;
KW Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 20..186
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414458"
FT ACT_SITE 60
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 103
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 69
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 186 AA; 20673 MW; 1B67C4906D738DDE CRC64;
MKRLISCLTI ICALNRSAAA ETTSSPCSRW ISLLKPVCQR IHQTWTEGHD DMYFSGYAWH
NRYTYRPEKI KSYNEAAWGG GLGKSLFDEK GNWHGLYAIA FLDSHRHIEP AVGYAYLKTA
SVNKDIKAGL GYSVLVTSRV DYDNVPFPGA LPWVALFYKR TTVAATYIPG SAGAGNVLYI
LGKISL
