PAGP_ERWAE
ID PAGP_ERWAE Reviewed; 189 AA.
AC D4I8K8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
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}; OrderedLocusNames=EAM_1115;
OS Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=716540;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49946 / CCPPB 0273 / Ea273 / 27-3;
RX PubMed=20118253; DOI=10.1128/jb.00022-10;
RA Sebaihia M., Bocsanczy A.M., Biehl B.S., Quail M.A., Perna N.T.,
RA Glasner J.D., DeClerck G.A., Cartinhour S., Schneider D.J., Bentley S.D.,
RA Parkhill J., Beer S.V.;
RT "Complete genome sequence of the plant pathogen Erwinia amylovora strain
RT ATCC 49946.";
RL J. Bacteriol. 192:2020-2021(2010).
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. {ECO:0000255|HAMAP-Rule:MF_00837}.
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}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00837}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837}.
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DR EMBL; FN666575; CBJ45790.1; -; Genomic_DNA.
DR RefSeq; WP_013035937.1; NC_013971.1.
DR AlphaFoldDB; D4I8K8; -.
DR SMR; D4I8K8; -.
DR GeneID; 8911472; -.
DR KEGG; eay:EAM_1115; -.
DR PATRIC; fig|665029.3.peg.1085; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR BioCyc; EAMY716540:EAM_RS05400-MON; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Acyltransferase; Cell outer membrane; Membrane; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 24..189
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414442"
FT ACT_SITE 61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 105
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 70
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 175
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 189 AA; 21902 MW; EEBEE5ABFD416AD8 CRC64;
MKLKSVLYLL MLLNCLGLKS AHAATLVHGI STSWHSFSNS VSQTWNEPQT FDLYMPALTW
HNRWTYDADK IDRYNERPWG AGGGMSRYDE KGNWNGIYLM AFKDSFNKWE PIGGYGWEKT
WRPLNDPDFH FGLGYTAGVT MRDNWNYIPI PLLLPLASIG YGAANFQMTY IPGTYNNGNV
YFAWLRWQF
