ID   PAGP_ERWAC              Reviewed;         189 AA.
AC   D4HYT3;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   25-MAY-2022, entry version 54.
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}; Synonyms=crcA;
GN   OrderedLocusNames=EAMY_1108;
OS   Erwinia amylovora (strain CFBP1430).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=665029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP1430;
RX   PubMed=20192826; DOI=10.1094/mpmi-23-4-0384;
RA   Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT   CFBP 1430 and comparison to other Erwinia spp.";
RL   Mol. Plant Microbe Interact. 23:384-393(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, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBA20058.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN434113; CBA20058.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_013035937.1; NC_013961.1.
DR   AlphaFoldDB; D4HYT3; -.
DR   SMR; D4HYT3; -.
DR   STRING; 665029.EAMY_1108; -.
DR   EnsemblBacteria; CBA20058; CBA20058; EAMY_1108.
DR   GeneID; 8911472; -.
DR   KEGG; eam:EAMY_1108; -.
DR   eggNOG; ENOG502Z7SY; Bacteria.
DR   HOGENOM; CLU_104099_0_0_6; -.
DR   OrthoDB; 1171115at2; -.
DR   Proteomes; UP000001841; Chromosome.
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_0000414443"
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