ID   PAGP_PECPW              Reviewed;         209 AA.
AC   D0KD36;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=Pecwa_4360;
OS   Pectobacterium parmentieri (strain WPP163) (Pectobacterium wasabiae (strain
OS   WPP163)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WPP163;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium wasabiae WPP163.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001790; ACX90052.1; -; Genomic_DNA.
DR   RefSeq; WP_014701937.1; NC_013421.1.
DR   AlphaFoldDB; D0KD36; -.
DR   SMR; D0KD36; -.
DR   GeneID; 66804737; -.
DR   KEGG; pwa:Pecwa_4360; -.
DR   eggNOG; ENOG502Z7SY; Bacteria.
DR   HOGENOM; CLU_104099_0_0_6; -.
DR   OMA; AQTWNEP; -.
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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   CHAIN           25..209
FT                   /note="Lipid A palmitoyltransferase PagP"
FT                   /id="PRO_0000414467"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   SITE            90
FT                   /note="Role in lipopolysaccharide recognition"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   SITE            195
FT                   /note="Role in the phospholipid gating"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ   SEQUENCE   209 AA;  24236 MW;  5068FB59C7999D04 CRC64;
     MHLKRALITL SLITLPIIPF SSYAVESINN TGSMESPASV AADSTSNKQD ESWWQRSKHN
     LSATWNTSQS HDIYIPAITW HNRWTYDKEK TDKYNERPWG AGYGVSRLDQ DGDWHGLYIM
     AFKDSFNKWE PIGGYGYEKR WRPTHDQDFQ LGLGFTAGFT MRDNWNYIPI PVLLPLASIS
     YSKLSFQATY IPGTYNNGNV FFAWFRWQI