ID   PAGP_LEGLN              Reviewed;         231 AA.
AC   D3HNB4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=LLO_0052;
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150;
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H.J., Sansom F.M., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E.L., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(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}.
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; FN650140; CBJ10376.1; -; Genomic_DNA.
DR   RefSeq; WP_003633776.1; NC_013861.1.
DR   AlphaFoldDB; D3HNB4; -.
DR   SMR; D3HNB4; -.
DR   STRING; 661367.LLO_0052; -.
DR   EnsemblBacteria; CBJ10376; CBJ10376; LLO_0052.
DR   KEGG; llo:LLO_0052; -.
DR   eggNOG; ENOG502Z7SY; Bacteria.
DR   HOGENOM; CLU_104099_0_1_6; -.
DR   OMA; AQTWNEP; -.
DR   OrthoDB; 1171115at2; -.
DR   Proteomes; UP000001060; 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..231
FT                   /note="Lipid A palmitoyltransferase PagP"
FT                   /id="PRO_0000414457"
FT   REGION          24..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ   SEQUENCE   231 AA;  25895 MW;  AE4485A8D87FEE3E CRC64;
     MNKLTVRNFI VGLLIVFSLN SFSSPPSISN SSSNSIDENS PINTFKISPD NQTSKKSDLA
     TEEPKGCKYW LSLFKPVCHR LHQVWTEGHT DLYLSGYAWH NRFTYSAERI REKKYNELAW
     GGGLGKGFFD EKGNWHGLYA FAFLDSHRNV EPTAGYAYLR VANITKEFKA GLGFSVLVTA
     RPDIFHNIPF PGAVPWAGIF YKKLSVKAAY IPGSSTNGNV LYVVGTYSFD K