ID   PAGP_SODGM              Reviewed;         191 AA.
AC   Q2NSM3;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=SG1577;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE74852.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NSM3; -.
DR   SMR; Q2NSM3; -.
DR   STRING; 343509.SG1577; -.
DR   EnsemblBacteria; BAE74852; BAE74852; SG1577.
DR   KEGG; sgl:SG1577; -.
DR   eggNOG; ENOG502Z7SY; Bacteria.
DR   HOGENOM; CLU_104099_0_0_6; -.
DR   OMA; AQTWNEP; -.
DR   Proteomes; UP000001932; 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..191
FT                   /note="Lipid A palmitoyltransferase PagP"
FT                   /id="PRO_0000414478"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   SITE            177
FT                   /note="Role in the phospholipid gating"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ   SEQUENCE   191 AA;  22586 MW;  1DF5595422FB6EA3 CRC64;
     MRLFYQRISL LISLCGFFSA AWASDVQPAS STGLWQRFTQ NVAETWHHSP HQDLYVPAIT
     WHNRFTYDDE HIRRYNERPW GAGYGISRYD EKGNWHAIYL IAFKDSFNKW EPFGGYAWEK
     QWRPFDRYQD IHFGAGFTAG VTARDNWKYI PVPALLPLAS VGYKQLTFQA TYIPGTYNNG
     NVFFAWLRYR F