ID   PAGP_PANAA              Reviewed;         190 AA.
AC   F2EP14;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-AUG-2022, entry version 50.
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=PAJ_0434;
OS   Pantoea ananatis (strain AJ13355).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=932677;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ13355;
RX   PubMed=22159605; DOI=10.1007/s00253-011-3713-5;
RA   Hara Y., Kadotani N., Izui H., Katashkina J.I., Kuvaeva T.M.,
RA   Andreeva I.G., Golubeva L.I., Malko D.B., Makeev V.J., Mashko S.V.,
RA   Kozlov Y.I.;
RT   "The complete genome sequence of Pantoea ananatis AJ13355, an organism with
RT   great biotechnological potential.";
RL   Appl. Microbiol. Biotechnol. 93:331-341(2012).
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=BAK10514.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP012032; BAK10514.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015700757.1; NC_017531.2.
DR   AlphaFoldDB; F2EP14; -.
DR   SMR; F2EP14; -.
DR   STRING; 932677.PAJ_0434; -.
DR   EnsemblBacteria; BAK10514; BAK10514; PAJ_0434.
DR   KEGG; paj:PAJ_0434; -.
DR   PATRIC; fig|932677.3.peg.505; -.
DR   eggNOG; ENOG502Z7SY; Bacteria.
DR   HOGENOM; CLU_104099_0_0_6; -.
DR   BioCyc; PANA932677:PAJ_RS02390-MON; -.
DR   Proteomes; UP000006690; 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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT   CHAIN           25..190
FT                   /note="Lipid A palmitoyltransferase PagP"
FT                   /id="PRO_0000414465"
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            176
FT                   /note="Role in the phospholipid gating"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ   SEQUENCE   190 AA;  22133 MW;  6DAD756562DD1DC5 CRC64;
     MNRYLLTTLS APLLALFFSF SLQAAMLSQE IKSGWDTFTG NVQQTWQQPD AIDVYVPAIT
     WHNRWTYDEE HIHRYNERPW GAGGGVSRYD EKGNWHGLYL MAFKDSFNKW EPFGGYGWEA
     TWRPLQDQNF HYGLGYTAGV TARHNWGYYP VPAILPLASI GYGSLNFQMT YIPGTYNNGN
     VYFAWLRWQF