PAGP_MUSP7
ID PAGP_MUSP7 Reviewed; 192 AA.
AC C6C6T1;
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}; OrderedLocusNames=Dd703_0182;
OS Musicola paradisiaca (strain Ech703) (Dickeya paradisiaca) (Dickeya
OS dadantii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Musicola.
OX NCBI_TaxID=579405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ech703;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Dickeya dadantii Ech703.";
RL Submitted (JUN-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACS84000.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001654; ACS84000.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C6C6T1; -.
DR SMR; C6C6T1; -.
DR STRING; 579405.Dd703_0182; -.
DR EnsemblBacteria; ACS84000; ACS84000; Dd703_0182.
DR KEGG; dda:Dd703_0182; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_6; -.
DR Proteomes; UP000002734; 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..192
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414435"
FT ACT_SITE 63
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 106
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 72
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 192 AA; 22590 MW; A594EF6AD5C317E1 CRC64;
MWLRFCAPAL MAWYWVFFPS TSQAATMEND GQDGFWQRAK NNLSETWHNG QSQDLYVPAM
TWHNRWTYSR QKIDKYNERP WGAGYGVSRL DSDGDWHGIY LMAFKDSFNK WEPIGGYGYE
KRWKPVAGND DFQLGLGFTA GVTMRDNWNY IPIPVLLPLA SINYQRLSFQ MTYIPGTHNN
GNVYFAWLRW QL
