PAGP_ECOLW
ID PAGP_ECOLW Reviewed; 186 AA.
AC E0J1Q4; H9XYT9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-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};
GN OrderedLocusNames=ECW_m0677, WFL_03365; ORFNames=EschWDRAFT_2559;
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Tremaine M.,
RA Landick R., Keating D., Woyke T.J.;
RT "The draft genome of Escherichia coli W.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=22075923; DOI=10.1007/s10295-011-1052-2;
RA Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L.,
RA Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.;
RT "Optical mapping and sequencing of the Escherichia coli KO11 genome reveal
RT extensive chromosomal rearrangements, and multiple tandem copies of the
RT Zymomonas mobilis pdc and adhB genes.";
RL J. Ind. Microbiol. Biotechnol. 39:629-639(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}.
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DR EMBL; AEDF01000012; EFN37868.1; -; Genomic_DNA.
DR EMBL; CP002185; ADT74205.1; -; Genomic_DNA.
DR EMBL; CP002967; AFH10341.1; -; Genomic_DNA.
DR RefSeq; WP_001349980.1; NZ_WBMH01000008.1.
DR AlphaFoldDB; E0J1Q4; -.
DR BMRB; E0J1Q4; -.
DR SMR; E0J1Q4; -.
DR EnsemblBacteria; ADT74205; ADT74205; ECW_m0677.
DR KEGG; ell:WFL_03365; -.
DR KEGG; elw:ECW_m0677; -.
DR PATRIC; fig|566546.30.peg.696; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR Proteomes; UP000008525; 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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 26..186
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414450"
FT ACT_SITE 58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 101
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 102
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 67
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 172
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 186 AA; 21740 MW; BD25B8B498684211 CRC64;
MNVSKYVAIF SFVFIQLISV GKVFANADEW MTTFRENIAQ TRQQPEHYDL YIPAITWHAR
FAYDKEKTDR YNERPWGGGF GLSRWDEKGN WHGLYAMAFK DSWNKWEPIA GYGWESTWRP
LADENFHLGL GFTAGVTARD NWNYIPLPVL LPLASVGYGP VTFQMTYIPG TYNNGNVYFA
WMRFQF
