PAGP_ERWSE
ID PAGP_ERWSE Reviewed; 185 AA.
AC E3DK69;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 46.
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=EJP617_22300;
OS Erwinia sp. (strain Ejp617).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia; unclassified Erwinia.
OX NCBI_TaxID=215689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ejp617;
RX PubMed=21075933; DOI=10.1128/jb.01246-10;
RA Park D.H., Thapa S.P., Choi B.S., Kim W.S., Hur J.H., Cho J.M., Lim J.S.,
RA Choi I.Y., Lim C.K.;
RT "Complete genome sequence of Japanese Erwinia strain Ejp617, a bacterial
RT shoot blight pathogen of pear.";
RL J. Bacteriol. 193:586-587(2011).
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}; Lipid-anchor {ECO:0000255|HAMAP-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; CP002124; ADP11911.1; -; Genomic_DNA.
DR RefSeq; WP_014543714.1; NC_017445.1.
DR AlphaFoldDB; E3DK69; -.
DR SMR; E3DK69; -.
DR STRING; 215689.EJP617_22300; -.
DR EnsemblBacteria; ADP11911; ADP11911; EJP617_22300.
DR KEGG; erj:EJP617_22300; -.
DR PATRIC; fig|215689.3.peg.2375; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR OrthoDB; 1171115at2; -.
DR Proteomes; UP000006865; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Signal; Transferase.
FT SIGNAL 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 15..185
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414447"
FT ACT_SITE 57
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 100
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 101
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 66
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 171
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT LIPID 15
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT LIPID 15
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 185 AA; 21409 MW; AF1BC62EE1612778 CRC64;
MKLKPVLYLL MLLGCLGLKS AHAATLAHGI SASWHSFSQK WNEPQTFDPY IPSIIWHNRW
TYDADKIDKY NERPWGAGGG VSHFDKKGNW NGIYLMAFKD SFNKWELISG YGWEKTWRPL
SDPDFHLGLG YTAGVTMRDN WSYIPIPVLL PLASIGYEYV SFQMTYIPGT YNNGNVYFAW
LRWQL
