PAGP_ERWPE
ID PAGP_ERWPE Reviewed; 185 AA.
AC D0FUE8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, 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}; OrderedLocusNames=EpC_24980;
OS Erwinia pyrifoliae (strain DSM 12162 / Ep1/96).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12162 / Ep1/96;
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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; FP236842; CAX56277.1; -; Genomic_DNA.
DR RefSeq; WP_012668771.1; NC_012214.1.
DR AlphaFoldDB; D0FUE8; -.
DR SMR; D0FUE8; -.
DR KEGG; epy:EpC_24980; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
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_0000414446"
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; 21452 MW; FF4DEB063C01276E CRC64;
MKLKPVLYLL MLLGCLGLKS AHAATLAHGI SASWHSFSQT WNEPQTFDPY IPSIIWHNRW
TYDADKIDKY NERPWGAGGG VSHFDKKGNW NGIYLMAFKD SFNKWELISG YGWEKTWRPL
RDPDFHLGLG YTAGVTMRDN WSYIPIPVLL PLASIGYEYV SFQMTYIPGT YNNGNVYFAW
LRWQL
