PAGP_ENTLS
ID PAGP_ENTLS Reviewed; 191 AA.
AC E3G4M5;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 25-MAY-2022, entry version 56.
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=Entcl_3173;
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=701347;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA Hazen T.C., Woyke T.;
RT "Complete sequence of Enterobacter cloacae SCF1.";
RL Submitted (OCT-2010) 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, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADO49419.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP002272; ADO49419.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; E3G4M5; -.
DR SMR; E3G4M5; -.
DR STRING; 701347.Entcl_3173; -.
DR EnsemblBacteria; ADO49419; ADO49419; Entcl_3173.
DR KEGG; esc:Entcl_3173; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_6; -.
DR Proteomes; UP000006872; 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; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 27..191
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414439"
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"
FT SITE 177
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 191 AA; 22123 MW; BCD99A749BAB2D37 CRC64;
MLKVNKYVIL IIAFVSQMMF STTAQASFSA TVSDAWSTLS NNVTQTWQAP EHYDLYVPVI
TWHARFAYDQ EKIDNYNERP WGAGFGMSRW DEKGNWNGLY LMAFKDSFNK WEPIVGYGWE
KTWRPLADDN FHLGLGYTLG VTARDNWNYI PLPVILPMAS VGYGPATFQM TYIPGTYNNG
NVYFAWLRFQ F
