PAGP_YERPB
ID PAGP_YERPB Reviewed; 202 AA.
AC B2K0E2;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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}; Synonyms=crcA;
GN OrderedLocusNames=YPTS_1744;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) 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}.
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DR EMBL; CP001048; ACC88711.1; -; Genomic_DNA.
DR RefSeq; WP_011192143.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K0E2; -.
DR SMR; B2K0E2; -.
DR GeneID; 66841944; -.
DR KEGG; ypb:YPTS_1744; -.
DR PATRIC; fig|502801.10.peg.1121; -.
DR OMA; AQTWNEP; -.
DR BioCyc; YPSE502801:YPTS_RS08895-MON; -.
DR GO; GO:0009279; C:cell outer membrane; ISS:UniProtKB.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; ISS:UniProtKB.
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..202
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_5000345389"
FT ACT_SITE 74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 118
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 83
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 188
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 202 AA; 23518 MW; 963C1A9FBCB0F0A2 CRC64;
MNYKDIINAC ILSGVFLLHS PSALADTPSV GVSKGQESLQ PAAEGNLWQR LIRNVSLAWN
SPHQELYIPV NTWHNRWTYD DEKIASYNER PWGVGYGKYR YDEDNNWHSV YAMAFMDSHN
RVEPILGYGY QKMWIPGERE GWRFGAGFTA SITARYEYHY IPLPLPLPLI SIEYNRLSLQ
TTYIPGTYNN GNVLFTWIRW QF
