PAGP_BORPC
ID PAGP_BORPC Reviewed; 182 AA.
AC F4LAC2;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=BPTD_2973;
OS Bordetella pertussis (strain CS).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1017264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS;
RX PubMed=21622744; DOI=10.1128/jb.05184-11;
RA Zhang S., Xu Y., Zhou Z., Wang S., Yang R., Wang J., Wang L.;
RT "Complete genome sequence of B. pertussis CS, Chinese pertussis vaccine
RT strain.";
RL J. Bacteriol. 193:4017-4018(2011).
RN [2]
RP LACK OF EXPRESSION.
RX PubMed=12694617; DOI=10.1046/j.1365-2958.2003.03484.x;
RA Preston A., Maxim E., Toland E., Pishko E.J., Harvill E.T., Caroff M.,
RA Maskell D.J.;
RT "Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl
RT transferase that is required for persistent colonization of the mouse
RT respiratory tract.";
RL Mol. Microbiol. 48:725-736(2003).
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, ECO:0000305}; Lipid-anchor {ECO:0000255|HAMAP-
CC Rule:MF_00837, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
CC -!- CAUTION: According to PubMed:12694617, it appears that PagP is not
CC expressed because of disruption of the putative promoter region by
CC insertion of an IS element. {ECO:0000305|PubMed:12694617}.
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DR EMBL; CP002695; AEE68202.1; -; Genomic_DNA.
DR RefSeq; WP_010931248.1; NC_017223.1.
DR AlphaFoldDB; F4LAC2; -.
DR SMR; F4LAC2; -.
DR GeneID; 45390479; -.
DR KEGG; bpc:BPTD_2973; -.
DR PATRIC; fig|1017264.3.peg.3203; -.
DR HOGENOM; CLU_104099_0_0_4; -.
DR OMA; AQTWNEP; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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.
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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 22..182
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414430"
FT ACT_SITE 55
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 98
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 99
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 64
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 182 AA; 20276 MW; 01A8BF24CF146F25 CRC64;
MTQYFRSLAF FLLPVPATAM ACDGWPSWAR GACQRVDQIW NEGGNDLYLT GYSWHNRAMY
SSDKIRSFNE LAWGGGLGKS IYDEDGDWQG LYAMAFLDSH SDIEPIAGYG FQKIGRIGAD
TRLGIGYTVF LTSRSDIMSR VPFPGILPLV SAGYRDATLY ATYIPGGKGN GNVLFMFGRW
EF
