PAGP_BORPA
ID PAGP_BORPA Reviewed; 182 AA.
AC Q7W4D1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BPP3735;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2]
RP INDUCTION.
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 -!- INDUCTION: The expression of pagP is down-regulated in Bvg-minus phase
CC and up-regulated in Bvg-plus phase. {ECO:0000269|PubMed:12694617}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
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DR EMBL; BX640434; CAE39018.1; -; Genomic_DNA.
DR RefSeq; WP_010929221.1; NC_002928.3.
DR AlphaFoldDB; Q7W4D1; -.
DR SMR; Q7W4D1; -.
DR EnsemblBacteria; CAE39018; CAE39018; BPP3735.
DR KEGG; bpa:BPP3735; -.
DR HOGENOM; CLU_104099_0_0_4; -.
DR OMA; AQTWNEP; -.
DR BRENDA; 2.3.1.251; 898.
DR Proteomes; UP000001421; Chromosome.
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 2: Evidence at transcript level;
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_0000414428"
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; 20334 MW; 2C394A64FFBABBEB CRC64;
MTQYFRALAF FLLLVPATAM ACDDWPSWAR GACQRVDQIW NEGGNDLYLT GYSWHNRAMY
SSDKIRSFNE LAWGGGLGKS IYDEDGDWQG LYAMAFLDSH SDIEPIAGYG FQKIGRIGAD
TRLGIGYTVF LTSRSDIMSR VPFPGILPLV SAGYRDATLY ATYIPGGKGN GNVLFMFGRW
EF
