PAGP_BORPE
ID PAGP_BORPE Reviewed; 182 AA.
AC Q7VUS0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=BP3006;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
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 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; BX640420; CAE43277.1; -; Genomic_DNA.
DR RefSeq; NP_881581.1; NC_002929.2.
DR RefSeq; WP_010931248.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VUS0; -.
DR SMR; Q7VUS0; -.
DR STRING; 257313.BP3006; -.
DR GeneID; 45390479; -.
DR KEGG; bpe:BP3006; -.
DR PATRIC; fig|257313.5.peg.3251; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_4; -.
DR OMA; AQTWNEP; -.
DR Proteomes; UP000002676; 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 3: Inferred from homology;
KW Acyltransferase; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; 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_0000414429"
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
