PAGP_BORBR
ID PAGP_BORBR Reviewed; 182 AA.
AC Q7WFT9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=BB4181;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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 FUNCTION AS PALMITOYL TRANSFERASE, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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).
RN [3]
RP RESISTANCE TO ANTIBODY-MEDIATED COMPLEMENT LYSIS.
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=15102794; DOI=10.1128/iai.72.5.2837-2842.2004;
RA Pilione M.R., Pishko E.J., Preston A., Maskell D.J., Harvill E.T.;
RT "pagP is required for resistance to antibody-mediated complement lysis
RT during Bordetella bronchiseptica respiratory infection.";
RL Infect. Immun. 72:2837-2842(2004).
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. Required for resistance to antibody-mediated
CC complement lysis. Modifications of lipid A with a palmitate chain allow
CC to evade host immune defenses by resisting antibody-mediated complement
CC lysis during respiratory infection. {ECO:0000269|PubMed:12694617,
CC ECO:0000269|PubMed:15102794}.
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 -!- DISRUPTION PHENOTYPE: Disruption of this gene suppresses the esterified
CC palmitate chain (16:0) in the lipid A and compromises the ability to
CC persist in a mouse after 7 days. However, the mutant is no different
CC from wild-type in its ability to colonize and persist within the
CC respiratory tract during the early part of the infection.
CC {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; BX640449; CAE34545.1; -; Genomic_DNA.
DR RefSeq; WP_003814556.1; NC_002927.3.
DR AlphaFoldDB; Q7WFT9; -.
DR SMR; Q7WFT9; -.
DR STRING; 257310.BB4181; -.
DR EnsemblBacteria; CAE34545; CAE34545; BB4181.
DR GeneID; 56477328; -.
DR GeneID; 66437284; -.
DR KEGG; bbr:BB4181; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_4; -.
DR OMA; AQTWNEP; -.
DR OrthoDB; 1171115at2; -.
DR BRENDA; 2.3.1.251; 227.
DR Proteomes; UP000001027; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; ISS:UniProtKB.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; IMP:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP: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 1: Evidence at protein 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_0000414427"
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; 3E2B65B4FD4795F6 CRC64;
MTQYFRALAF FLLLVPATAM ACDGWPSWAR GACQRVDQIW NEGGNDLYLT GYSWHNRAMY
SSDKIRSFNE LAWGGGLGKS IYDEDGDWQG LYAMAFLDSH SDIEPIAGYG FQKIGRIGAD
TRLGIGYTVF LTSRSDIMSR VPFPGILPLV SAGYRDATLY ATYIPGGKGN GNVLFMFGRW
EF
