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Lipid A palmitoyltransferase PagP (EC 2.3.1.251) (Lipid A acylation protein)

 PAGP_BORBR              Reviewed;         182 AA.
Q7WFT9;
14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
23-MAY-2018, entry version 69.
RecName: Full=Lipid A palmitoyltransferase PagP {ECO:0000255|HAMAP-Rule:MF_00837};
EC=2.3.1.251 {ECO:0000255|HAMAP-Rule:MF_00837};
AltName: Full=Lipid A acylation protein {ECO:0000255|HAMAP-Rule:MF_00837};
Flags: Precursor;
Name=pagP {ECO:0000255|HAMAP-Rule:MF_00837}; OrderedLocusNames=BB4181;
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
(Alcaligenes bronchisepticus).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257310;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
PubMed=12910271; DOI=10.1038/ng1227;
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[2]
FUNCTION AS PALMITOYL TRANSFERASE, DISRUPTION PHENOTYPE, AND
INDUCTION.
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
PubMed=12694617; DOI=10.1046/j.1365-2958.2003.03484.x;
Preston A., Maxim E., Toland E., Pishko E.J., Harvill E.T., Caroff M.,
Maskell D.J.;
"Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl
transferase that is required for persistent colonization of the mouse
respiratory tract.";
Mol. Microbiol. 48:725-736(2003).
[3]
RESISTANCE TO ANTIBODY-MEDIATED COMPLEMENT LYSIS.
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
PubMed=15102794; DOI=10.1128/IAI.72.5.2837-2842.2004;
Pilione M.R., Pishko E.J., Preston A., Maskell D.J., Harvill E.T.;
"pagP is required for resistance to antibody-mediated complement lysis
during Bordetella bronchiseptica respiratory infection.";
Infect. Immun. 72:2837-2842(2004).
-!- FUNCTION: Transfers a palmitate residue from the sn-1 position of
a phospholipid to the N-linked hydroxymyristate on the proximal
unit of lipid A or its precursors. Required for resistance to
antibody-mediated complement lysis. Modifications of lipid A with
a palmitate chain allow to evade host immune defenses by resisting
antibody-mediated complement lysis during respiratory infection.
{ECO:0000269|PubMed:12694617, ECO:0000269|PubMed:15102794}.
-!- CATALYTIC ACTIVITY: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
+ hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-
acyl lipid A. {ECO:0000255|HAMAP-Rule:MF_00837}.
-!- CATALYTIC ACTIVITY: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
+ lipid II(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid II(B).
{ECO:0000255|HAMAP-Rule:MF_00837}.
-!- CATALYTIC ACTIVITY: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
+ lipid IV(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid IV(B).
{ECO:0000255|HAMAP-Rule:MF_00837}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00837}.
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
Rule:MF_00837, ECO:0000305}; Lipid-anchor {ECO:0000255|HAMAP-
Rule:MF_00837, ECO:0000305}.
-!- INDUCTION: The expression of pagP is down-regulated in Bvg-minus
phase and up-regulated in Bvg-plus phase.
{ECO:0000269|PubMed:12694617}.
-!- DISRUPTION PHENOTYPE: Disruption of this gene suppresses the
esterified palmitate chain (16:0) in the lipid A and compromises
the ability to persist in a mouse after 7 days. However, the
mutant is no different from wild-type in its ability to colonize
and persist within the respiratory tract during the early part of
the infection. {ECO:0000269|PubMed:12694617}.
-!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
{ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
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EMBL; BX640449; CAE34545.1; -; Genomic_DNA.
RefSeq; WP_003814556.1; NC_002927.3.
ProteinModelPortal; Q7WFT9; -.
SMR; Q7WFT9; -.
STRING; 257310.BB4181; -.
PRIDE; Q7WFT9; -.
EnsemblBacteria; CAE34545; CAE34545; BB4181.
KEGG; bbr:BB4181; -.
eggNOG; ENOG41079UR; Bacteria.
eggNOG; ENOG410XTHE; LUCA.
HOGENOM; HOG000117945; -.
KO; K12973; -.
OMA; AQTWNEP; -.
OrthoDB; POG091H0I4Y; -.
Proteomes; UP000001027; Chromosome.
GO; GO:0009279; C:cell outer membrane; ISS:UniProtKB.
GO; GO:0016416; F:O-palmitoyltransferase activity; IMP:UniProtKB.
GO; GO:0009245; P:lipid A biosynthetic process; IMP:UniProtKB.
HAMAP; MF_00837; PagP_transferase; 1.
InterPro; IPR011250; OMP/PagP_b-brl.
InterPro; IPR009746; Peptid-resist/lipidA_acyl_PagP.
Pfam; PF07017; PagP; 1.
ProDom; PD103779; PagP; 1.
SUPFAM; SSF56925; SSF56925; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
Acyltransferase; Cell outer membrane; Complete proteome; Lipoprotein;
Membrane; Palmitate; Signal; Transferase.
SIGNAL 1 21 {ECO:0000255|HAMAP-Rule:MF_00837}.
CHAIN 22 182 Lipid A palmitoyltransferase PagP.
/FTId=PRO_0000414427.
ACT_SITE 55 55 {ECO:0000255|HAMAP-Rule:MF_00837}.
ACT_SITE 98 98 {ECO:0000255|HAMAP-Rule:MF_00837}.
ACT_SITE 99 99 {ECO:0000255|HAMAP-Rule:MF_00837}.
SITE 64 64 Role in lipopolysaccharide recognition.
{ECO:0000255|HAMAP-Rule:MF_00837}.
LIPID 22 22 N-palmitoyl cysteine. {ECO:0000255|HAMAP-
Rule:MF_00837}.
LIPID 22 22 S-diacylglycerol cysteine.
{ECO:0000255|HAMAP-Rule:MF_00837}.
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


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