PAGP_METFK
ID PAGP_METFK Reviewed; 184 AA.
AC Q1H2L0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=pagP1 {ECO:0000255|HAMAP-Rule:MF_00837}; OrderedLocusNames=Mfla_0865;
GN and
GN Name=pagP2 {ECO:0000255|HAMAP-Rule:MF_00837}; OrderedLocusNames=Mfla_1009;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837}.
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DR EMBL; CP000284; ABE49133.1; -; Genomic_DNA.
DR EMBL; CP000284; ABE49277.1; -; Genomic_DNA.
DR RefSeq; WP_011479230.1; NC_007947.1.
DR AlphaFoldDB; Q1H2L0; -.
DR SMR; Q1H2L0; -.
DR STRING; 265072.Mfla_0865; -.
DR EnsemblBacteria; ABE49133; ABE49133; Mfla_0865.
DR EnsemblBacteria; ABE49277; ABE49277; Mfla_1009.
DR KEGG; mfa:Mfla_0865; -.
DR KEGG; mfa:Mfla_1009; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_4; -.
DR OMA; AQTWNEP; -.
DR OrthoDB; 1171115at2; -.
DR Proteomes; UP000002440; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
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.
PE 3: Inferred from homology;
KW Acyltransferase; Cell outer membrane; Membrane; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 23..184
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414464"
FT ACT_SITE 57
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 100
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 101
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 66
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 184 AA; 20802 MW; 8AE2CFF640F9F8C1 CRC64;
MNIRHGIIAM SSTMLVPLAA EAACNTDYSW IDKSCERISD TWKNGDHDLY IPLWTHHLRF
AYDNDKIDSF REFTWGLGYG RSRYNAAGNW EGVYLMAFSD SHSNVQPMLG YGHQWMMGPR
SGLHAGVGYT AFLTSRADIY KNIPIPGVLP IASLNYRQYS VNTSYVPGGR GNGNILFFWS
RVGF
