PAGP_PANAM
ID PAGP_PANAM Reviewed; 190 AA.
AC D4GM10;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 52.
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}; Synonyms=crcA;
GN OrderedLocusNames=PANA_1113;
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103;
RX PubMed=20348253; DOI=10.1128/jb.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
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, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADD76280.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001875; ADD76280.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015700757.1; NC_013956.2.
DR AlphaFoldDB; D4GM10; -.
DR SMR; D4GM10; -.
DR STRING; 706191.PANA_1113; -.
DR EnsemblBacteria; ADD76280; ADD76280; PANA_1113.
DR KEGG; pam:PANA_1113; -.
DR PATRIC; fig|553.3.peg.3199; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OrthoDB; 1171115at2; -.
DR BioCyc; PANA706191:PANA_RS05700-MON; -.
DR Proteomes; UP000001702; 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..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 25..190
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414466"
FT ACT_SITE 62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 105
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 106
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 176
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 190 AA; 22133 MW; 6DAD756562DD1DC5 CRC64;
MNRYLLTTLS APLLALFFSF SLQAAMLSQE IKSGWDTFTG NVQQTWQQPD AIDVYVPAIT
WHNRWTYDEE HIHRYNERPW GAGGGVSRYD EKGNWHGLYL MAFKDSFNKW EPFGGYGWEA
TWRPLQDQNF HYGLGYTAGV TARHNWGYYP VPAILPLASI GYGSLNFQMT YIPGTYNNGN
VYFAWLRWQF