PAGP_SALPC
ID PAGP_SALPC Reviewed; 193 AA.
AC C0PW57;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 49.
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=SPC_0643;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN44820.1; -; Genomic_DNA.
DR AlphaFoldDB; C0PW57; -.
DR SMR; C0PW57; -.
DR EnsemblBacteria; ACN44820; ACN44820; SPC_0643.
DR KEGG; sei:SPC_0643; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR Proteomes; UP000001599; 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; Signal; Transferase.
FT SIGNAL 1..32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 33..193
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414471"
FT ACT_SITE 65
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 108
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 109
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 74
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 179
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 193 AA; 22424 MW; A94E87508859D7E1 CRC64;
MNGMAVVMII RKYFLIIALL VMPWLAIPSV SAADKGGFNT FTDNVAETWR QPEHYDLYVP
AITWHARFAY DKEKTDRYNE RPWGVGFGQS RWDDKGNWHG LYMMAFKDSF NKWEPIGGYG
WEKTWRPLED DNFRLGLGFT AGVTARDNWN YIPIPVLLPL ASIGYGPATF QMTYIPGSYN
NGNVYFAWMR FQF
