PAGP_CROTZ
ID PAGP_CROTZ Reviewed; 192 AA.
AC C9XYQ1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=Ctu_12560;
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX PubMed=21037008; DOI=10.1128/jb.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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; FN543093; CBA29120.1; -; Genomic_DNA.
DR RefSeq; WP_007768012.1; NC_013282.2.
DR AlphaFoldDB; C9XYQ1; -.
DR SMR; C9XYQ1; -.
DR EnsemblBacteria; CBA29120; CBA29120; CTU_12560.
DR GeneID; 60372571; -.
DR KEGG; ctu:CTU_12560; -.
DR PATRIC; fig|693216.3.peg.1194; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR Proteomes; UP000002069; 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..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 27..192
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414432"
FT ACT_SITE 64
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT ACT_SITE 108
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 73
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 178
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
SQ SEQUENCE 192 AA; 22053 MW; 4AF14F5FD028D63F CRC64;
MTVVNKSFLT FLVFFCQILF PLNASALEAP RTVKAWASVL GDNIAETWNE PQHVDLYVPA
ITWHARFAYD KEKTDRYNER PWGAGIGKSR WDEKGNWHGL YVMAFKDSYN KWEPIAGYGW
EATWRPLPDD AFHVGLGYTL GVTARDNWDY IPIPLVLPLA SVGYGPATFQ MTYIPGTYNN
GNVYFAWLRL QF
