PAGP_SALTY
ID PAGP_SALTY Reviewed; 190 AA.
AC Q8ZR06; Q9ZHL7;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Lipid A palmitoyltransferase PagP {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305};
DE EC=2.3.1.251 {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000269|PubMed:11013210, ECO:0000269|PubMed:9790526};
DE AltName: Full=Antimicrobial peptide resistance;
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, ECO:0000303|PubMed:9790526};
GN OrderedLocusNames=STM0628;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS PALMITOYL TRANSFERASE AND IN
RP CAMP RESISTANCE, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=9790526; DOI=10.1016/s0092-8674(00)81750-x;
RA Guo L., Lim K.B., Poduje C.M., Morad D., Gunn J.S., Hackett M.,
RA Miller S.I.;
RT "Lipid A acylation and bacterial resistance against vertebrate
RT antimicrobial peptides.";
RL Cell 95:189-198(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION AS PALMITOYL TRANSFERASE, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=11013210; DOI=10.1093/emboj/cdd507;
RA Bishop R.E., Gibbons H.S., Guina T., Trent M.S., Miller S.I., Raetz C.R.;
RT "Transfer of palmitate from phospholipids to lipid A in outer membranes of
RT gram-negative bacteria.";
RL EMBO J. 19:5071-5080(2000).
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. Required for resistance to cationic
CC antimicrobial peptides (CAMPs). Modifications of lipid A with a
CC palmitate chain allow to evade host immune defenses by resisting
CC antimicrobial peptides and attenuating the inflammatory response to
CC infection triggered by lipopolysaccharide through the Toll-like
CC receptor 4 (TLR4) signal transduction pathway.
CC {ECO:0000269|PubMed:11013210, ECO:0000269|PubMed:9790526}.
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 ECO:0000269|PubMed:9790526};
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 ECO:0000269|PubMed:11013210};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00837}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00837, ECO:0000269|PubMed:11013210}.
CC -!- INDUCTION: Regulated by the PhoP/PhoQ two-component regulatory system.
CC {ECO:0000305|PubMed:9790526}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene increases outer membrane
CC permeability in response to CAMP. {ECO:0000269|PubMed:9790526}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF057021; AAC67499.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL19579.1; -; Genomic_DNA.
DR RefSeq; NP_459620.1; NC_003197.2.
DR RefSeq; WP_000289054.1; NC_003197.2.
DR AlphaFoldDB; Q8ZR06; -.
DR SMR; Q8ZR06; -.
DR STRING; 99287.STM0628; -.
DR PaxDb; Q8ZR06; -.
DR EnsemblBacteria; AAL19579; AAL19579; STM0628.
DR GeneID; 1252148; -.
DR KEGG; stm:STM0628; -.
DR PATRIC; fig|99287.12.peg.662; -.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR BioCyc; MetaCyc:STM0628-MON; -.
DR BioCyc; SENT99287:STM0628-MON; -.
DR BRENDA; 2.3.1.251; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Cell outer membrane; Membrane; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 30..190
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000414473"
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 71
FT /note="Role in lipopolysaccharide recognition"
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; 22199 MW; 75A8892C7BBF3FD9 CRC64;
MYVAMIIRKY FLIIALLLMP WLAIPSVSAA DKGGFNTFTD NVAETWRQPE HYDLYVPAIT
WHARFAYDKE KTDRYNERPW GVGFGQSRWD DKGNWHGLYM MAFKDSFNKW EPIGGYGWEK
TWRPLEDDNF RLGLGFTAGV TARDNWNYIP IPVLLPLASI GYGPATFQMT YIPGSYNNGN
VYFAWMRFQF
