PAGP_ECOLI
ID PAGP_ECOLI Reviewed; 186 AA.
AC P37001; P77617; Q9R7T4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 147.
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};
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};
GN Synonyms=crcA {ECO:0000303|PubMed:8844142}, ybeG;
GN OrderedLocusNames=b0622, JW0617;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8844142; DOI=10.1093/genetics/143.4.1521;
RA Hu K.H., Liu E., Dean K., Gingras M., Degraff W., Trun N.J.;
RT "Overproduction of three genes leads to camphor resistance and chromosome
RT condensation in Escherichia coli.";
RL Genetics 143:1521-1532(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Yamanaka K., Mitani T., Ogura T., Niki H., Hiraga S.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Ramanathan Y., Narayanarao A.V.S.S., Mathur M., Mahajan S.K.;
RT "A new Escherichia coli gene encoding a negative regulator of growth in
RT cold.";
RL Thesis (1994), University of Bombay, India.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP PROTEIN SEQUENCE OF 26-35, FUNCTION AS PALMITOYL TRANSFERASE, CATALYTIC
RP ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=K12;
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).
RN [9]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (MAR-1994).
RN [10]
RP INDUCTION.
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 [11]
RP SUBSTRATE SPECIFICITY, AND FUNCTION.
RX PubMed=20853818; DOI=10.1021/bi1011496;
RA Khan M.A., Moktar J., Mott P.J., Vu M., McKie A.H., Pinter T., Hof F.,
RA Bishop R.E.;
RT "Inscribing the perimeter of the PagP hydrocarbon ruler by site-specific
RT chemical alkylation.";
RL Biochemistry 49:9046-9057(2010).
RN [12]
RP STRUCTURE BY NMR OF 26-186, MUTAGENESIS OF HIS-58; ASP-101; SER-102 AND
RP SER-155, AND ACTIVE SITE.
RX PubMed=12357033; DOI=10.1073/pnas.212344499;
RA Hwang P.M., Choy W.Y., Lo E.I., Chen L., Forman-Kay J.D., Raetz C.R.,
RA Prive G.G., Bishop R.E., Kay L.E.;
RT "Solution structure and dynamics of the outer membrane enzyme PagP by
RT NMR.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13560-13565(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 26-186 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, HYDROCARBON RULER SELECTIVITY, MUTAGENESIS OF GLY-113, AND
RP ACTIVITY REGULATION.
RX PubMed=15272304; DOI=10.1038/sj.emboj.7600320;
RA Ahn V.E., Lo E.I., Engel C.K., Chen L., Hwang P.M., Kay L.E., Bishop R.E.,
RA Prive G.G.;
RT "A hydrocarbon ruler measures palmitate in the enzymatic acylation of
RT endotoxin.";
RL EMBO J. 23:2931-2941(2004).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 26-186 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, FUNCTION, MUTAGENESIS OF TYR-172, REACTION MECHANISM, AND ACTIVE
RP SITE.
RX PubMed=20826347; DOI=10.1016/j.str.2010.06.014;
RA Cuesta-Seijo J.A., Neale C., Khan M.A., Moktar J., Tran C.D., Bishop R.E.,
RA Pomes R., Prive G.G.;
RT "PagP crystallized from SDS/cosolvent reveals the route for phospholipid
RT access to the hydrocarbon ruler.";
RL Structure 18:1210-1219(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. Phosphatidylglycerol (PtdGro),
CC phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and
CC phosphatidic acid (Ptd-OH) are all effective acyl donors.
CC {ECO:0000269|PubMed:11013210, ECO:0000269|PubMed:20826347,
CC ECO:0000269|PubMed:20853818}.
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:11013210};
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 -!- ACTIVITY REGULATION: Inhibited by lauryldimethylamine oxide (LDAO) and
CC dodecylphosphocholine (DPC). {ECO:0000269|PubMed:15272304}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00837,
CC ECO:0000269|PubMed:11013210, ECO:0000269|PubMed:15272304,
CC ECO:0000269|PubMed:20826347}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00837, ECO:0000269|PubMed:11013210}.
CC -!- INDUCTION: In magnesium-deficient conditions.
CC {ECO:0000269|PubMed:9790526}.
CC -!- MISCELLANEOUS: Overproduction leads to camphor resistance and
CC chromosome condensation. {ECO:0000269|PubMed:8844142}.
CC -!- SIMILARITY: Belongs to the lipid A palmitoyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
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DR EMBL; S83396; AAN86719.1; -; Genomic_DNA.
DR EMBL; D28497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L29054; AAA67555.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40822.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73723.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35265.2; -; Genomic_DNA.
DR PIR; D64796; D64796.
DR RefSeq; NP_415155.1; NC_000913.3.
DR RefSeq; WP_001103094.1; NZ_STEB01000031.1.
DR PDB; 1MM4; NMR; -; A=26-186.
DR PDB; 1MM5; NMR; -; A=26-186.
DR PDB; 1THQ; X-ray; 1.90 A; A=26-186.
DR PDB; 3GP6; X-ray; 1.40 A; A=26-186.
DR PDBsum; 1MM4; -.
DR PDBsum; 1MM5; -.
DR PDBsum; 1THQ; -.
DR PDBsum; 3GP6; -.
DR AlphaFoldDB; P37001; -.
DR BMRB; P37001; -.
DR SMR; P37001; -.
DR BioGRID; 4260645; 351.
DR STRING; 511145.b0622; -.
DR DrugBank; DB03967; Dodecyl sulfate.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR PaxDb; P37001; -.
DR PRIDE; P37001; -.
DR EnsemblBacteria; AAC73723; AAC73723; b0622.
DR EnsemblBacteria; BAA35265; BAA35265; BAA35265.
DR GeneID; 66671103; -.
DR GeneID; 946360; -.
DR KEGG; ecj:JW0617; -.
DR KEGG; eco:b0622; -.
DR PATRIC; fig|1411691.4.peg.1646; -.
DR EchoBASE; EB2097; -.
DR eggNOG; ENOG502Z7SY; Bacteria.
DR HOGENOM; CLU_104099_0_0_6; -.
DR OMA; AQTWNEP; -.
DR BioCyc; EcoCyc:EG12180-MON; -.
DR BioCyc; MetaCyc:EG12180-MON; -.
DR BRENDA; 2.3.1.251; 2026.
DR EvolutionaryTrace; P37001; -.
DR PRO; PR:P37001; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR GO; GO:0016416; F:O-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 3D-structure; Acyltransferase; Cell outer membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT CHAIN 26..186
FT /note="Lipid A palmitoyltransferase PagP"
FT /id="PRO_0000079332"
FT ACT_SITE 58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837,
FT ECO:0000305|PubMed:12357033, ECO:0000305|PubMed:20826347"
FT ACT_SITE 101
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837,
FT ECO:0000305|PubMed:12357033, ECO:0000305|PubMed:20826347"
FT ACT_SITE 102
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837,
FT ECO:0000305|PubMed:12357033, ECO:0000305|PubMed:20826347"
FT SITE 67
FT /note="Role in lipopolysaccharide recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT SITE 172
FT /note="Role in the phospholipid gating"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00837"
FT MUTAGEN 58
FT /note="H->F: Drastically reduces palmitoyltransferase
FT activity while leaving expression and membrane insertion
FT intact."
FT /evidence="ECO:0000269|PubMed:12357033"
FT MUTAGEN 58
FT /note="H->N: Drastically reduces palmitoyltransferase
FT activity while leaving expression and membrane insertion
FT intact."
FT /evidence="ECO:0000269|PubMed:12357033"
FT MUTAGEN 101
FT /note="D->A: Drastically reduces palmitoyltransferase
FT activity while leaving expression and membrane insertion
FT intact."
FT /evidence="ECO:0000269|PubMed:12357033"
FT MUTAGEN 101
FT /note="D->N: Drastically reduces palmitoyltransferase
FT activity while leaving expression and membrane insertion
FT intact."
FT /evidence="ECO:0000269|PubMed:12357033"
FT MUTAGEN 102
FT /note="S->A: Drastically reduces palmitoyltransferase
FT activity while leaving expression and membrane insertion
FT intact."
FT /evidence="ECO:0000269|PubMed:12357033"
FT MUTAGEN 113
FT /note="G->A: Mutant with longer amino-acid side chains at
FT position 113 preferentially transfers pentadecane chain
FT (15:0)."
FT /evidence="ECO:0000269|PubMed:15272304"
FT MUTAGEN 113
FT /note="G->C: Mutants with longer amino-acid side chains at
FT position 113 preferentially transfers myristate chain
FT (14:0)."
FT /evidence="ECO:0000269|PubMed:15272304"
FT MUTAGEN 113
FT /note="G->M: Mutants with longer amino-acid side chains at
FT position 113 preferentially transfers laurate chain
FT (12:0)."
FT /evidence="ECO:0000269|PubMed:15272304"
FT MUTAGEN 155
FT /note="S->A: Fully functional."
FT /evidence="ECO:0000269|PubMed:12357033"
FT MUTAGEN 172
FT /note="Y->A: Does not cause significant structural
FT perturbations of the enzyme, but induces a 2-fold increase
FT in the palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20826347"
FT MUTAGEN 172
FT /note="Y->F: Does not cause significant structural
FT perturbations of the enzyme, but induces a 2.3-fold
FT increase in the palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20826347"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 47..60
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:3GP6"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1MM4"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1MM4"
FT STRAND 106..118
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 126..138
FT /evidence="ECO:0007829|PDB:3GP6"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3GP6"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:3GP6"
SQ SEQUENCE 186 AA; 21770 MW; 4BC35B02286844A7 CRC64;
MNVSKYVAIF SFVFIQLISV GKVFANADEW MTTFRENIAQ TWQQPEHYDL YIPAITWHAR
FAYDKEKTDR YNERPWGGGF GLSRWDEKGN WHGLYAMAFK DSWNKWEPIA GYGWESTWRP
LADENFHLGL GFTAGVTARD NWNYIPLPVL LPLASVGYGP VTFQMTYIPG TYNNGNVYFA
WMRFQF
