(data stored in ACNUC7421 zone)

SWISSPROT: PAGP_ECO57

ID   PAGP_ECO57              Reviewed;         186 AA.
AC   Q8XBR9; Q7AGP7;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 84.
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=ECs0661, Z0767;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   FUNCTION AS PALMITOYL TRANSFERASE.
RX   PubMed=18070877; DOI=10.1074/jbc.M708163200;
RA   Smith A.E., Kim S.H., Liu F., Jia W., Vinogradov E., Gyles C.L.,
RA   Bishop R.E.;
RT   "PagP activation in the outer membrane triggers R3 core
RT   oligosaccharide truncation in the cytoplasm of Escherichia coli
RT   O157:H7.";
RL   J. Biol. Chem. 283:4332-4343(2008).
CC   -!- FUNCTION: Transfers a palmitate residue from the sn-1 position of
CC       a phospholipid to the N-linked hydroxymyristate on the proximal
CC       unit of lipid A or its precursors. {ECO:0000255|HAMAP-
CC       Rule:MF_00837, ECO:0000269|PubMed:18070877}.
CC   -!- CATALYTIC ACTIVITY: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
CC       + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-
CC       acyl lipid A. {ECO:0000255|HAMAP-Rule:MF_00837}.
CC   -!- CATALYTIC ACTIVITY: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
CC       + lipid II(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid II(B).
CC       {ECO:0000255|HAMAP-Rule:MF_00837}.
CC   -!- CATALYTIC ACTIVITY: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine
CC       + lipid IV(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid IV(B).
CC       {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}.
DR   EMBL; AE005174; AAG54957.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34084.1; -; Genomic_DNA.
DR   PIR; A85562; A85562.
DR   PIR; E90711; E90711.
DR   RefSeq; NP_308688.1; NC_002695.1.
DR   RefSeq; WP_001301703.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBR9; -.
DR   SMR; Q8XBR9; -.
DR   STRING; 155864.Z0767; -.
DR   EnsemblBacteria; AAG54957; AAG54957; Z0767.
DR   EnsemblBacteria; BAB34084; BAB34084; BAB34084.
DR   GeneID; 917021; -.
DR   KEGG; ece:Z0767; -.
DR   KEGG; ecs:ECs0661; -.
DR   PATRIC; fig|386585.9.peg.772; -.
DR   eggNOG; ENOG41079UR; Bacteria.
DR   eggNOG; ENOG410XTHE; LUCA.
DR   HOGENOM; HOG000117945; -.
DR   KO; K12973; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0016416; F:O-palmitoyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 2.40.160.20; -; 1.
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   ProDom; PD103779; PagP; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8XBR9.
DR   SWISS-2DPAGE; Q8XBR9.
KW   Acyltransferase; Cell outer membrane; Complete proteome; Membrane;
KW   Signal; Transferase.
FT   SIGNAL        1     25       {ECO:0000255|HAMAP-Rule:MF_00837}.
FT   CHAIN        26    186       Lipid A palmitoyltransferase PagP.
FT                                /FTId=PRO_0000414452.
FT   ACT_SITE     58     58       {ECO:0000255|HAMAP-Rule:MF_00837}.
FT   ACT_SITE    101    101       {ECO:0000255|HAMAP-Rule:MF_00837}.
FT   ACT_SITE    102    102       {ECO:0000255|HAMAP-Rule:MF_00837}.
FT   SITE         67     67       Role in lipopolysaccharide recognition.
FT                                {ECO:0000255|HAMAP-Rule:MF_00837}.
FT   SITE        172    172       Role in the phospholipid gating.
FT                                {ECO:0000255|HAMAP-Rule:MF_00837}.
SQ   SEQUENCE   186 AA;  21798 MW;  4BD52A6BEE47F3F7 CRC64;
     MNVSKYVAIF SFVFIQLISV GKVFANADEW MTTFRENIVQ TWQQPEHYDL YIPAITWHAR
     FAYDKEKTDR YNERPWGGGF GLSRWDEKGN WHGLYAMAFK DSWNKWEPIA GYGWESTWRP
     LADENFHLGL GFTAGVTARD NWNYIPLPVL LPLASVGYGP VTFQMTYIPG TYNNGNVYFA
     WMRFQF
//

If you have problems or comments...

PBIL Back to PBIL home page