(data stored in ACNUC1104 zone)

SWISSPROT: LPXD_BORPA

ID   LPXD_BORPA              Reviewed;         363 AA.
AC   Q7WA50;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523};
GN   OrderedLocusNames=BPP1537;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine
CC       using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the
CC       biosynthesis of lipid A, a phosphorylated glycolipid that anchors
CC       the lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-acyl-alpha-D-
CC         glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D-
CC         glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78827, ChEBI:CHEBI:137740,
CC         ChEBI:CHEBI:137748; Evidence={ECO:0000255|HAMAP-Rule:MF_00523};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxD subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
DR   EMBL; BX640427; CAE36839.1; -; Genomic_DNA.
DR   RefSeq; WP_003811779.1; NC_002928.3.
DR   SMR; Q7WA50; -.
DR   EnsemblBacteria; CAE36839; CAE36839; BPP1537.
DR   KEGG; bpa:BPP1537; -.
DR   HOGENOM; HOG000294339; -.
DR   KO; K02536; -.
DR   OMA; GFGYAHT; -.
DR   BioCyc; BPAR257311:G1GSY-1577-MONOMER; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03352; LbH_LpxD; 1.
DR   HAMAP; MF_00523; LpxD; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR007691; LpxD.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR   PANTHER; PTHR43378; PTHR43378; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q7WA50.
DR   SWISS-2DPAGE; Q7WA50.
KW   Acyltransferase; Complete proteome; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Repeat; Transferase.
FT   CHAIN         1    363       UDP-3-O-acylglucosamine N-
FT                                acyltransferase.
FT                                /FTId=PRO_0000059649.
FT   ACT_SITE    266    266       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00523}.
SQ   SEQUENCE   363 AA;  37556 MW;  EFAB658996E5A449 CRC64;
     MPVLLDPENA LALDVLLAGT DAQGLDWHLS APDAADLPRI RGIGTLSSAG NEEISFLSNP
     RYQNQLATTR AAAVIVTPDV AQARQEQGAS GHVLVVCKHP YLLYARLAQW FERASRPAGP
     AGVHPSAVVD PSAEIDADAR VGAQCVIEAG ARIGRGARLG PGCVIGAGST VGADSLLHPR
     VTLYAGVHVG ERAIIHSGAV LGADGFGFAP DPTLGRGAWG KIPQLGGVRV GNDVEIGANT
     TIDRGALDDT IVGDGVKLDN QIMVAHNVRI GAHTAIAACV GIAGSTTIGE RCTIGGASML
     SGHLAIADDV NISGGTAVTS NIAKAGRYTG VYPYAEHSEW QRNAAVIQQL ALLRRRLRAL
     ERE
//

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