ID   LPXD2_LEGPA             Reviewed;         343 AA.
AC   Q5X0T1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD2 {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=lpp3015;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-
CC       hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of
CC       lipid A, a phosphorylated glycolipid that anchors the
CC       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-[(3R)-3-hydroxyacyl]-
CC         alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC         EC=2.3.1.191; Evidence={ECO:0000255|HAMAP-Rule:MF_00523};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
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DR   EMBL; CR628336; CAH14168.1; -; Genomic_DNA.
DR   RefSeq; WP_014844979.1; NC_006368.1.
DR   AlphaFoldDB; Q5X0T1; -.
DR   SMR; Q5X0T1; -.
DR   KEGG; lpp:lpp3015; -.
DR   LegioList; lpp3015; -.
DR   HOGENOM; CLU_049865_0_0_6; -.
DR   OMA; YKIPHAG; -.
DR   UniPathway; UPA00973; -.
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; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Repeat; Transferase.
FT   CHAIN           1..343
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase 2"
FT                   /id="PRO_0000264390"
FT   ACT_SITE        251
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   343 AA;  36457 MW;  3C1A498A556F5D3F CRC64;
     MSNYQFTKPA GPFRLSELAK ISGATLYEGK GETFTVSGLA KLSEATSNDL VMLHQKKYVK
     ELKNTAARSC IIGPDYVKFA PDSMYLLVHP NPYKAFALIA QAFYPSEKSS SFIAPSAKIE
     STALIGSDCS IAHGAYVGNH ARIGKRCKIG VNTYIGDGVT IGDNCIIEDN VSIRHAVIGS
     NVVVYPGARI GQDGFGFASD AEGHYKIPHA GGVIIGNDVE IGANTCIDRG SLGNTVIEDW
     CRLDNLVQIG HNVKIGKGSI IVAQVGIAGS TELGEHVTLA GQVGVIGHLK IGKGATVLTC
     SKVLRNVQPG DRVIGYPAIS ISDWQKQIRF LKTAIKSKNP LKS