ID   LPXD2_LEGPL             Reviewed;         343 AA.
AC   Q5WSK5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=lpl2873;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
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; CR628337; CAH17117.1; -; Genomic_DNA.
DR   RefSeq; WP_011216787.1; NC_006369.1.
DR   AlphaFoldDB; Q5WSK5; -.
DR   SMR; Q5WSK5; -.
DR   EnsemblBacteria; CAH17117; CAH17117; lpl2873.
DR   KEGG; lpf:lpl2873; -.
DR   LegioList; lpl2873; -.
DR   HOGENOM; CLU_049865_0_0_6; -.
DR   OMA; YKIPHAG; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002517; 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; 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.
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_0000264388"
FT   ACT_SITE        251
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   343 AA;  36231 MW;  43D0F3C7CAB8EBDB CRC64;
     MSNYQFTKPA GPFYLAELAE ISGSTLYEGK GEAFTVSGLA KLSEATTHNL VMLHQKKYLK
     ELKNTAARAC IIGPEYVKFA PDSMYLLVHP NPYKAFALIA QAFYPSEKPA GFIASSAAIE
     TSAVIGSNCY IAHGVYIGNN AKIGSGCQIG VNTYIGDGVT IGDDCLIEDN VSIRHAVIGK
     HVVIYPGARI GQDGFGFASD ASGHYKIPHA GGVIIGNHVE IGANTCIDRG SLDNTVIEDW
     CRLDNLVQVG HNVKIGKGSI IVAQVGIAGS TELGEYVTLA GQAGVIGHLK IGKGATVLAS
     GKVYKNVKSG DRVGGHPAVS ISDWQKQIRF LKTAIKPKKS PKS