ID   LPXD2_LEGPH             Reviewed;         343 AA.
AC   Q5ZRD8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 98.
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=lpg2944;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU28990.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017354; AAU28990.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015443878.1; NC_002942.5.
DR   RefSeq; YP_096937.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZRD8; -.
DR   SMR; Q5ZRD8; -.
DR   STRING; 272624.lpg2944; -.
DR   PaxDb; Q5ZRD8; -.
DR   EnsemblBacteria; AAU28990; AAU28990; lpg2944.
DR   KEGG; lpn:lpg2944; -.
DR   PATRIC; fig|272624.6.peg.3144; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_6; -.
DR   BRENDA; 2.3.1.191; 2943.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000609; 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; 3.
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; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..343
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase 2"
FT                   /id="PRO_0000264392"
FT   ACT_SITE        251
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   343 AA;  36561 MW;  A05D0DF320BDF29D CRC64;
     MSNYQFTKPA GPFRLFELAK ISGATLYEGK GETFTVSGLA KLSEATSNDL VMLHQKKYVK
     ELKHTAARVC IIGPDYVKYA PDSMYLLVHP NPYKAFALIA QAFYPSEKPP GFIATSAMIE
     SSAIIGVDCF IAHGAYIGNQ VKIGNRCKIG VNTYIGDTVT IGDDCLIEDN VSIRHAVIGN
     NVVIYSGARI GQDGFGFASD ANGHYKIPHA GGVIIGNDVE IGANTCIDRG SLDNTVIEDW
     CRLDNLVQIG HNVKIGKGSV LVAQVGIAGS TELGEHVTLA GQVGVIGHLK IGKGATVLAS
     AKVYKNVKSG DRVGGHPAVS ISDWQKQIRF LKTAIKSKKS PKS