ID   LPXD_SALCH              Reviewed;         341 AA.
AC   Q57T29;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
DE   AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=SCH_0226;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC       (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as
CC       the acyl donor. Is involved in the biosynthesis of lipid A, a
CC       phosphorylated glycolipid that anchors the lipopolysaccharide to the
CC       outer membrane of the cell. {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-
CC         2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:71573,
CC         ChEBI:CHEBI:78474, ChEBI:CHEBI:78847; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00523};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000255|HAMAP-
CC       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; AE017220; AAX64132.1; -; Genomic_DNA.
DR   RefSeq; WP_001539055.1; NC_006905.1.
DR   AlphaFoldDB; Q57T29; -.
DR   SMR; Q57T29; -.
DR   EnsemblBacteria; AAX64132; AAX64132; SCH_0226.
DR   KEGG; sec:SCH_0226; -.
DR   HOGENOM; CLU_049865_0_1_6; -.
DR   OMA; QIQIAHN; -.
DR   UniPathway; UPA00359; UER00479.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
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; 4.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Repeat; Transferase.
FT   CHAIN           1..341
FT                   /note="UDP-3-O-(3-hydroxymyristoyl)glucosamine N-
FT                   acyltransferase"
FT                   /id="PRO_0000264432"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   341 AA;  35903 MW;  4A8383BCF9C8C86E CRC64;
     MPSIRLADLA EQLDAELHGD GDIVITGVAS MQSATTGHIT FMVNPKYREH LGLCQASAVV
     MTQDDLPFAK SAALVVKNPY LTYARMAQIL DTTPQPAQNI APSAVIDATA TLGSNVSVGA
     NAVIESGVQL GDNVVIGAGC FVGKNSKIGA GSRLWANVTI YHDIQIGENC LIQSSTVIGA
     DGFGYANDRG NWVKIPQLGR VIIGDRVEIG ACTTIDRGAL DDTVIGNGVI IDNQCQIAHN
     VVIGDNTAVA GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV
     YSSGIPLQPN KVWRKTAALV MNIDDMSKRL KAIERTVNQQ D