ID   LPXD_CHLAB              Reviewed;         359 AA.
AC   Q5L612;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=CAB466;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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; CR848038; CAH63919.1; -; Genomic_DNA.
DR   RefSeq; WP_011097096.1; NC_004552.2.
DR   AlphaFoldDB; Q5L612; -.
DR   SMR; Q5L612; -.
DR   EnsemblBacteria; CAH63919; CAH63919; CAB466.
DR   KEGG; cab:CAB466; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_0; -.
DR   OMA; QIQIAHN; -.
DR   OrthoDB; 1602061at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001012; 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; 3.
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..359
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000264357"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   359 AA;  38764 MW;  92A94CDEAEAC9BF7 CRC64;
     MPQELVYTLQ QLADLLKVEV QGNTETPISG VEEISAAKAH HVTFLDNEKY ARFIKITEAG
     AIILSKAQAQ KYGHLNKNFL IVSEFPSIAF QKCIELFISP VDSGFPGIHP TAVIHPTASI
     GKDVCIEPYA VICQHACIGD STYIGTGSVI GAYSTLGEHC LVHPKVVVRE RVEIGKRVII
     QPGAVIGSCG FGYITNAFGR HKHLKHLGKV IIEDDVEIGA NTTIDRGRFK NSVIREGTKI
     DNQVQIAHHV EVGKHSMIVA QAGIAGSTKI GNHVIIGGQT GITGHISITD HVIMMAQTGV
     TKSISSPGIY GGAPARPYQE IHRQVAKIRS LPKLEERLGM LEEKVKGLSA QSTELQITP