ID   LPXD_CHLT2              Reviewed;         354 AA.
AC   B0B7F9; O84245; Q9S530;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=CTL0495;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10463174; DOI=10.1099/13500872-145-8-2077;
RA   Bannantine J.P., Rockey D.D.;
RT   "Use of primate model system to identify Chlamydia trachomatis protein
RT   antigens recognized uniquely in the context of infection.";
RL   Microbiology 145:2077-2085(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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; AF077009; AAC35947.1; -; Genomic_DNA.
DR   EMBL; AM884176; CAP03935.1; -; Genomic_DNA.
DR   RefSeq; WP_009873666.1; NC_010287.1.
DR   RefSeq; YP_001654572.1; NC_010287.1.
DR   AlphaFoldDB; B0B7F9; -.
DR   SMR; B0B7F9; -.
DR   EnsemblBacteria; CAP03935; CAP03935; CTL0495.
DR   KEGG; ctb:CTL0495; -.
DR   PATRIC; fig|471472.4.peg.533; -.
DR   HOGENOM; CLU_049865_0_0_0; -.
DR   OMA; QIQIAHN; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000795; 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..354
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_1000127669"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
FT   CONFLICT        2
FT                   /note="S -> C (in Ref. 1; AAC35947)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        7
FT                   /note="S -> F (in Ref. 1; AAC35947)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="G -> A (in Ref. 1; AAC35947)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  38403 MW;  7DD4084538E68E77 CRC64;
     MSQSTYSLEQ LADFLKVEFQ GNGATLLSGV EEIEEAKTAH ITFLDNEKYA KHLKSSEAGA
     IIISRTQFQK YRDLNKNFLI TSESPSLVFQ KCLELFITPV DSGFPGIHPT AVIHPTAIIE
     DHVCIEPYAV VCQHAHVGSA CHIGSGSVIG AYSTVGQHSY IHPRVVIRER VSIGKRVIIQ
     PGAVIGSCGF GYVTSAFGQH KHLKHLGKVI IEDDVEIGAN TTIDRGRFKH SVVREGSKID
     NLVQIAHQVE VGQHSMIVAQ AGIAGSTKIG NHVIIGGQAG ITGHICIADH VIMMAQTGVT
     KSITSPGIYG GAPARPYQEI HRQVAKVRNL PRLEERIAAL EKLVQKLEAL SEQH