ID   LPXD_CAMC1              Reviewed;         317 AA.
AC   A7ZD79;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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};
GN   OrderedLocusNames=Ccon26_08690; ORFNames=CCC13826_0138;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000792; EAT97514.1; -; Genomic_DNA.
DR   RefSeq; WP_012001678.1; NC_009802.2.
DR   AlphaFoldDB; A7ZD79; -.
DR   SMR; A7ZD79; -.
DR   STRING; 360104.CCC13826_0138; -.
DR   PRIDE; A7ZD79; -.
DR   EnsemblBacteria; EAT97514; EAT97514; CCC13826_0138.
DR   KEGG; cco:CCC13826_0138; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_1_7; -.
DR   OMA; QIQIAHN; -.
DR   OrthoDB; 1602061at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001121; 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; 4.
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..317
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_1000050937"
FT   ACT_SITE        229
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   317 AA;  33585 MW;  A8457B43FE67D035 CRC64;
     MKLSEIALKV DATFSGEDLE IFALNSLKNA NKAELTYCDG EKNAKFISTS NAGAILVTKS
     LLDLVPAGMV ALVCDNPHLA FAILSKIYAK PLFCEPKPSN IAQSATIMPN VYIGSNVSVG
     ENTIVMAGAF LGDNVTIGKN CIIHPNVVIY NDCVIGNECH LLANCVIGSD GFGYAHTKTG
     EHVKIYHNGN VVLGDFVEIG ACTTIDRGVF ESTMIANYTK IDNLVQIGHN CELGNGCLIV
     SQTGLAGSTV LGRNVVMGGQ SGSAGHVKVG DFAQIAARGG VSKDLPGGKK YAGAYPIMEL
     SEQFKFQAKI LRFFKKN