LPXD_RICBR
ID LPXD_RICBR Reviewed; 342 AA.
AC Q1RH94;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=RBE_1189;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05270.1; -; Genomic_DNA.
DR RefSeq; WP_011477848.1; NC_007940.1.
DR AlphaFoldDB; Q1RH94; -.
DR SMR; Q1RH94; -.
DR STRING; 336407.RBE_1189; -.
DR EnsemblBacteria; ABE05270; ABE05270; RBE_1189.
DR KEGG; rbe:RBE_1189; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_0_5; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001951; 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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Repeat; Transferase.
FT CHAIN 1..342
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000264429"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 342 AA; 36599 MW; 6F84A6093DA28FF9 CRC64;
MVNSNFYRNL GPRKLMAIAD FLQDFIEAPK IHEDVAIHDI KILQEASSND ISFLSNIKYS
RFLKNTKAAA CIVPKDFTGE VNPNTVLLRA ENSYFAYGKL IDFFYAPVKS YPAKIMKSAY
VAESATIGKN CYVGHNAVIE DNVVIGDDSI IEAGSFIGTG VVIGRNARIE SNVSINYSVI
GDDVVILSGA KIGQDGFGFS TEKGMHHKIF HTGIVKIGNN VEIGANTTID RGSLQDTIIE
DLCRIDNLVQ IGHSVKIGKG SIIVAQAGIA GSSVIGKYCA LGGQVGVAGH LYIGDGAQVA
AQGGVAQNIE AGKIVGGSPA VPIMDWHRQS IIMKQLINKR SK