LPXD_BARHE
ID LPXD_BARHE Reviewed; 348 AA.
AC Q8VQ23;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=BH06290;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zimmermann R., Augustin K., Schaal K., Sander A.;
RT "Cloning, nucleotide sequencing, and expression of a hemin-binding protein
RT of Bartonella henselae.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; AF461795; AAL66375.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF27433.1; -; Genomic_DNA.
DR RefSeq; WP_011180553.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q8VQ23; -.
DR SMR; Q8VQ23; -.
DR STRING; 283166.BH06290; -.
DR PaxDb; Q8VQ23; -.
DR PRIDE; Q8VQ23; -.
DR DNASU; 2865601; -.
DR EnsemblBacteria; CAF27433; CAF27433; BH06290.
DR GeneID; 64156908; -.
DR KEGG; bhe:BH06290; -.
DR eggNOG; COG1044; Bacteria.
DR OMA; QIQIAHN; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000421; 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; 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; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Repeat; Transferase.
FT CHAIN 1..348
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000059646"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 348 AA; 36836 MW; 7E8C57BA9ED50749 CRC64;
MADTFFFTPS RRLTVANVAE LTGAKLLNPE FSNTVINTLS SLESAGKGSL VFVEHRKFSD
ALVGSSAVAV FCTNEIVFKV PESMAILVTS TPQRDFAQIG RILFPDSVKP MPWFGQREIS
PHAHIHPSAK LAGDVCIEAG AVIGRNVEIG SGSLIASTAV IGENCRIGCD CYIAPKVTVQ
YSLIGDKVHL YPGACIGQDG FGYIGGASGI EKVPQLGRVI IEDGVEIGAN TTIDRGTFED
TIIGEGSKID NLVQIAHNVK IGRYCLIAAQ CGIAGSTSIG DMSQLGGSVG VADHIVIGKY
VQIAAGSGVM NDIPDGEKWG GSPARPFKQW FREVAALRSI GKVKKEKR