LPXD_CAUVN
ID LPXD_CAUVN Reviewed; 339 AA.
AC B8GWR3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=CCNA_01990;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL95455.1; -; Genomic_DNA.
DR RefSeq; WP_010919779.1; NC_011916.1.
DR RefSeq; YP_002517363.1; NC_011916.1.
DR AlphaFoldDB; B8GWR3; -.
DR SMR; B8GWR3; -.
DR PRIDE; B8GWR3; -.
DR EnsemblBacteria; ACL95455; ACL95455; CCNA_01990.
DR GeneID; 7333318; -.
DR KEGG; ccs:CCNA_01990; -.
DR PATRIC; fig|565050.3.peg.1949; -.
DR HOGENOM; CLU_049865_0_2_5; -.
DR OMA; QIQIAHN; -.
DR OrthoDB; 1602061at2; -.
DR PhylomeDB; B8GWR3; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001364; 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; 2.
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; Reference proteome; Repeat; Transferase.
FT CHAIN 1..339
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_1000190892"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 339 AA; 34330 MW; 51EFC03BAD3733DB CRC64;
MPDPRFFDSL GPALLSELAQ AGAATLADAA LGERVITHAA PLDASDAQAI TFFSDAKRKD
AAASTRAGAC FVRPEHQGFL PPTCAALVTG RPQAAWAAAA NRLHAPRRHE AGAPSLHPDA
ALEDGVALAP NVTIGQGASI GRGTRIGPGV VIGPGVVIGR YCRIGANAVI GFAMLGDNVA
ISAGAVIGEA GFGAALGPRG MVDLPQLGRV VIQDNVTLGA NSCVDRGAFG DTTIGENTKI
DNLVHVAHNV RIGRNCVLAA YTGVSGSTVV GDGVAFGGKA GVADHLNIGS GASIGAAASV
FKDVPDGETW TGFPARPLKR WLRETAWLSR MAGGRGTRG