LPXD_YERPS
ID LPXD_YERPS Reviewed; 340 AA.
AC Q667J9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
DE AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=YPTB2993;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as
CC the acyl donor. Is involved in the biosynthesis of lipid A, a
CC phosphorylated glycolipid that anchors the lipopolysaccharide to the
CC outer membrane of the cell. {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 -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-
CC 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
CC Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:71573,
CC ChEBI:CHEBI:78474, ChEBI:CHEBI:78847; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00523};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000255|HAMAP-
CC 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; BX936398; CAH22231.1; -; Genomic_DNA.
DR RefSeq; WP_002212141.1; NZ_CP009712.1.
DR AlphaFoldDB; Q667J9; -.
DR SMR; Q667J9; -.
DR EnsemblBacteria; CAH22231; CAH22231; YPTB2993.
DR GeneID; 66844578; -.
DR KEGG; ypo:BZ17_3628; -.
DR KEGG; yps:YPTB2993; -.
DR PATRIC; fig|273123.14.peg.3809; -.
DR OMA; QIQIAHN; -.
DR UniPathway; UPA00359; UER00479.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
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; 3.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Repeat; Transferase.
FT CHAIN 1..340
FT /note="UDP-3-O-(3-hydroxymyristoyl)glucosamine N-
FT acyltransferase"
FT /id="PRO_0000059718"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ SEQUENCE 340 AA; 35779 MW; BAC1F8C2DDEF4589 CRC64;
MPSIRLADLA QQLDAQVHGD GDLVITGIAS MHSAQPEQIT FLSNSRYREQ LASCNAGAVV
LTEADLPFCK VAALVVENPY FTYARMAQIM DTTPQPAQDI APSAVISPQA TLGEGVSVGA
NAVIESGVVL GDNVVIGAGC FIGKNTHIGA GSRLWANVSI YHEVVIGQNC LIQSGTVIGA
DGFGYANDRG NWVKIPQLGS VHIGDRVEIG ACTTIDRGAL DNTIIGNGVI IDNQCQIAHN
VVIGDNTAVA GGVIMAGSLK VGRYCMIGGA SVINGHMEIC DKVTITGMGM VMRPITEPGL
YSSGIPLQPN KMWRKTAALV MNIDGINKRL KAVERKIDKE
