ID   LPXD_NEIMB              Reviewed;         348 AA.
AC   P95377; Q9K1H2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   25-MAY-2022, entry version 118.
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=NMB0180;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=9197543; DOI=10.1016/s0378-1119(97)00005-x;
RA   Steeghs L., Jennings M.P., Poolman J.T., Der Ley P.;
RT   "Isolation and characterization of the Neisseria meningitidis lpxD-fabZ-
RT   lpxA gene cluster involved in lipid A biosynthesis.";
RL   Gene 190:263-270(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; U79481; AAC45422.1; -; Genomic_DNA.
DR   EMBL; AE002098; AAF40637.1; -; Genomic_DNA.
DR   PIR; E81228; E81228.
DR   RefSeq; NP_273238.1; NC_003112.2.
DR   RefSeq; WP_002243946.1; NC_003112.2.
DR   AlphaFoldDB; P95377; -.
DR   SMR; P95377; -.
DR   STRING; 122586.NMB0180; -.
DR   PaxDb; P95377; -.
DR   EnsemblBacteria; AAF40637; AAF40637; NMB0180.
DR   KEGG; nme:NMB0180; -.
DR   PATRIC; fig|122586.8.peg.222; -.
DR   HOGENOM; CLU_049865_0_1_4; -.
DR   OMA; QIQIAHN; -.
DR   BRENDA; 2.3.1.191; 3593.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000425; 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; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..348
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT                   /id="PRO_0000059684"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
FT   CONFLICT        1..3
FT                   /note="MIP -> VAV (in Ref. 2; AAC45422)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  36449 MW;  F555038EEAE229A8 CRC64;
     MIPATYTLSQ ITARLGGEWR GEDISVTAVR PLADAQAEHI SFLANPKYKA EVHDSSAGAV
     IVSAKAADGF EGRNLIVADD PYLYFAKVAR LFSPVVKARG GIHPTAVVEP GATVPTSCEI
     GANVYIGANT VLGEGCRILA NAVVQHDCKL GDEVVLHPNA VVYYGCTLGR RVEIHSGAVI
     GADGFGLAFA DDSWFKIPQT GAVTLGDDVE IGSNTNIDRG AMSDTTVGNG TKIDNQVQIG
     HNCKIGSHTV IAAKTGISGS VTIGSYCIIG GGVGTVGHIE IADKTTIGGG TSVTHSITES
     GKHLAGIFPM STHKEWARNA VYIHRLSEMN KRLKTLEQQL SDAGQDSK