ID   LPXB_COXB2              Reviewed;         376 AA.
AC   B6J161;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE            EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN   Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; OrderedLocusNames=CbuG_1383;
OS   Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CbuG_Q212;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
CC   -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC       diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor
CC       of lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine = a lipid A disaccharide + H(+) + UDP;
CC         Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343;
CC         EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
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DR   EMBL; CP001019; ACJ18689.1; -; Genomic_DNA.
DR   RefSeq; WP_012570233.1; NC_011527.1.
DR   AlphaFoldDB; B6J161; -.
DR   SMR; B6J161; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; cbg:CbuG_1383; -.
DR   HOGENOM; CLU_036577_3_1_6; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   TIGRFAMs; TIGR00215; lpxB; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..376
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000191470"
SQ   SEQUENCE   376 AA;  41943 MW;  6D11A61B53A59CFE CRC64;
     MSNKSVLLIA GEPSGDLLGA HLAQSLKSLE PNLKLAGMGG KRMREAGVEV FINADKLAVV
     GLLEILRQFR DIRHAMQTLK RYFKKTPPDL VVFIDYPGFN LHMAKQAKKA GIKVLYYVSP
     QIWAWRYGRI KKIKKYVDHM AVLFDFEEKL YQKENVPVSF VGHPLANAPT PSLSRNEICK
     QFNLDPDKPI VALFPGSREQ EINKLLPMMV QAGKLIQTQI PTVQFILPLA LNLALDKIRP
     FLSPEIKVIQ NDISHVLAIA HAAVAASGTV TLEIALQQVP LVIIYKVAPL TFWLGKKLIR
     LSFIGLCNLV SPEPVAVELL QQDATPQAIA DEVFQLLNNH NYRQSIIGKL GHLRPQLDRG
     NAAQNVAKVI HNLIFS